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Pectinase Industries

Pectinase Research Institutes




BAC 'landing' on chromosomes of Brachypodium distachyon for comparative genome alignment

Glyn Jenkins, Robert Hasterok

SUMMARY: Fluorescence in situ hybridization (FISH) using bacterial artificial chromosomes (BACs) with large genomic DNA inserts as probes (BAC 'landing') is a powerful means by

CONTEXT: ...kit (Roche, cat. no. 1 976 776 910) Nonfat dry milk blocking agent; see REAGENT SETUP PBS; see REAGENT SETUP Pectinase (Sigma, cat. no. P-0690); see REAGENT SETUP Pectolyase (Sigma, cat. no. P-3026); seeREAGENT SETUP DNase-free RNase...

Nature Protocols 2, 88 - 98 (01 Feb 2007)

2. The genome of an industrial workhorse

Dan Cullen

SUMMARY: Sequencing of the filamentous fungus Aspergillus niger offers new opportunities for the production of specialty chemicals and enzymes.

CONTEXT: ...of a saprophyte often isolated from soils and decaying vegetation, an array of cellulase-, xylanase-, amylase- and pectinase-encoding genes were identified. Compared with related Aspergilli, few pectate lyase genes were predicted,...

Nature Biotechnology 25, 189 - 190 (01 Feb 2007) News and Views

3. Fusion PCR and gene targeting in Aspergillus nidulans

Edyta Szewczyk, Tania Nayak, C Elizabeth Oakley, Heather Edgerton, Yi Xiong, Naimeh Taheri-Talesh, Stephen A Osmani, Berl R Oakley

SUMMARY: We describe a rapid method for the production of fusion PCR products that can be used, generally without band purification, to transform Aspergillus nidulans.

CONTEXT: purchased from Guzmer Enterprises ( It has pectinase and 1,3-1,6 glucanase activity. Novo Nordisk makes a number of enzymes with similar names so be careful to obtain...

Nature Protocols 1, 3111 - 3120 (01 Jan 2007)

4. Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72

Andrea Krause, Adarsh Ramakumar, Daniela Bartels, Federico Battistoni, Thomas Bekel, Jens Boch, Melanie Böhm, Frauke Friedrich, Thomas Hurek, Lutz Krause, Burkhard Linke, Alice C McHardy, Abhijit Sarkar, Susanne Schneiker, Arshad Ali Syed, Rudolf Thauer, Frank-Jörg Vorhölter, Stefan Weidner, Alfred Pühler, Barbara Reinhold-Hurek, Olaf Kaiser, Alexander Goesmann

SUMMARY: Azoarcus sp. strain BH72, a mutualistic endophyte of rice and other grasses, is of agrobiotechnological interest because it supplies biologically fixed nitrogen to its

CONTEXT: ...macerate plant cell wall polymers and thus contribute to a phytopathogenic lifestyle and plant damage are rare: pectinase-encoding genes are absent; only a few genes encode putative glycosidases (palZ, spr1, ndvC, eglA), some of them...

Nature Biotechnology 24, 1385 - 1391 (01 Nov 2006) Research

5. Cytogenetic comparisons between A and G genomes in Oryza using genomic in situ hybridization

Zhi Yong Xiong, Guang Xuan Tan, Guang Yuan He, Guang Cun He, Yun Chun Song

SUMMARY: The genomic structures of Oryza sativa (A genome) and O. meyeriana (G genome) were comparatively studied using bicolor genomic in situ hybridization (GISH). GISH

CONTEXT: ...acid (3:1) at 4 °C overnight. After washing with distilled water, the root tips were treated with a mixture of 2% pectinase (SERVA) and 2% cellulase (SERVA) at 28 °C for 3 h before squashing on slides and drying in a flame 24. For...

Cell Research 16, 260 - 266 (01 Mar 2006) Original Article

Composite Films from Pectin and Fish Skin Gelatin or Soybean Flour Protein

LinShu Liu,* Cheng-Kung Liu, Marshall L. Fishman, and Kevin B. Hicks

J. Agric. Food Chem., 55 (6), 2349 -2355, 2007. 10.1021/jf062612u S0021-8561(06)02612-4
Web Release Date: February 21, 2007

Crop Conversion Science and Engineering Research Unit and Fats, Oils and Animal Co-products Research Unit, Eastern Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture, 600 East Mermaid Lane, Wyndmoor, Pennsylvania 19038

Received for review September 11, 2006. Revised manuscript received December 8, 2006. Accepted January 4, 2007. Mention of trade names or commercial products in this article is solely for providing specific information and does not imply recommendation or endorsement by the U.S. Department of Agriculture.


Composite films were prepared from pectin and fish skin gelatin (FSG) or pectin and soybean flour protein (SFP). The inclusion of protein promoted molecular interactions, resulting in a well-organized homogeneous structure, as revealed by scanning electron microscopy and fracture-acoustic emission analysis. The resultant composite films showed an increase in stiffness and strength and a decrease in water solubility and water vapor transmission rate, in comparison with films cast from pectin alone. The composite films inherited the elastic nature of proteins, thus being more flexible than the pure pectin films. Treating the composite films with glutaraldehyde/methanol induced chemical cross-linking with the proteins and reduced the interstitial spaces among the macromolecules and, consequently, improved their mechanical properties and water resistance. Treating the protein-free pectin films with glutaraldehyde/methanol also improved the Young's modulus and tensile strength, but showed little effect on the water resistance, because the treatment caused only dehydration of the pectin films and the dehydration is reversible. The composite films were biodegradable and possessed moderate mechanical properties and a low water vapor transmission rate. Therefore, the films are considered to have potential applications as packaging or coating materials for food or drug industries.

