Skip to main content

Structural and Biochemical Properties of Pectinases

  • Chapter
Industrial Enzymes

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Akita, M., Suzuki, A., Kobayashi., T., Ito, S. and Yamane, T. (2000) Crystallization and preliminary X-Ray analysis of High-Alkaline Pectate Lyase. Acta Crystallogr. D. 56, 749–750.

    Article  PubMed  CAS  Google Scholar 

  • Albersheim, P. (1966) Pectin lyase from fungi. Methods enzymol. 8, 628–631.

    Article  CAS  Google Scholar 

  • Alkorta, I., Garbisu, G., Llama, M.J. and Serra, J.L. (1998) Industrial applications of pectic enzymes: A review. Proc. Biochem. 33, 21–28.

    Article  CAS  Google Scholar 

  • Anthon, G.E., Sekine, Y., Watanabe, N. and Barrett. D.M. (2002) Thermal Inactivation of Pectin Methylesterase, Polygalacturonase, and Peroxidase in Tomato Juice. Agric. Food Chem. 50, 6153–6159.

    Article  CAS  Google Scholar 

  • Armand, S., Wagemaker, M.J., Sanchez-Torres, P., Kester, H.C., van Santen, Y., Dijkstra, B.W., Visser, J. and Benen, J.A. (2000) The active site topology of Aspergillus niger endopolygalacturonase II as studied by site-directed mutagenesis. J. Biol. Chem. 275, 691–696.

    Article  PubMed  CAS  Google Scholar 

  • Beldman, G., Rombouts, F.M., Voragen, A.G.J. and Pilnik, W. (1984) Application of cellulase and pectinase from fungal origin for the liquifaction and sachharification of biomass. Enzyme Microbiol. Technol. 6, 503–507.

    Article  CAS  Google Scholar 

  • Brown, I.E., Mallen, M.H., Charnock, S.J., Davies, G.J. and Black, G.W. (2001) Pectate lyase 10A from Pseudomonas cellulosa is a modular enzyme containing a family 2a carbohydrate-binding module. Biochem. J. 355, 155–165.

    Article  PubMed  CAS  Google Scholar 

  • Carr, J.G. (1985) Tea, coffee and cocoa. In: Wood, B.J.B. (Eds.), Microbiology of Fermented Foods, vol. II. Elsevier Applied Science, London, pp. 133–154.

    Google Scholar 

  • Chin, L., Ali, Z.M. and Lazan, H. (1999) Cell wall modifications, degrading enzymes and softening of carambola fruit during ripening. J. Experimental Botany. 50, 767–775.

    Article  CAS  Google Scholar 

  • Cho, S.W, Lee, S and 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.

    Article  PubMed  CAS  Google Scholar 

  • Christensen. T.M., Nielsen, J.E., Kreiberg, J.D., Rasmussen, P. and Mikkelsen, J.D. (2002) Pectin methyl esterase from orange fruit: characterization and localization by in-situ hybridization and immunohistochemistry. Planta. 206, 493–503.

    Article  Google Scholar 

  • Coutinho, P.M. and Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach. In: Gilbert, H.J., Davies, G., Henrissat, B. and Svensson B. (Eds.), Recent Advances in Carbohydrate Bioengineering, The Royal Society of Chemistry, Cambridge, pp. 3–12.

    Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  • Dingle, J., Reid, W.W. and Solomons, G.L. (1953) The enzymatic degradation of pectin and other polysaccharides. II. Application of the ‘Cup-plate’ assay to the estimation of enzymes. J. Sci. Food Agric. 4, 149–155.

    Article  CAS  Google Scholar 

  • DiPietro, A. and Roncero, M.I. (1996) Purification and characterization of an exo-polygalacturonase from the tomato vascular wilt pathogen Fusarium oxysporum f.sp. lycopersici. FEMS Microbiol. Lett. 145, 295–299.

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

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

    Article  PubMed  ADS  CAS  Google Scholar 

  • Fogarty, W.M. and Ward, O.P. (1973) Pectinases and pectic polysaccharides. Prog. Ind. Microbiol. 13, 61–119.

    Google Scholar 

  • Fogarty, W.M. and Kelly, C.T. (1983) Pectic enzymes. In: Fogarty, M.W. (Eds.), Microbial Enzymes and Biotechnology. Applied Science Publishers, London, pp. 131–182.

    Google Scholar 

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

    Article  CAS  Google Scholar 

  • Godfrey, A. (1985) Production of industrial enzymes and some applications in fermented foods. In: Wood BJB (Eds.) Microbiology of fermented foods, Vol 1. Elsevier, London, pp 345-371.

    Google Scholar 

  • Grassin, C. and Fauquembergue, P. (1996) Fruit juices. In: Godfrey, T., West, S. (Eds.), Industrial Enzymology, second ed. Stockholm Press, New York, pp. 225-264.

