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Microbial pectinase: sources, characterization and applications

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Abstract

Today pectinases are upcoming industrially important bacterial enzymes. It can be produced by a variety of microorganisms. These enzymes act on pectin, which is the major component of middle lamella in plant cell wall. Pectinolytic enzymes are classified according to their mode of attack on the galacturonan part of the pectin molecules such as protopectinases, esterase’s and depolymerases. As we know that microbial enzymes work depends up on the type of enzymes application, temperature, concentration, and pH and so on, therefore, pectinase enzyme also differentiated according to their physical and chemical factors too. The biochemical structures of pectinases include members of all the major classes and the structure–function relationship, studies of a few available complexes of pectinases with substrate/analogs could be considered as prototypes for related family member and the molecular characterization of pectinolytic enzymes is also well documented. Furthermore, it provides a bird’s eye view of the possible application of these enzymes in commercial sector.

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References

  • Aalbersberg WY, Hamer RJ, Jasperse P, de Jongh HHJ, de Kruif CG, Walstra P, de Wolf FA (2003) Industrial proteins in perspective 23:1–284. ISBN: 9780444513946

    Google Scholar 

  • Abe J, Bergman FW, Obata K, Hikuri S (1988) Production of raw starch digesting amylase by Aspergillus K-27. Appl Microbiol Biotechnol 27:447–450

    CAS  Google Scholar 

  • Aguilar G, Huirton C (1990) Constitutive exo-pectinase produced by Aspergillus sp. CH-Y-1043 on different carbohydrate source. Biotechnol Lett 12:655–660

    CAS  Google Scholar 

  • Akita M, Suzuki A, Kobayashi T, Ito S, Yamane T (2000) Crystallization and preliminary X-ray analysis of high-alkaline pectate lyase. Acta Crystallogr D 56:749–750

    CAS  Google Scholar 

  • Alkorta I, Garbisu G, Llama MJ, Serra JL (1998) Industrial applications of pectic enzymes: a review. Process Biochem 1:21–28

    Google Scholar 

  • Alonso J, Canet W, Hawell N, Alique R (2003) Purification and characterization of carrot (Daucas carota L.) pectinesterase. J Sci Food Agric 83:1600–1606

    CAS  Google Scholar 

  • Amorim HV, Amorim VL (1977) Coffee enzyme and coffee quality. In: Ori R, St. Angelo AJ (eds) Enzymes in food and beverage processing. ACS Symposium Series 47:27–56

  • Arenas-Ocampo ML, Evangelista-Lozano S, Arana-Errasquin R, Jiménez-Aparicio A, Dávila-Ortíz G (2003) Softening and biochemical changes of sapote mamey fruit (Pouteria sapota) at different development and ripening stages. J Food Chem 27:91–95

    CAS  Google Scholar 

  • Arias C, Burns JA (2002) Pectinmethylesterase gene associated with a heatstable extract from citrus. J Agric Food Chem 50:3465–3472

    CAS  Google Scholar 

  • Armand S, Wagemaker MJ, Sanchez-Torres P, Kester HC, Van Santen Y, Dijkstra BW, Visser J, Benen JA (2000) The active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis. J Biol Chem 275:691–696

    CAS  Google Scholar 

  • Assis SA, Fernandes P, Ferreira BS, Trevisan HC, Cabral JMS, Oliveira OMMF (2004) Screening of supports for the immobilization of pectin-methylesterase from acerola (Malpighia glabra L.). J Chem Technol Biotechnol 79:277–280

    Google Scholar 

  • Beldman G, Rombouts FM, Voragen AGJ, Pilink W (1984) Application of cellulase and pectinase from fungal origin for the liquefaction and saccharification of biomass. Enzyme Microbiol Technol 6:503–507

    CAS  Google Scholar 

  • Bhat MK (2000) Research review paper: cellulases and related enzymes in biotechnology. Biotechnol Adv 18:355–383

    CAS  Google Scholar 

  • Braconnot H, Keppler F, Hamilton JTG, Braß M, Röckmann T (2006) Methane emissions from terrestrial plants under aerobic conditions. Nature 439:187–191

    Google Scholar 

  • Brown IE, Mallen MH, Charnock SJ, Davies GJ, Black GW (2001) Pectate lyase 10A from Pseudomonas cellulosa is a modular enzyme containing a family 2a carbohydrate-binding module. Biochem J 355:155–165