Composition and Rheological Properties of -Lactoglobulin/Pectin Coacervates: Effects of Salt Concentration and Initial Protein/Polysaccharide Ratio

Xiaoyong Wang, Jooyoung Lee, Yu-Wen Wang, and Qingrong Huang*

Biomacromolecules, 8 (3), 992 -997, 2007. 10.1021/bm060902d S1525-7797(06)00902-0
Web Release Date: February 17, 2007

Department of Food Science, Rutgers University, 65 Dudley Road, New Brunswick, New Jersey 08901

Received September 21, 2006

Revised December 11, 2006


The composition and rheological properties of -lactoglobulin/pectin coacervates have shown significant correlations with sodium chloride concentration (CNaCl) and initial protein/polysaccharide ratio (r). An increase of CNaCl from 0.01 to 0.21 M at r = 5:1 leads to the increase in both -lactoglobulin and pectin contents in the coacervates, which can be explained in terms of salt-enhanced effect at lower salt concentrations. Further increase of CNaCl from 0.21 to 0.41 M decreases the proportions of these two biopolymers in the coacervates, exhibiting salt-reduced effect at higher salt concentrations. Moreover, the stronger self-aggregation of -lactoglobulin with increasing salt concentration gives rise to a decreasing actual protein/polysaccharide ratio in the coacervates at 0.01-0.21 M CNaCl and r = 5:1. An increase of r from 5:1 to 40:1 often increases the actual amount of pectin chains in -lactoglobulin/pectin coacervates, but it exhibits a maximum in -lactoglobulin content at r = 20:1. A much higher storage modulus (G') than loss modulus (G' ') for all -lactoglobulin/pectin coacervates suggests the formation of highly interconnected gel-like structure. The values of G' increase as CNaCl increases from 0.01 to 0.21 M, whereas a further increase of CNaCl from 0.21 to 0.41 M causes G' values to decrease to much lower values. These results further disclose the salt-enhanced effect and the salt-reduced effect at low and high salt concentrations, respectively. On the other hand, increasing r from 5:1 to 40:1 favors the formation of stronger gel-like -lactoglobulin/pectin coacervates, which mainly originates from the higher actual amount of pectin chains in -lactoglobulin/pectin coacervates at higher r values.

Impact of Electrostatic Interactions on Formation and Stability of Emulsions Containing Oil Droplets Coated by -Lactoglobulin-Pectin Complexes

Demet Guzey and David Julian McClements*

Biopolymers and Colloids Laboratory, Department of Food Science, University of Massachusetts, Amherst, Massachusetts 01003

J. Agric. Food Chem., 55 (2), 475 -485, 2007. 10.1021/jf062342f S0021-8561(06)02342-9
Web Release Date: December 19, 2006

Received for review August 14, 2006. Revised manuscript received November 6, 2006. Accepted November 14, 2006. This material is based upon work supported by the Cooperative State Research, Extension, Education Service, U.S. Department of Agriculture, Massachusetts Agricultural Experiment Station (Project 831), by an U.S. Department of Agriculture, CREES, IFAFS Grant (Award 2001-4526), and by an U.S. Department of Agriculture, CREES, NRI Grant (Award 2005-01357).


Interfacial protein-polysaccharide complexes can be used to improve the physical stability of oil-in-water emulsions. The purpose of this study was to examine the impact of ionic strength on the formation and stability of oil-in-water emulsions containing polysaccharide-protein-coated droplets. Emulsions were prepared that contained 0.1 wt % corn oil, 0.05 wt % -lactoglobulin, and 0.02 wt % pectin at pH 7. The emulsions were then adjusted to pH 4 to promote electrostatic deposition of the pectin molecules onto the surfaces of the protein-coated droplets. The salt concentration of the aqueous phase (0 or 50 mM NaCl) was adjusted either before or after deposition of the pectin molecules onto the droplet surfaces. We found that stable emulsions containing polysaccharide-protein-coated droplets could be formed when the salt was added after pectin adsorption but not when it was added before pectin adsorption. This phenomenon was attributed to the ability of NaCl to promote droplet flocculation in the protein-coated droplets so that the pectin molecules adsorbed onto the surfaces of flocs rather than individual droplets when salt was added before pectin adsorption. We also found that polysaccharide-protein-coated droplets had a much improved stability to salt-induced flocculation than protein-coated droplets with the same droplet charge (-potential). Theoretical predictions indicated that this was due to the ability of the adsorbed polysaccharide layer to strongly diminish the van der Waals attraction between the droplets.

Microstructure of -Lactoglobulin/Pectin Coacervates Studied by Small-Angle Neutron Scattering

Xiaoyong Wang, Yunqi Li, Yu-Wen Wang, Jyotsana Lal, and Qingrong Huang*

Department of Food Science, Rutgers University, 65 Dudley Road, New Brunswick, New Jersey 08901, State Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, P. R. China, and Intense Pulsed Neutron Source Division, Argonne National Laboratory, Argonne, Illinois 60439