    Google Scholar 

  • Gummadi, S.N. and Kumar, D.S. (2005) Microbial pectic transeliminases. jtBiotechnol. Lett. 27, 451–458.

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Gurucharanam, K. and Deshpande, K.S. (1986) Polysaccharides of Curbularia lunata: Use in degumming of ramie fibers. Ind. J. Phytopathol. 39, 385–389.

    CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Hasunuma, T., Fukusaki, E.I. and Kobayashi, A. (2003) Methanol production is enhanced by expression of an Aspergillus niger pectin methylesterase in tobacco cells. J. Biotechnol. 106, 45–52.

    Article  PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  • Henriksson, G., Akin, D.E., Slomczynski, D. and Eriksson, K.E.L. (1999) Production of highly efficient enzymes for flax retting by Rhizomucor pusillus. J. Biotechnol. 68, 115–123.

    Article  CAS  Google Scholar 

  • Herron, S.R., Benen, J.A., Scavetta, R.D., Visser, J. and Jurnak, F. (2000) Structure and function of pectic enzymes: virulence factors of plant pathogens. Proc. Natl. Acad. Sci. U S A. 97, 8762–8769.

    Article  PubMed  ADS  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Hoondal, G.S., Tewari, R.P., Tewari, R., Dahiya, N. and Beg, Q.K. (2002) Microbial alkaline pectinases and their industrial applications a review. Appl. Microbiol. Biotechnol. 59, 409–418.

    Article  PubMed  CAS  Google Scholar 

  • Jenkins, J., Mayans, O., Smith, D., Worboys, K. and Pickersgill, R.W. (2001) Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site. J. Mol. Biol. 305, 951–60.

    Article  PubMed  CAS  Google Scholar 

  • Johansson, K., El-Ahmad, M., Friemann, R., Jornvall, H., Markovic, O. and Eklund, H. (2002) Crystal structure of plant pectin methylesterase. FEBS Lett.51, 243–249.

    Article  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Kilara, A. (1982) Enzymes and their uses in the processed apple industry: A Review. Proc. Biochem. 23, 35–41.

    Google Scholar 

  • Kita, N., Boyd, C.M., Garrett, M.R., Jurnak, F. and Keen, N.T. (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.

    Article  PubMed  CAS  Google Scholar 

  • Koller, A. and Neukom, H. (1967) Onteruschimgen uber den pektolytischen enzyme von Aspergillus niger. Mitt Geb Debensmittelunter Hug. 58, 512.

    Google Scholar 

  • Krebbers, B., Matser, A.M., Hoogerwerf, S.W., Moezelaar, R., Tomassen, M.M., Robert, W. and Vanden Berg, R.W. (2003) Combined high-pressure and thermal treatments for processing of tomato puree: evaluation of microbial inactivation and quality parameters. Innovative Food Sci. Emerg. Technol. 4, 377–385.

    Article  Google Scholar 

  • Lang, C. and Dörenberg, H. (2000) Perspective in the biological function and the technological applications of polygalacturonases. Appl. Microbiol. Biotechnol. 53, 366–375.

    Article  PubMed  CAS  Google Scholar 

  • Lietzke, S.E., Keen, N.T., Yoder, M.D. and Jurnak, F. (1994) The Three-Dimensional Structure of Pectate Lyase E, a Plant Virulence Factor from Erwinia chrysanthemi. Plant Physiol. 106, 849–862.

    PubMed  CAS  Google Scholar 

  • Lopez, P., Sanchez, A.C., Vercet, A. and Burgos, J. (1997) Thermal resistance of tomato polygalacturonase and pectinmethylesterase at physiological pH. Z. Lebensm.-Unters.-Forsch. A. 204, 146–150

    Article  CAS  Google Scholar 

  • Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and 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.

    Article  PubMed  CAS  Google Scholar 

  • Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., Pickersgill, R. and 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.

    Article  PubMed  CAS  Google Scholar 

  • McCarthy, R.E., Kotarski, S.F. and Salyers, A.A. (1985) Location and characteristics of enzymes involved in the breakdown of polygalacturonic acid by Bacteroides thetaiotaomicron.J. Bacteriol. 161, 493–499.

    PubMed  CAS  Google Scholar 

  • Moharib, S.A., El-Sayed, S.T. and Jwanny, E.W. (2000) Evaluation of enzymes produced from yeast. Nahrung. 44, 47–51.

    Article  PubMed  CAS  Google Scholar 

  • Naidu, G.S.N. and Panda, T. (1998a) Production of pectolytic enzymes – a review. Bioproc. Eng. 19, 355–361.