    CAS  Google Scholar 

  • Bruhlman F, Kim KS, Zimmerman W, Fiecher A (1994) Pectinolytic enzymes from actinomycetes for the degumming of ramie bast fibers. Appl Environ Microbial 60:2107–2112 (Chimia 14:165–167)

    Google Scholar 

  • Cao J, Zheng L, Chen S (1992) Screening of pectinase producer from alkalophilic bacteria and study on its potential application in degumming of rammie. Enzyme Microb Technol 4:1013–1016

    Google Scholar 

  • Chadha R, Kumbhar BK, Sarkar BC (2003) Enzymatic hydrolysis of carrot for increased juice recovery. J Food Sci Technol 40:35–39

    Google Scholar 

  • Chesson A (1980) Maceration in relation to the post handling and processing of plant material. J Appl Biotechnol 48:1–45

    CAS  Google Scholar 

  • Cho SW, Lee S, Shin W (2001) The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase–octagalacturonate complex. J Mol Biol 311:863–878

    CAS  Google Scholar 

  • Christensen TM, Nielsen JE, Kreiberg JD, Rasmussen P, Mikkelsen JD (2002) Pectin methyl esterase from orange fruit: characterization and localization by in situ hybridization and immunohistochemistry. Planta 206:493–503

    Google Scholar 

  • Cornick NA, Jensen NS, Stahl DA, Hartman PA, Allison MJ (1994) Lachnospira pectinoschiza sp. nov., an anaerobic pectinophile from the pig intestine. Int J Syst Bacteriol 44:87–93

    CAS  Google Scholar 

  • Corredig M, Kerr W, Wicker L (2000) Separation of thermostable pectinmethylesterase from marsh grapefruit pulp. J Agric Food Chem 48:4918–4923

    CAS  Google Scholar 

  • Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D (2005) Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein. Plant Cell 17:849–858

    Google Scholar 

  • Dixit VS, Kumar AR, Pant A, Khan MI (2004) Low molecular mass pectate lyase from Fusarium moniliforme: similar modes of chemical and thermal denaturation. Biochem Biophys Res Commun 315:477–484

    CAS  Google Scholar 

  • Dominguez H, Nunez MJ, Lema JM (1994) Enzymatic pretreatment to enhance oil extraction from fruits and oil seeds: a review. Food Chem 49:271–286

    CAS  Google Scholar 

  • Dorokhov YL, Mankinen K, Frolova OY, Mertis A, Saarinen J, Kalkkinen N et al (1999) A novel function for a ubiquitous plant enzyme pectin methylesterase: the host-cell receptor for the tobacco mosaic virus movement protein. FEBS Lett 461:233–238

    Google Scholar 

  • Fayyaz A, Asbi BA, Ghazali HM, Che Man TB, Jinap S (1993) Pectinesterase extraction from papaya. Food Chem 47:183–185

    CAS  Google Scholar 

  • Fayyaz A, Fukusaki EI, Kobayashi A (2003) Methanol production is enhanced by expression of an Aspergillus niger pectin methylesterase in tobacco cells. J Biotechnol 106:45–52

    Google Scholar 

  • Federici L, Caprari C, Mattei B, Savino C, Di Matteo A, De Lorenzo G, Cervone F, Tsernoglou D (2001) Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein). Proc Natl Acad Sci USA 98:13425–13430

    CAS  Google Scholar 

  • Forster H (1988) Pectinesterase from Phytophthora infestans. Methods Enzymol 161:355–357

    CAS  Google Scholar 

  • Gaffe J, Tizando ME, Handa AK (1997) Characterization and functional expression of a ubiquitously expressed tomato pectin methylesterase. Plant Physiol 114:1547–1556

    CAS  Google Scholar 

  • Gainvors A, Frezier V, Lemaresquier H, Lequart C, Aigle M, Belarbi A (1994) Detection of polygalacturonase, pectin lyase and pectinesterase activities in Saccharomyces cerevisiae strain. Yeast 10:1311–1319

    CAS  Google Scholar 

  • Grassin C, Fauquembergue P (1996) Fruit juices. In: Godfrey T, West S (eds) Industrial enzymology, 2nd edn. Stockholm Press, New York, pp 225–264