J. Phys. Chem. B, 111 (3), 515 -520, 2007. 10.1021/jp0632891 S1520-6106(06)03289-5
Web Release Date: December 23, 2006

Received: May 29, 2006

In Final Form: October 31, 2006


Small-angle neutron scattering (SANS) has been used to investigate the microstructure of -lactoglobulin/pectin coacervates prepared by different initial protein/polysaccharide weight ratio (r), sodium chloride concentration (CNaCl), and pectin charge density. The higher r and higher pectin charge density lead to higher scattering intensity at small q range (0.007 -1 < q < 0.02 -1), suggesting that the charges of pectin chains are screened significantly by the binding of oppositely charged protein molecules, leading to a tighter aggregation of pectin chains. On the other hand, the appearance of a shoulder peak at intermediate q range (0.04 -1 < q < 0.2 -1) is used to interpret the formation of protein domains in -lactoglobulin/pectin coacervates. At CNaCl = 0.1 M, the coacervate of -lactoglobulin and pectin A does not show a shoulder peak at intermediate q range at r = 10:1, suggesting that protein molecules are separately bound on pectin chains. However, a shoulder peak appears at intermediate q range at r = 20:1 and 30:1, and the average protein domain size estimated from the shoulder peak position is 7.2 and 8.5 nm, respectively, for these two coacervates. When CNaCl increases from 0.05 to 0.2 M, the shoulder peak shifts toward smaller q and becomes broader, indicating that the addition of a higher amount of salt leads to a more heterogeneous coacervate structure. Pectin B with a lower linear charge density favors the formation of larger protein domains. The formation of protein domains in -lactoglobulin/pectin coacervates is partially ascribed to the self-aggregation of -lactoglobulin molecules. Two kinds of microstructures of -lactoglobulin/pectin coacervates with and without observable protein domains have been proposed.

Structural Features and Complement-Fixing Activity of Pectin from Three Brassica oleracea Varieties: White Cabbage, Kale, and Red Kale

Anne Berit Samuelsen,* Bjrge Westereng, Osman Yousif, Ann Katrin Holtekjlen, Terje E. Michaelsen, and Svein H. Knutsen

School of Pharmacy, Department of Pharmaceutical Chemistry, Pharmacognosy, P.O. Box 1068 Blindern, N-0316 Oslo, Norway, MATFORSK, The Norwegian Food Research Institute, Osloveien 1, N-1430 s, Norway, and The Norwegian Institue of Public Health, P.O. Box 4404 Nydalen, N-0403 Oslo, Norway

Biomacromolecules, 8 (2), 644 -649, 2007. 10.1021/bm060896l S1525-7797(06)00896-8
Web Release Date: January 25, 2007

Received September 20, 2006

Revised November 7, 2006


Leaves of different cabbage species are used both as food and as wound healing remedies in traditional medicine. This supposed wound healing activity might be connected to presence of immunomodulating water soluble polysaccharides. To study this, three different cabbage varieties, white cabbage (W), kale (K), and red kale (RK), were pretreated with 80% ethanol and then extracted with water at 50 C and 100 C for isolation of polysaccharide-containing fractions. The fractions were analyzed for monosaccharide composition, glycosidic linkages, Mw distribution, protein content, and phenolic compounds and then tested for complement-fixing activity. All fractions contained pectin type polysaccharides with linkages corresponding to homogalacturonan and hairy regions. Those extracted at 50 C contained higher amounts of neutral side chains and were more active in the complement-fixation test than those extracted at 100 C. The fractions can be ranged by decreasing activity: K-50 > RK-50 > W-50 K-100 > RK100 W-100. Studies on structure-activity relationships (SAR) employing multivariate statistical analysis strongly suggest that the magnitude of the measured activity is influenced by the content of certain side chains in the polymers. High activity correlates to large neutral side chains with high amounts of (16)- and (13,6)-linked Gal and low amounts of (14)-linked GalA but not on molecular weight distribution of the polymers.

Effect of Modified Pectin Molecules on the Growth of Bone Cells

Hanna E. Kokkonen,* Joanna M. Ilvesaro, Marco Morra, Henk A. Schols, and Juha Tuukkanen

Department of Anatomy and Cell Biology, University of Oulu, Oulu, Finland, Division of Hematology/Oncology, Department of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294, Nobil Bio Ricerche, Villafranca d'Asti, Italy, and Laboratory of Food Chemistry, Wageningen University, Bomenweg 2, 6703HD Wageningen, The Netherlands

Biomacromolecules, 8 (2), 509 -515, 2007. 10.1021/bm060614h S1525-7797(06)00614-3
Web Release Date: December 16, 2006

Received June 28, 2006

Revised October 13, 2006


The aim of this study was to investigate molecular candidates for bone implant nanocoatings, which could improve biocompatibility of implant materials. Primary rat bone cells and murine preosteoblastic MC3T3-E1 cells were cultured on enzymatically modified hairy regions (MHR-A and MHR-B) of apple pectins. MHRs were covalently attached to tissue culture polystyrene (TCPS) or glass. Uncoated substrata or bone slices were used as controls. Cell attachment, proliferation, and differentiation were investigated with fluorescence and confocal microscopy. Bone cells seem to prefer MHR-B coating to MHR-A coating. On MHR-A samples, the overall numbers as well as proportions of active osteoclasts were diminished compared to those on MHR-B, TCPS, or bone. Focal adhesions indicating attachment of the osteoblastic cells were detected on MHR-B and uncoated controls but not on MHR-A. These results demonstrate the possibility to modify surfaces with pectin nanocoatings.

Extraction and Characterization of Foeniculum vulgare Pectins and Their Use for Preparing Biopolymer Films in the Presence of Phaseolin Protein

Concetta V. L. Giosafatto, Loredana Mariniello,* and Steve Ring

Department of Food Science, University of Naples "Federico II", Parco Gussone, 80055 Portici, Naples, Italy, and Institute of Food Research, Norwich Research Park, Colney, Norwich NR47UA, United Kingdom

J. Agric. Food Chem., 55 (4), 1237 -1240, 2007. 10.1021/jf062725d S0021-8561(06)02725-7
Web Release Date: January 30, 2007

Received for review September 22, 2006. Revised manuscript received December 6, 2006. Accepted December 14, 2006. We thank the EC Commission for the award of a Marie Curie fellowship to C.V.L.G.


Pectins from Foeniculum vulgare were extracted under acidic conditions. The obtained pectins were mainly composed of uronic acid but also contained traces of rhamnose, galactose, and arabinose. Extracted pectins were used as a carbohydrate source to prepare biopolymer films in the absence and in the presence of phaseolin protein. The swelling characteristics of the films were examined as a function of ionic strength, pH, and the applied osmotic stress. The swelling behavior was dominated by a Donnan-type effect, which decreases with increasing ionic strength and counterion valency. In all cases the swelling of films containing phaseolin was reduced, suggesting a network formation between protein and pectins. Mechanical property studies have also estimated the validity of the obtained novel biopolymer films in terms of mechanical resistance.

Separation and Utilization of Pectin Lyase from Commercial Pectic Enzyme via Highly Methoxylated Cross-Linked Alcohol-Insoluble Solid Chromatography for Wine Methanol Reduction

Ming-Chang Wu, Chii-Ming Jiang, Ping-Hsiu Huang, Mei-Yi Wu, and Yuh Tai Wang*

Deptartment of Food Science, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan, Department of Sea Food Science, National Kaohsiung Marine University, Kaohsiung 811, Taiwan, and Life Science Center, Hsing Wu College, Number 101, Section 1, Fen-Liao Road, Lin-Kou, Taipei 244, Taiwan

J. Agric. Food Chem., 55 (4), 1557 -1562, 2007. 10.1021/jf062880s S0021-8561(06)02880-9
Web Release Date: January 31, 2007

Received for review October 6, 2006. Revised manuscript received December 10, 2006. Accepted January 1, 2007.


The isolation and utilization of pectin lyase (PL) from commercial pectic enzyme for methanol reduction in wine production was investigated. PL can be separated from pectinesterase (PE) and polygalacturonase (PG) on HM-CL-AIS affinity chromatography at pH 4; however, it is difficult to further distinguish PE from PG. Some desirable physicochemical properties such as transmittance, lightness, redness, and lower total pectin content are found in the external enzyme adding groups (PL, PE and PG, and pectic enzyme groups) in comparison to the control group. Methanol contents in pectic enzyme and the PE and PG groups increase from 628 13 (control group) to 3103 16 and 1736 67 mg/L ethanol in the final products, respectively. Nevertheless, the adding of PL does not cause any increase in methanol content. The results present in this study suggest that the HM-CL-AIS column is a simple, inexpensive, convenient, and effective method for PL purification. Moreover, the partial purified PL is a potential replacement of commercial pectic enzyme for pectin depolymerizing, methanol content reducing, and wine quality improving in wine production.

List of Most Recent Abstracts (Elsevier Publications)

Purification and mechanistic characterisation of two polygalacturonases from Sclerotium rolfsii Enzyme and Microbial TechnologyVolume 40, Issue 71 June 2007Pages 1739-1747
W. Schnitzhofer, H.-J. Weber, M. Vransk, P. Biely, A. Cavaco-Paulo and G.M. Guebitz
Sclerotium rolfsii (strain CBS 350.80) was found to produce extraordinary high amounts of polygalacturonases (PGs). Two of these extracellular enzymes were purified by a recently introduced preparative electrophoretic device (isoelectric focusing mode of free flow electrophoresis). PG 1 (39.5 kDa, pI 6.5) and PG 2 (38 kDa, pI 5.4) exhibited quite similar properties, they were found to be both endo-acting enzymes. Both PGs cleaved penta- and trigalacturonic acid while tetragalacturonic acid was only cleaved when trigalacturonic acid was present. The latter substrate was hydrolysed much faster by PG 2. Both enzymes were active on pectins with different degrees of esterification, they were sensitive towards Ca-cations and not glycosylated. The kinetic properties were measured by viscosimetry with polygalacturonic acid as a substrate. NMR experiments on a model substrate revealed an inverting mechanism of carbohydrate hydrolysis for both enzymes.
Combined Magnetic and Chemical Covalent Immobilization of Pectinase on Composites Membranes Improves Stability and Activity
Food Chemistry
In Press, Accepted ManuscriptAvailable online 5 May 2007
Zhongli Lei, Shuxian Bi, Bing Hu and Hong Yang
Optimizing bioscouring condition of cotton knitted fabrics with an alkaline pectinase from Bacillus subtilis WSHB04-02 by using response surface methodology
Biochemical Engineering JournalVolume 34, Issue 2May 2007Pages 107-113
Qiang Wang, Xue-Rong Fan, Zhao-Zhe Hua and Jian Chen
This present study was undertaken to find optimum conditions of pH, temperature, incubation time and enzyme concentration for bioscouring of cotton knitted fabrics with an alkaline pectinase isolated from Bacillus subtilis WSHB04-02 by use of response surface methodology (RSM). A central composite design was used as an experimental design for the analysis of the allocation of treatment combination. A second-order polynomial regression model was fitted and was found adequate with a determination coefficient R2 of 0.9844 (P < 0.001). The effect of pH was the most significant factor influencing cotton bioscouring and no significant interactions between different factors were found. Estimated optimum parameters were as follows: pH 9.1, temperature 57 C, incubation time 1.25 h and pectinase concentration 1.0 g/l. Under these conditions, a desired pectin removal percentage companied with adequate wettability was reached. In addition, a boiling water pretreatment of 30 min before enzymatic scouring was found to be useful for subsequent pectinase degradation due to the improvement of the accessibility of pectinase to the pectins in cotton fibers.