    Google Scholar 

  • Gummadi SN, Panda T (2003) Purification and biochemical properties of microbial pectinases: a review. Process Biochem 38:987–996

    CAS  Google Scholar 

  • Gupta S, Kapoor M, Sharma KK, Nair LM, Kuhad RC (2008) Production and recovery of an alkaline exo-polygalacturonase from Bacillus subtilis RCK under solid-state fermentation using statistical approach. Bioresour Technol 99:937–945

    CAS  Google Scholar 

  • Gysler C, Harmsen JAM, Kester HCM, Visser J, Heim J (1990) Gene 89:101–108

    CAS  Google Scholar 

  • Hadj TN, Ayadi M, Trigui S, Bouabdollah F, Gargouri A (2002) Hyper production of pectinase activities by fully constitutive mutant (CT 1) of Penicillium occitanis. Enzyme Microbial Technol 30:662–666

    Google Scholar 

  • Hayashi K, Inoue Y, Shiga M, Sato S, Takano R, Hirayae K, Hibi T, Hara S (1997) Pectinolytic enzymes from pseudomonas marginalis MAFF 03-01173. Phytochemistry 45:1359–1363

    CAS  Google Scholar 

  • Herron SR, Scavetta RD, Garrett M, Legner M, Jurnak F (2003) Characterization and implications of Ca2+ binding to pectate lyase C. J Biol Chem 278:12271–12277

    CAS  Google Scholar 

  • Holbom B, Ekman R, Sjoholm R, Eckerman C, Thornton J (1991) Chemical changes in peroxide bleaching of mechanical pulps. Das Papier A 45(10):V16–V22

    Google Scholar 

  • Horikoshi K (1990) Enzymes of alkalophiles. In: Fogarty WM, Kelly CT (eds) Microbial enzymes and biotechnology, 2nd edn. Elsevier Applied Science, London, pp 275–294

    Google Scholar 

  • Horikoshi K (1995) Discovering novel bacteria, with an eye to biotechnological applications. Curr Opin Biotechnol 6:292–297

    CAS  Google Scholar 

  • Horn D, Linhart F (1996) Retention aids. In: Roberts JC (ed) Paper chemistry. Blackie Academic and Professional, London, pp 64–82

    Google Scholar 

  • Innocenzo MD, Lajalo FM (2001) Effect of gamma irradiation on softening changes and enzyme activities during ripening of papaya fruit. J Food Biochem 25:19–27

    Google Scholar 

  • Janssens L, de Pooter HL, Vandamme EJ et al (1992) Production of flavours by microorganisms. Process Biochem 27:195–215

    CAS  Google Scholar 

  • Jayani RS, Saxena S, Gupta R (2005) Microbial pectinolytic enzymes: a review. Process Biochem 40:2931–2944

    CAS  Google Scholar 

  • Jenkins J, Mayans O, Smith D, Worboys K, Pickersgill RW (2001) Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site. J Mol Biol 305:951–960

    CAS  Google Scholar 

  • Jensen MH, Otten H, Christensen U, Borchert TV, Christensen LL, Larsen S, Leggio LL (2010) Structural and biochemical studies elucidate the mechanism of rhamnogalacturonan lyase from Aspergillus aculeatus. J Mol Biol 404:100

    CAS  Google Scholar 

  • Johansson K, Ahmad ME, Friemann R, Jörnvall H, Markovi O, Eklund H (2002) Crystal structure of plant pectin methylesterase. FEBS Lett 514:243–249

    CAS  Google Scholar 

  • Junwei C, Weihua S, Yong P, Shuyun C (2000) High-producers of polygalacturonase selected from mutants resistant to rifampin in alkalophilic Bacillus sp. NTT33. Enzyme Microb Technol 27:545–548

    Google Scholar 

  • Karam NE, Belarbi A (1995) Detection of polygalacturonase and pectinesterases in lactic acid bacteria. World J Microbiol Biotechnol 11:559–563

    CAS  Google Scholar 

  • Kareem SO, Adebowale AA (2007) Clarification of orange juice by crude fungal pectinase from citrus peel. Niger Food J 25:130–137

    CAS  Google Scholar 

  • Kashyap DR, Vohra PK, Chopra S, Tewari R (2001) Applications of pectinases in the commercial sector: a review. Biores Technol 77:215–227