Hydrolysis of grapefruit peel waste with cellulase and pectinase enzymes
Bioresource TechnologyVolume 98, Issue 8May 2007Pages 1596-1601
Mark R. Wilkins, Wilbur W. Widmer, Karel Grohmann and Randall G. Cameron

Approximately 1 million metric tons of grapefruit were processed in the 2003/04 season resulting in 500,000 metric tons of peel waste. Grapefruit peel waste is usually dried, pelletized, and sold as a low-value cattle feed. This study tested different loadings of commercial cellulase and pectinase enzymes and pH levels to hydrolyze grapefruit peel waste to produce sugars. Pectinase and cellulase loadings of 0, 1, 2, 5, and 10 mg protein/g peel dry matter were tested at 45 C. Hydrolyses were supplemented with 2.1 mg beta-glucosidase protein/g peel dry matter. Five mg pectinase/g peel dry matter and 2 mg cellulase/g peel dry matter were the lowest loadings to yield the most glucose. Optimum pH was 4.8. Cellulose, pectin, and hemicellulose in grapefruit peel waste can be hydrolyzed by pectinase and cellulase enzymes to monomer sugars, which can then be used by microorganisms to produce ethanol and other fermentation products.

Loss of rutin and antioxidant activity of asparagus juice caused by a pectolytic enzyme preparation from Aspergillus niger
Food Chemistry
In Press, Corrected ProofAvailable online 9 April 2007
Ting Sun, Joseph R. Powers and Juming Tang

We found that a commercial pectolytic enzyme preparation from Aspergillus niger (pectinase AN) contained laccase activity that decreased rutin content and antioxidant activity of asparagus juice. This research investigated the effects of pH, temperature, and concentration of pectinase AN on pectinase ANs laccase activity to decrease rutin content and antioxidant activity of asparagus juice. Asparagus juice was incubated with pectinase AN at different pHs (3.2, 4.5 and 5.8), temperatures (25, 37, and 50 C) and enzyme concentrations (0.1%, 0.5% and 1%). Rutin content and antioxidant activity of samples was determined by HPLC and 2,2′-diphenyl-1-picrylhydrazyl (DPPH) free radical method, respectively. The rate of loss of rutin and antioxidant activity of asparagus juice was smaller at pH 3.2 than at pH 4.5 and pH 5.8, smaller for 0.1% pectinase AN than 0.5% and 1% pectinase AN. The rate of loss of rutin of asparagus juice was greater at 25 C than at the other two temperatures. Pectinase AN can decrease rutin content and antioxidant activity of asparagus juice at the selected conditions. But rutin content and antioxidant activity of asparagus juice produced using pectinase AN could be less decreased at pH 3.2 and 0.1% of enzyme with less than 2 h of incubation time. This information was helpful for juice industry to produce juices with high antioxidant activity using pectinase AN.

Optimization of biomass, pellet size and polygalacturonase production by Aspergillus sojae ATCC 20235 using response surface methodology
Enzyme and Microbial TechnologyVolume 40, Issue 53 April 2007Pages 1108-1116
C. Tari, N. Ggus and F. Tokatli

A two-step optimization procedure using central composite design with four factors (concentrations of maltrin and corn steep liquor (CSL), agitation speed and inoculation ratio) was used in order to investigate the effect of these parameters on the polygalacturonase (PG) enzyme activity, mycelia growth (biomass) and morphology (pellet size) of Aspergillus sojae ATCC 20235. According to the results of response surface methodology (RSM), initial concentrations of maltrin and CSL and agitation speed were significant (p < 0.05) on both PG enzyme production and biomass formation. As a result of this optimization, maximum PG activity (13.5 U/ml) was achievable at high maltrin (120 g/l), at low CSL (0 g/l), high agitation speed (350 rpm) and high inoculation ratio (2  107 total spore). Similarly, maximum biomass (26 g/l) could be obtained under the same conditions with only the difference for higher level of CSL requirement. The diameter of pellets in all optimization experiments ranged between 0.05 and 0.76 cm. The second optimization step improved the PG activity by 74% and the biomass by 40%.

The silica-coated chitosan particle from a layer-by-layer approach for pectinase immobilization
Enzyme and Microbial TechnologyVolume 40, Issue 53 April 2007Pages 1442-1447
Zhongli Lei and Shuxian Bi

We investigate the enzymatic activity of pectinase adsorbed on a novel type of colloidal particles. The colloidal stability is not impeded by the adsorbed proteins despite the fact that up to 247.8 mg of enzyme is adsorbed per gram of the carrier particles. Various characteristics of immobilized pectinase such as the pH stability, thermal stability, and storage stability were valuated. The immobilized pectinase revealed acceptable pH stability over a broad experimental range. The activity of immobilized pectinase adsorbed onto these particles is analyzed in terms of the MichaelisMenten parameters. The Michaelis constant Km differs only slightly from the Km value of the native enzyme when the amount of adsorbed enzyme is raised despite the high local concentration of immobilized enzymes.

Degradation kinetics of pectins by an alkaline pectinase in bioscouring of cotton fabrics
Carbohydrate PolymersVolume 67, Issue 419 February 2007Pages 572-575
Qiang Wan+g, Xuerong Fan, Zhaozhe Hua, Weidong Gao and Jian Chen

Alkaline pectinases have been proven to be effective as bioscouring agents of cotton fabrics. In order to monitor the scouring degree of cotton fabrics quantificationally, a kinetic study of the degradation of pectins in cotton by an alkaline pectinase Bioprep 3000L was performed and the influences of initial pectinase concentration and treatment time on bioscouring were evaluated quantitatively. The results showed that although the degradation products increased as pectinase concentration grew higher at same incubation time, the growth multiples of the maximum degradation rate which was used as the starting degradation rate were less than those of initial enzyme concentration. The degradation kinetics of pectins in cotton fibers with a pectinase could be described by modified GhoseWalseth kinetic empirical equations which had been previously applied to the degradation reaction of cellulose.

Effects of Neodymium on Growth, Pectinase Activity and Mycelium Permeability of Fusarium oxysporum
Journal of Rare EarthsVolume 25, Issue 1February 2007Pages 100-105
Zhang Yufeng, Yang Lifen, Chen Kaoshan and Dong Liang

The diameter of the colony of Fusarium oxysporum in solid medium, and the mycelium growth, pectinase activity, and mycelium permeability of Fusarium oxysporum in liquid medium under varying concentrations of Nd3+(0, 2, 4, 10, 20, 40, 60, 80, 100, 120, 140, 160, 180, 200, 300, and 400 mgL−1) were measured. The results indicated that the growth of Fusarium oxysporum was stimulated in solid medium when the concentration of Nd3+ ranges from 2 to 180 mgL−1, whereas it was inhibited when Nd3+ concentration was greater than 200 mgL−1. The colonies were fewer and smaller when Nd3+ was used in the solid medium. The growth of Fusarium oxysporum was inhibited in liquid medium when Nd3+ was used. The inhibition rate showed by the dry weight of mycelium ranged from 4.83% to 52.18% and increased with Nd3+ concentration. The pectinase activity decreased compared with that of controls. When the concentration of Nd3+ was 10 and 400 mgL−1, the pectinase activity decreased by 95% at both concentrations. Mycelium cell membrane permeability increased when Nd3+ concentrations ranged from 10 to 400 mgL−1 but decreased when Nd3+ concentration was 2 mgL−1.

Preparation and properties of immobilized pectinase onto the amphiphilic PS-b-PAA diblock copolymers
Journal of BiotechnologyVolume 128, Issue 130 January 2007Pages 112-119
Zhongli Lei and Shuxian Bi

Well-defined amphiphilic block copolymers poly(styrene-b-acrylic acid) (PS-b-PAA) with controlled block length were synthesized using atom transfer radical polymerization (ATRP). Pectinase enzyme was immobilized on the well-defined amphiphilic block copolymers PS-b-PAA. The carboxyl groups on the amphiphilic PS-b-PAA diblock copolymers present a very simple, mild, and time-saving process for enzyme immobilization. Various characteristics of immobilized pectinase such as the pH and temperature stability, thermal stability, and storage stability were valuated. Among them the pH optimum and temperature optimum of free and immobilized pectinase were found to be pH 6.0 and 65 C.

Enzyme aided extraction of lycopene from tomato tissues
Food ChemistryVolume 102, Issue 12007Pages 77-81
Sheetal M. Choudhari and Laxmi Ananthanarayan

Lycopene is a natural carotenoid pigment and a high value nutraceutical having wide use. The objective of the present work was to obtain a good yield of lycopene from tomato tissues, using cellulase and pectinase enzymes. Various parameters such as concentration of enzymes and time of incubation were optimised, to improve the yield of lycopene from tomatoes. Enzyme aided extraction of lycopene from whole tomatoes under optimised conditions resulted in an increase in the lycopene yield by 132 μg/g (198%) in cellulase treated sample and 108 μg/g (224%) in case of pectinase treated sample. Extraction from tomato peel under optimised conditions showed a remarkable increase in the yield of lycopene by 429 μg/g (107%) and 1104 μg/g (206%), for cellulase and pectinase treated samples, respectively. Likewise, the enzyme aided extraction of lycopene from fruit pulper waste and industrial waste of tomatoes was done to determine the potential for recovering the natural pigment from tomato waste.

Chitosan-tethered the silica particle from a layer-by-layer approach for pectinase immobilization
Food ChemistryVolume 104, Issue 22007Pages 577-584
Zhongli Lei, Shuxian Bi and Hong Yang

Spherical polyelectrolyte brush of coreshell structure were prepared by grafting poly (sodium 4-styrenesulphonate) (PSStNa) from SiO2 nanoparticle via the surface-initiated atom transfer radical polymerization strategy. The colloidal stability was not impeded by the adsorbed proteins despite the fact that up to 316.8 mg of enzyme was adsorbed per gram of the carrier particles. The immobilized pectinase revealed acceptable pH stability over a broad experimental range of 3.04.5. The activity half lives for native and bound states of enzyme were found as 13.5 d and 30 d, respectively. The activity of immobilized pectinase adsorbed onto these particles was analyzed in terms of the MichaelisMenten parameters. Kinetic parameters were calculated as 8.28 and 9.98 g pectin ml−1 for Km and 1.165  10−3 g pectin s−1 g enzyme−1 1.124  10−3 g pectin s−1 g particle−1 for Vmax in the case of free and immobilized enzymes, respectively. Enzyme activity was found to be approximately 49.7% for immobilized enzyme after storage for 1 month.