    CAS  Google Scholar 

  • Kawano CY, Chellegatti MASC, Said S, Fonseca MJV (1999) Comparative study of intracellular and extracellular pectinases produced by Penicillium frequentans. Biotechnol Appl Biochem 29:133–140

    CAS  Google Scholar 

  • Kertesz Z (1930) A new method for enzymic clarification of unfermented apple juice. New York State Agricultural Experimentation Station (Geneva). US Patent 1,932,833. Bull. No. 689

  • Kita N, Boyd CM, Garrett MR, Jurnak F, Keen NT (1996) Differential effect of site-directed mutations in PelC of pectate lyase activity, plant tissue maceration, and elicitor activity. J Biol Chem 271:26529–26535

    CAS  Google Scholar 

  • Kitamoto N, Yasuda YS, Ohmiya K, Tsukagoshi N (2001) Biosci Biotechnol Biochem 65:209–212

    CAS  Google Scholar 

  • Kobayashi T, Higaki N, Suzumatsu A, Sawada K, Hagihara H, Kawai S, Ito S (2001) Purification and properties of a highmolecular-weight, alkaline exopolygalacturonase from a strain of Bacillus. Enzyme Microb Technol 29:70–75

    CAS  Google Scholar 

  • Koboyashi T, Koike K, Yoshimatsu T, Higaki N, Suzumatsu A, Ozawa T et al (1999) Purification and properties of a low-molecular weight, high-alkaline pectate lyase from an alkaliphilic strain of Bacillus. Biosci Biotechnol Biochem 63:72–75

    Google Scholar 

  • Kotoujansky A (1987) Molecular genetics of pathogenesis by soft-rot Erwinia. Annu Rev Phytopathol 25:405–430

    CAS  Google Scholar 

  • Kumar S, Tamura K, Nei M (2004) Brief Bioinform 5:150–163

    CAS  Google Scholar 

  • Lassmann T, Sonnhammer EL (2006) Nucleic Acids Res 34(Web Server Issue):W596–W599

  • Laurent F, Kotoujansky A, Bertheau Y (2000) Overproduction in Escherichia coli of the pectin methylesterase A from Erwinia chrysanthemi 3937: one-step purification, biochemical characterization, and production of polyclonal antibodies. Can J Microbiol 46:474–480

    CAS  Google Scholar 

  • Libkind D, Pérez P, Sommaruga R, Diéguez MC, Ferraro M, Brizzio S, Zagarese H, Van Broock M (2004) Constitutive and UV-inducible synthesis of photoprotective compounds (carotenoids and mycosporines) by freshwater yeasts. Photochem Photobiol Sci 3:281–286

    CAS  Google Scholar 

  • Lietzke SE, Keen NT, Yoder MD, Jurnak F (1994) The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi. Plant Physiol 106:849–862

    CAS  Google Scholar 

  • Macdonald HC, Evans R (1996) Purification and properties of apple pectinesterase. J Sci Food Agric 70:321–326

    CAS  Google Scholar 

  • Maiorano AE, Schmidell W, Ogaki Y (1995) Short communication: determination of the enzymatic activity of pectinases from different microorganisms. World J Microbiol Biotechnol 11:355–356

    CAS  Google Scholar 

  • Maldonado MC, Saad AMS, Callieri DAS (1994) Purification and characterization of pectinesterase produced by a strain of Aspergillus niger. Curr Microbiol 24:193–196

    Google Scholar 

  • Maldonaldo MS, Saad AMS (1998) Production of pectinesterase and polygalacturonase by Aspergillus niger in submerged and solid state systems. J Ind Microbiol Biotechnol 20:34–38

    Google Scholar 

  • Martin N, De Souza RS, De Silva R, Gomes E (2004) Pectinases production by fungal strain in solid state fermentation agro-industrial by-product. Braz Arch Biol Technol 47:813–819

    CAS  Google Scholar 

  • Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J, Pickersgill R, Jenkins J (1997) Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate binding clefts of pectin and pectate lyases. Structure 5:677–689

    CAS  Google Scholar 

  • McCarthy RE, Kotarski SF, Salyers AA (1985) Location and characteristics of enzymes involved in the breakdown of polygalacturonic acid by Bacteroides thetaiotaomicron. J Bacteriol 161:493–499