Xylanase and pectinase production by Aspergillus awamori on grape pomace in solid state fermentation
Process BiochemistryVolume 42, Issue 1January 2007Pages 98-101
Carolina Botella, Ana Diaz, Ignacio de Ory, Colin Webb and Ana Blandino

The feasibility of using grape pomace for the production of xylanase and exo-polygalacturonase by Aspergillus awamori in solid state fermentation has been evaluated. Solid state fermentation experiments indicated that the particle size did not influence the enzyme production. The addition of extra carbon sources and the initial moisture content of the grape pomace were found to have a marked influence on the enzymes yields. Xylanase and exo-PG activities were high at 65% (w/w) initial moisture content and glucose supplementation.

Optimization of process for the production of fungal pectinases from deseeded sunflower head in submerged and solid-state conditions
Bioresource TechnologyVolume 97, Issue 18December 2006Pages 2340-2344
Sarvamangala R. Patil and A. Dayanand

Pectinase production studies were carried out in submerged and solid-state conditions from deseeded sunflower head employing Aspergillus niger. The two potential strains of A. niger, DMF 27 for submerged and DMF 45 for solid-state were isolated by multi-step screening technique based on coefficient of pectolysis and capability of pectinase production. Process variables such as size of inoculum, pH, temperature, particle size and moisture content were optimized with an aim to achieve the maximum production of pectinases. The increased level of pectinase production was recorded at pH 5.0 and temperature 34 C in submerged and solid-state conditions. The optimum inoculum size was 1  105 ml−1 for submerged and 1  107 g−1 for solid-state conditions. Five hundred micrometer particle size and 65% moisture content of the substrate were optimum for the maximum production of pectinases in solid-state condition. Under optimum conditions, maximum production of exo-pectinase was 34.2 U/g in SSF and endo-pectinase was 12.6 U/ml in SmF.

Production of pectinase from deseeded sunflower head by Aspergillus niger in submerged and solid-state conditions
Bioresource TechnologyVolume 97, Issue 16November 2006Pages 2054-2058
Sarvamangala R. Patil and A. Dayanand

Studies were carried out on the production of pectinases using deseeded sunflower head by Aspergillus niger DMF 27 and DMF 45 in submerged fermentation (SmF) and solid-state fermentation (SSF). Higher titres of endo- and exo-pectinases were observed when medium was supplemented with carbon (4% glucose for SmF and 6% sucrose for SSF) and nitrogen (ammonium sulphate, 0.3% for both SmF and SSF) sources. Green gram husk proved to be relatively a better supplement to attain higher yield of endo-pectinase (11.7 U/g) and exo-pectinase (30.0 U/g) in solid-state conditions. Maximum production of endo-pectinase (19.8 U/g) and exo-pectinase (45.9 U/g) by DMF 45 were recorded in SSF when compared to endo-pectinase (18.9 U/ml) and exo-pectinase (30.3 U/ml) by DMF 27 in SmF under optimum process conditions.

The role of pectin in orange juice stabilization: Effect of pectin methylesterase and pectinase activity on the size of cloud particles
Food HydrocolloidsVolume 20, Issue 7October 2006Pages 961-965
Sarah Croak and Milena Corredig

In citrus juice cloud particles impart the characteristic color and flavor, and although the chemical composition of these particles is known, the details of their stabilization are not well understood. Pectin, a major component of orange juice cloud, is thought to play an important role in juice destabilization: in the presence of the active enzyme pectin methylesterase (PME), pectin forms calcium pectate complexes and causes the precipitation of cloud particles. This research summarizes a study on the changes occurring to orange juice cloud particles after addition of pectinase and PME. The particle size of juice cloud did not change with addition of pectinase. On the other hand, at the natural pH (3.8) of the juice, the addition of PME caused aggregation of the cloud particles within a few minutes, and the amount of enzyme added affected the kinetics of the aggregation. A higher amount of enzyme was necessary to cause the same effects at pH 6.0, while at low pH (2.5) cloud particles showed faster aggregation and a higher particle size, possibly because of a decreased surface charge at this pH. The results obtained by dynamic light scattering provided evidence of a direct effect of the PME on cloud and question our current understanding of the mechanism of cloud loss.

The effect of polysaccharide-degrading wine yeast transformants on the efficiency of wine processing and wine flavour
Journal of BiotechnologyVolume 125, Issue 41 October 2006Pages 447-461
C. Louw, D. La Grange, I.S. Pretorius and P. van Rensburg

Commercial polysaccharase preparations are applied to winemaking to improve wine processing and quality. Expression of polysaccharase-encoding genes in Saccharomyces cerevisiae allows for the recombinant strains to degrade polysaccharides that traditional commercial yeast strains cannot. In this study, we constructed recombinant wine yeast strains that were able to degrade the problem-causing grape polysaccharides, glucan and xylan, by separately integrating the Trichoderma reesei XYN2 xylanase gene construct and the Butyrivibrio fibrisolvens END1 glucanase gene cassette into the genome of the commercial wine yeast strain S. cerevisiae VIN13. These genes were also combined in S. cerevisiae VIN13 under the control of different promoters. The strains that were constructed were compared under winemaking conditions with each other and with a recombinant wine yeast strain expressing the endo-β-1,4-glucanase gene cassette (END1) from B. fibrisolvens and the endo-β-1,4-xylanase gene cassette (XYN4) from Aspergillus niger, a recombinant strain expressing the pectate lyase gene cassette (PEL5) from Erwinia chrysanthemi and the polygalacturonase-encoding gene cassette (PEH1) from Erwinia carotovora. Wine was made with the recombinant strains using different grape cultivars. Fermentations with the recombinant VIN13 strains resulted in significant increases in free-flow wine when Ruby Cabernet must was fermented. After 6 months of bottle ageing significant differences in colour intensity and colour stability could be detected in Pinot Noir and Ruby Cabernet wines fermented with different recombinant strains. After this period the volatile composition of Muscat dAlexandria, Ruby Cabernet and Pinot Noir wines fermented with different recombinant strains also showed significant differences. The Pinot Noir wines were also sensorial evaluated and the tasting panel preferred the wines fermented with the recombinant strains.

Pectinase production by solid fermentation from Aspergillus niger by a new prescription experiment
Ecotoxicology and Environmental SafetyVolume 64, Issue 2June 2006Pages 244-250
Jing Debing, Li Peijun, Frank Stagnitti, Xiong Xianzhe and Ling Li

The Ordos Plateau in China is covered with up to 300,000 ha of peashrub (Caragana) which is the dominant natural vegetation and ideal for fodder production. To exploit peashrub fodder, it is crucially important to optimize the culture conditions, especially culture substrate to produce pectinase complex. In this study, a new prescription process was developed. The process, based on a uniform experimental design, first optimizes the solid substrate and second, after incubation, applies two different temperature treatments (30 ring operatorC for the first 30 h and 23 ring operatorC for the second 42 h) in the fermentation process. A multivariate regression analysis is applied to a number of independent variables (water, wheat bran, rice dextrose, ammonium sulfate, and Tween 80) to develop a predictive model of pectinase activity. A second-degree polynomial model is developed which accounts for an excellent proportion of the explained variation (R2=97.7%). Using unconstrained mathematical programming, an optimized substrate prescription for pectinase production is subsequently developed. The mathematical analysis revealed that the optimal formula for pectinase production from Aspergillus niger by solid fermentation under the conditions of natural aeration, natural substrate pH (about 6.5), and environmental humidity of 60% is rice dextrose 8%, wheat bran 24%, ammonium sulfate ((NH4)2SO4) 6%, and water 61%. Tween 80 was found to have a negative effect on the production of pectinase in solid substrate. With this substrate prescription, pectinase produced by solid fermentation of A. niger reached 36.3 IU/(g DM). Goats fed on the pectinase complex obtain an incremental increase of image during the initial 25 days of feeding, which is a very promising new feeding prospect for the local peashrub. It is concluded that the new formula may be very useful for the sustainable development of arid and semiarid pastures such as those of the Ordos Plateau.

Purification and characterization of a novel pectinase from Acrophialophora nainiana with emphasis on its physicochemical properties
Journal of BiotechnologyVolume 123, Issue 13 May 2006Pages 33-42
S. Maria C. Celestino, S. Maria de Freitas, F. Javier Medrano, M. Valle de Sousa and E. Ximenes Ferreira Filho

An extracellular pectinase (PECI) was purified to apparent homogeneity from liquid state cultures of the thermophilic fungus Acrophialophora nainiana by ultrafiltration and a combination of gel filtration and ion-exchange chromatographic procedures. The molecular masses of PECI were 35,500 and 30,749 Da, as determined by SDS-PAGE and mass spectrometry, respectively. It was more active at 60 C and pH 8.0 and showed high stability at 50 C with half-life of 7 days. However at 60 and 70 C, PECI was much less stable with half lives of approximately 20 and 3 min, respectively. The thermostability of purified PECI was also investigated by fluorescence and circular dichroism spectroscopy. Fluorescence revealed that the unfolding transition region was observed between 45 and 70 C. A major decrease in the stability was found at 70 C. Circular dichroism measurements at pH between 5.0 and 9.0 showed a transition temperature (Tm) range of 5055. The thermodynamic analysis of these results showed that EPGI is thermal stable protein exhibiting maximum stability (ΔG25) of 22.65 and 19.19 kcal/mol at pH 8.0 and 9.0, respectively. The apparent Km value on pectin from citrus fruits was 4.22 mg ml−1. PECI exhibited no detectable activity of pectin methylesterase, endo-polygalacturonase, mannanase, xylanase and cellulase. However, it showed exo-polygalacturonase and pectin lyase activities. The presence of carbohydrate was detected in the pure PECI. It was activated by l-tryptophan, DEPC, DTT, DTNB, DTP, l-cystein and β-mercaptoethanol and inhibited by NBS, Fe2+, Cu2+, Zn2+, Mn2+, Al3+ and Ca2+. The enzyme showed homology with a pectin lyases from Xanthomonas campestris and Bacillus licheniformis.

A marked enhancement in the production of a highly alkaline and thermostable pectinase by Bacillus pumilus dcsr1 in submerged fermentation by using statistical methods
Bioresource TechnologyVolume 97, Issue 5March 2006Pages 727-733
D.C. Sharma and T. Satyanarayana

The production of a highly alkaline and thermostable pectinase of Bacillus pumilus was optimized in submerged fermentation using PlackettBurman design and response surface methodology. Three fermentation variables (C:N ratio, K2HPO4, and pH), which were identified to significantly affect pectinase production by PlackettBurman design were further optimized using response surface methodology of central composite design (CCD). An over all 34- and 41-fold increase in enzyme production was achieved in shake flasks and lab fermenter by the optimization of variables using statistical approaches, respectively. The enzyme was optimally active at pH 10.5 and 50 C, and selectively degraded only the noncellulosic gummy material of ramie (Boehmeria nivea) fibres causing 10.96% fibre weight loss, and therefore, the enzyme could find application in fibre processing industry. The use of the enzyme in fibre processing reduces the use of alkali, and the associated alkalinization of water bodies.








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