    CAS  Google Scholar 

  • Moharib SA, El-Sayed ST, Jwanny EW (2000) Evaluation of enzymes produced from yeast. Nahrung 44:47–51

    CAS  Google Scholar 

  • Naidu GSN, Panda T (1998) Application of response surface methodology to evaluate some aspects of pectolytic enzymes from Aspergillus niger. Biochem Eng J 2:71–77

    CAS  Google Scholar 

  • Naidu GSN, Panda T (1999) Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: a statistical approach. Enzyme Microb Technol 25:116–124

    CAS  Google Scholar 

  • Naidu GSN, Panda T (2003) Studies on pH and thermal deactivation of pectolytic enzymes from Aspergillus niger. Biochem Eng J 16:57–67

    CAS  Google Scholar 

  • Oeser B, Heidrich PM, Müller U, Tudzynski P, Tenberge KB (2002) Polygalacturonase is a pathogenicity factor in the Claviceps purpurea/rye interaction. Fungal Genet Biol 36:176–186

    CAS  Google Scholar 

  • Pages S, Heijne WH, Kester HC, Visser J, Benen JA (2000) Subsite mapping of Aspergillus niger endopolygalacturonase II by site-directed mutagenesis. J Biol Chem 275:29348–29353

    CAS  Google Scholar 

  • Palomaki T, Saarilahti HT (1997) Isolation and characterization of new C-terminal substitution mutation affecting secretion of polygalacturonases in Erwinia carotovora ssp. carotovora. FEBS Lett 400:122–126

    CAS  Google Scholar 

  • Pathak N, Sanwal GG (1998) Multiple forms of polygalacturonase from banana fruits. Phytochemistry 48:249–255

    CAS  Google Scholar 

  • Patill NP, Chaudhari BL (2010) Microbiology production and purification of pectinase by soil isolate penicillium sp and search for better agroresidue for its ssf. Recent Res Sci Technol 2(7):36–42

    Google Scholar 

  • Patill SR, Dayanand A (2006) Exploration of regional agrowastes for the production of pectinase by Aspergillus niger. Food Technol Biotechnol 44(2):289–292

    Google Scholar 

  • Perrone G, Mulè G, Susca A, Battilani P, Pietri A, Logrieco A (2006) Ochratoxin A production and AFLP analysis of Aspergillus carbonarius, Aspergillus tubingensis, and Aspergillus niger strains isolated from grapes in Italy. Appl Environ Microbiol 72:680–685

    CAS  Google Scholar 

  • Petersen TN, Kauppinen S, Larsen S (1997) The crystal structure of a rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix. Structure 5:533–544

    CAS  Google Scholar 

  • Pickersgill R, Jenkins J, Harris G, Nasser W, Robert-Baudouy J (1994) The structure of Bacillus subtilis pectate lyase in complex with calcium. Nat Struct Biol 1:717–723

    CAS  Google Scholar 

  • Pickersgill R, Smith D, Worboys K, Jenkins J (1998) Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora. J Biol Chem 273:24660–24664

    CAS  Google Scholar 

  • Pilnik W, Voragen AGJ (1993) Pectic enzymes in fruit juice and vegetable juice manufacture. In: Reeds G (ed) Food and science technology, enzymes in food processing. Academic Press, New York, pp 363–399

    Google Scholar 

  • Pitkanen K, Heikinheimo R, Pakkanen R (1992) Purification and characterization of Erwinia chrysanthemi B374 pectin methylesterase produced by Bacillus subtilis. Enzyme Microbial Technol 14:832–836

    CAS  Google Scholar 

  • Powell ALT, Van Kan JAL, Ten Have A, Visser J, Greve LC, Bennett AB, Labavitch JM (2000) Transgenic expression of pear PGIP in tomato limits colonization. Mol Plant Microbe Interact 13(9):942–950

    CAS  Google Scholar 

  • Rajagopalan G, Krishnan C (2008) Immobilization of maltooligosaccharide forming α-amylase from Bacillus subtilis KCC103: properties and application in starch hydrolysis. J Chem Technol Biotechnol 83(11):1511–1517

    CAS  Google Scholar 

  • Rebeck H (1990) Processing of citrus juices. In: Hick D (ed) Production and packaging of non-carbohydrate fruit juices and fruit beverages. Van Nostrand Reinhold, New York

    Google Scholar 

  • Reid I, Ricard M (2000) Pectinase in paper making: solving retention problems in mechanical pulp, bleached with hydrogen peroxide. Enzyme Microb Technol 26:115–123

    CAS  Google Scholar 

  • Sakai T (1992) Degradation of pectins. In: Winkelmann G (ed) Microbial degradation of natural products. VCH, Weinheim, pp 57–81

    Google Scholar 

  • Sakiyama CCH, Paula EM, Pereira PC, Borges AC, Silva DO (2001) Characterization of pectin lyase produced by an endophytic strain isolated from coffee cherries. Lett Appl Microbiol 33:117–121

    CAS  Google Scholar 

  • Salemi M, Vandamme A (2003) The phylogenetic handbook: a practical approach to DNA and protein phylogeny. Cambridge University Press, Cambridge

    Google Scholar 

  • Sanchez S, Demain AL (2002) Review: metabolic regulation of fermentation processes. Enzyme Microb Technol 31:895–906

    CAS  Google Scholar 

  • Sarkenen S (1991) Enzymatic lignin degradation: an extracurricular view. In: Leatham GF, Himmel ME (eds) Enzymes in biomass conversion. ACS Symposium Series, American Chemical Society, USA. 460:247–269. ISBN-13: 9780841219953

  • Scavetta RD, Herron SR, Hotchkiss AT, Kita N, Keen NT, Benen JA, Kester HC, Visser J, Jurnak F (1999) Structure of a plant cell wall fragment complexed to pectate lyase C. Plant Cell 11:1081–1092

    CAS  Google Scholar 

  • Schell MA, Denny TP, Huang J (1994) Extracellular virulence factors of Pseudomonas solanacearum: role in disease and their regulation. In: Kado CI, Crosa JH (eds) Molecular mechanisms of bacterial virulence. Kluwer, Dordrecht, pp 311–324

    Google Scholar 

  • Schnitzhofer W, Weber H-J, Vršanská M, Biely P, Cavaco-Paulo A, Guebitz GM (2007) Purification and mechanistic characterisation of two polygalacturonases from Sclerotium rolfsii. Enzyme Microb Technol 40:1739–1747

    CAS  Google Scholar 

  • Scott-Craig JS, Panaccione DG, Cervone F, Walton JD (1990) Endopolygalacturonase is not required for pathogenicity of Cochliobolus carbonum on maize. Plant Cell 2:1191–1200

    CAS  Google Scholar 

  • Semenova MV, Grishutin SG, Gusakov AV, Okunev ON, Sinitsyu AP (2003) Isolation and properties of pectinases from the fungus Aspergillus japonicus. Biochemistry 68:559–569

    CAS  Google Scholar 

  • Semenova M, Sinitsyna O, Morozova V et al (2006) Use of a preparation from fungal pectin lyase in the food industry. Appl Biochem Microbiol 42:598–602

    CAS  Google Scholar 

  • Sharma HSS, Robinson E (1983) Fungal colonization during glyphosate induced desiccation and dew-retting of flax cultivars. Technical report no. 2281.11

  • Sharma NR, Sasankan A, Singh A, Soni G (2011) Production of polygalacturonase and pectin methyl esterase from agrowaste by using various isolates of Aspergillus niger. Insight Microbiol 1:1–7

    CAS  Google Scholar 

  • Shi GY, Jie TY, Bing TH, Hua WK, Wei CK (2007) Chin J Agric Biotechnol 4:33

    Google Scholar 

  • Shieh M, Brown RL, Whitehead MP, Carey JW, Cotty PL, Cleveland TE, Dean RA (1997) Molecular genetic evidence for the involvement of a specific polygalacturonase P2c, in the invasion and spread of Aspergillus flavus in cotton bolls. Appl Environ Microbiol 63:3548–3552

    CAS  Google Scholar 

  • Shimizu T, Nakatsu T, Miyairi K, Okuno T, Kato H (2002) Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution. Biochemistry 41:6651–6659

    CAS  Google Scholar 

  • Singh SA, AppuRao AG (1989) A simple fractionation protocol for and a comprehensive study of the molecular properties of two major endopolygalacturonases from Aspergillus niger. Biotechnol Appl Biochem 35:115–123

    Google Scholar 

  • Singh SA, Plattnera H, Diekmann H (1999) Exopolygalacturonate lyase from a thermophulic Bacillus sp. Enzyme Microb Technol 25:420–425

    CAS  Google Scholar 

  • Someren MAK, Harmsen JAM, Kester HCM, Visser J (1991) Curr Genet 20:293–299

    Google Scholar 

  • Someren MAK, Flipphi M, de Graaff L, van den Broeck H, Kester H, Hinnen A, Visser J (1992) Mol Gen Genom 234:113–120

    Google Scholar 

  • Soresen SO, Pauly M, Bush M, Skjot M, McCann MC, Borkhardt B, Ulvoskov P (2000) Pectin engineering: modification of potato pectin by in vivo expression of endo-1,4-β-d-galacturonase. Proc Natl Acad Sci USA 97:7639–7644

    Google Scholar 

  • Soriano M, Diaz P, Pastor FIJ (2005) Pectinolytic systems of two aerobic sporogenous bacterial strains with high activity on pectin. Curr Microb 50:114–118

    CAS  Google Scholar 

  • Suneetha V, Khan ZA (2011) Screening, characterisation and optimization of microbial pectinase. In: Shukla G, Varma A (eds) Soil enzymology. Soil Biology 22. Springer, Berlin, pp 3–337

  • Suneetha V, Tulsyan S (2010) Bioinformatics structure analysis of microbial pectinase. J Biotechnol Res (online). ISSN: 0975-1735

  • Sutton MD, Peterson JBD (2001) Fermentation of sugarbeet pulp for ethanol production using bioengineered Klebsiella oxytoca strain P2. J Sugar Beet Res 38:1

    Google Scholar 

  • Takao M, Nakaniwa T, Yoshikawa K, Terashita T, Sakai T (2000) Purification and characterization of thermostable pectate lyase with protopectinase activity from thermophilic Bacillus sp. TS 47. Biosci Biotechnol Biochem 64:2360–2367

    CAS  Google Scholar 

  • Takao M, Nakaniwa T, Yoshikawa K, Terashita T, Sakai T (2001) Molecular cloning, DNA sequence, and expression of the gene encoding for thermostable pectate lyase of thermophilic Bacillus sp. TS 47. Biosci Biotechnol Biochem 65:322–329

    CAS  Google Scholar 

  • Tanabe H, Kobayashi Y (1987) Plant tissue maceration caused by pectinolytic enzymes from Erwinia spp. under alkaline conditions. Agric Biol Chem 51(10):2845–2846

    CAS  Google Scholar 

  • Tanabe H, Kobayashi Y, Akamatsu I (1986) Pretreatment of pectic wastewater from orange canning by soft-rot Erwinia carotovora. J Ferment Technol 64:265–268

    CAS  Google Scholar 

  • Templeton MD, Sharrock KR, Bowen JK, Crowhurst RN, Rikkerink EH (1994) Gene 142:141–146

    CAS  Google Scholar 

  • Ten Have A, Mulder W, Visser JN, Van Kan AL (1998) The endopolygalacturonase gene Bcpg1 is required for full virulence of Botrytis cinerea. Mol Plant Microbe Interact 11:1009–1016

    Google Scholar 

  • Ten Have A, Tenberge KB, Benen JAE, Tudzynski P, Visser J, Van Kan AL (2002) The contribution of cell wall degrading enzymes to pathogenesis of fungal plant pathogens. In: Kempken F (ed) The mycota XI agricultural application. Springer, Berlin, pp 341–358

    Google Scholar 

  • Thomas LM, Doan CN, Oliver RL, Yoder MD (2002) Structure of pectate lyase A: comparison to other isoforms. Acta Crystallogr D 58:1008–1015

    Google Scholar 

  • Trejo-Hernendez MR, Oriol E, Lopez-Canales A, Roussos S, Viniegra G, Raimbault M (1991) Production of pectinase by Aspergillus niger by solid state fermentation on support. Micol Neotrop Apl 4:49–62

    Google Scholar 

  • Truong LV, Tuyen H, Helmke E, Binh LT, Schweder T (2001) Cloning of two pectate lyase genes from the marine Antarctic bacterium Pseudoalteromonas haloplanktis strain ANT/505 and characterization of the enzymes. Extremophiles 5:35–44

    CAS  Google Scholar 

  • Van Alebeek GJWM, Christensen TMIE, Schols HE, Mikkelsen JD, Voragen AGJ (2002) Mode of action of pectin lyase A of Aspergillus niger on differently C6-substituted oligogalacturonides. J Biol Chem 277(29):25929–25936

    Google Scholar 

  • Van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW (2003) Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger. FEBS Lett 554:462–466

    Google Scholar 

  • Van Santen Y, Benen JAE, Schroter KH, Kalk KH, Armand S, Visser J, Dijkstra BW (1999) 1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis. J Biol Chem 274:30474–30480

    Google Scholar 

  • Visser J, Bussink HJ, Witteveen C (2004) In Smith A (ed) Gene expression in recombinant microorganisms. Marcel Dekker, Inc., New York, pp 241–306

  • Vitali J, Schick B, Kester HCM, Visser J, Jurnak F (1998) The three dimensional structure of Aspergillus niger pectin lyase B at 1.7-Å resolution. Plant Physiol 116:69–80

    CAS  Google Scholar 

  • Voigt CA, Schafer W, Salomon S (2005) A secreted lipase of Fusarium graminearum is a virulence factor required for infection of cereals. Plant J 42:364–375

    CAS  Google Scholar 

  • Voragen AGJ, Coenen G-J, Verhoef RP, Schols HA (2009) Pectin, a versatile polysaccharide present in plant cell walls. Struct Chem 20:263–275

    CAS  Google Scholar 

  • Walkinshaw MD, Arnott S (1981a) Conformations and interactions of pectins. I. X-ray diffraction analysis of sodium pectate in neutral acidified forms. J Mol Biol 153:1055–1073

    CAS  Google Scholar 

  • Walkinshaw MD, Arnott S (1981b) Conformations and interactions of pectins. II. Models of junction zones in pectinic acid and calcium pectate gels. J Mol Biol 153:1075–1085

    CAS  Google Scholar 

  • Wanyoike WM, Kang Z, Buchenauer H (2002) Importance of cell wall degrading enzymes produced by Fusarium graminearum during infection of wheat head. Eur J Plant Pathol 108:803–810

    Google Scholar 

  • Ward OP, Moo-Young M (1989) Enzymatic degradation of cell wall and related plant polysaccharides. CRC Crit Rev Biotechnol 8:237–274

    CAS  Google Scholar 

  • Warrilow AGS, Turner RJ, Jones MG (1994) A novel form of pectinesterase in tomato. Phytochemistry 35:862–872

    Google Scholar 

  • West S (1996) Olive and other edible oils. In: Godfrey T, West S (eds) Industrial enzymology, 2nd edn. Stockholm Press, New York, pp 293–300

    Google Scholar 

  • Whitaker JR (1991) In: Kelly CT, Fogarty WM (eds) Microbial enzymes and biotechnology. Elsevier Applied Science, London, pp 133–175

    Google Scholar 

  • Wubben JP, Ten Have A, Van Kan JAL, Visser J (2000) Regulation of endopolygalacturonase gene expression in Botrytis cinerea by galacturonic acid, ambient pH and carbon catabolite repression. Curr Genet 37:152–157

    CAS  Google Scholar 

  • Yadav S, Yadav PK, Yadav D, Yadav KDS (2009) Process Biochem 44:1–10

    Google Scholar 

  • Yakoby N, Beno-Moualem D, Keen NT, Dinnor A, Pines O, Prusky D (2001) Colletotrichum gloeosporioides pelB is an important virulence factor in avocado fruit fungus interaction. Mol Plant Microbe Interact 14:988–995

    CAS  Google Scholar 

  • Yoder MD, Keen NT, Jurnak F (1993) New domain motif: structure of pectate lyase C, a secreted plant virulence factor. Science 260:1503–1507

    CAS  Google Scholar 

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Correspondence to Nevadita Sharma.

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Sharma, N., Rathore, M. & Sharma, M. Microbial pectinase: sources, characterization and applications. Rev Environ Sci Biotechnol 12, 45–60 (2013). https://doi.org/10.1007/s11157-012-9276-9

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