    Article  CAS  Google Scholar 

  • Naidu, G.S.N. and Panda, T. (1998b) Application of response surface methodology to evaluate some aspects of pectolytic enzymes from Aspergillus niger. Biochem. Engg. J. 2, 71–77.

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Naidu, G.S.N. and Panda, T. (1999b) Behaviour of pectinases under process conditions. Bioproc. Eng. 21, 397–400.

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Nakagawa, T., Miyaji, T., Yurimoto, H., Sakai, Y., Kato, N. and Tomizuka, M.A. (2000) Methylotrophic pathway participates in pectin utilization by Candida boidinii. Appl. Environ. Microbiol. 66, 4253–4257.

    Article  PubMed  CAS  Google Scholar 

  • Nedjma, M., Hoffmann, N. and Belari, A. (2001) Selective and sensitive detection of pectin lyase activity using a colorimetric test: Application to the screening of micro-organisms possessing pectin lyase activity. Anal. Biochem. 291, 290–296.

    Article  PubMed  CAS  Google Scholar 

  • Novoa De Armas, H., Verboven, C., De Ranter, C., Desair, J., Vande Broek, A., Vanderleyden, J. and Rabijns, A. (2004) Azospirillum irakense pectate lyase displays a toroidal fold. Acta Crystallogr D. 60, 999–1007.

    Article  PubMed  CAS  Google Scholar 

  • Pages, S., Heijne, W.H., Kester, H.C., Visser, J. and Benen, J.A. (2000) Subsite mapping of Aspergillus niger endopolygalacturonase II by site-directed mutagenesis. J. Biol. Chem. 275, 29348–29353.

    Article  PubMed  CAS  Google Scholar 

  • Pathak, N. and Sanwal, G.G. (1998) Multiple forms of polygalacturonase from banana fruits. Phytochem. 48, 249–255.

    Article  CAS  Google Scholar 

  • Petersen, S. (2001) Enzymes to upgrade plant nutrients. Feed Mix. 9, 12–15.

    CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  • Pilnik, W. and Voragen, A.G.J. (1993) Pectic enzymes in fruit juice and vegetable juice manufacture. In: Reeds, G. (Eds.), Food and Science Technology, Enzymes in Food Processing. Academic Press, New York, pp. 363–399 .

    Google Scholar 

  • Pressey, R. and Avants, J.K. (1975) Modes of action of carrot and peach exopolygalacturonases. Phytochem. 14, 957–961.

    Article  CAS  Google Scholar 

  • Preston, J.F., Rice, J.D., Ingram, L.O. and Keen, N.T. (1992) Differential depolymerization mechanisms of pectate lyases secreted by Erwinia chrysanthemiEC16. J. Bacteriol. 174, 2039–2042.

    PubMed  CAS  Google Scholar 

  • Rebeck, H. (1990) Processing of citrus juices. In: Hick, D. (Eds.), Production and Packaging of Non-Carbohydrate Fruit Juices and Fruit Beverages. Van Nosrand Reinhold, New York.

    Google Scholar 

  • Rombouts, F.M. and Pilnik, W. (1986) Pectinases and other cell-wall degrading enzymes of industrial importance. Symbiosis 2, 79–89.

    CAS  Google Scholar 

  • Sakiyama, C.C.H., Paula, E.M., Pereira, P.C., Borges, A.C. and Silva, D.O. (2001) Characterization of Pectin lyase produced by an endophytic strain isolated from coffee cherries. Lett. Appl. Microbiol 33, 117–121.

    Article  CAS  Google Scholar 

  • Salazar, L. and Jayasinghe, U. (1999) Fundamentals of purification of plant viruses. In: Techniques in plant virology CIP Training manual 5.0, Virus purification, International potato society, Peru, pp. 1–10. ISSN 0256 6311.

    Google Scholar 

  • Scavetta, R.D., Herron, S.R., Hotchkiss, A.T., Kita, N., Keen, N.T., Benen, J.A., Kester, H.C., Visser, J. and Jurnak, F. (1999) Structure of a plant cell wall fragment complexed to pectate lyase C. Plant Cell. 11, 1081–1092.

    Article  PubMed  CAS  Google Scholar 

  • Shimizu, T., Nakatsu, T., Miyairi, K., Okuno, T. and 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.

    Article  PubMed  CAS  Google Scholar 

  • Silva, D., Tokuioshi, K., Silva, E.D., SilvaMartins, R.D. and Gomes, E. (2005) Production of pectinases by solid state fermentation with Penicillium viridicatum RFC3. Proc. Biochem. 40, 2885–2889.

    Article  CAS  Google Scholar 

  • Singh, S.A. and Rao, A.G.A. (2002) 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.

    Article  PubMed  CAS  MathSciNet  Google Scholar 

  • Singh, S.A., Plattnera, H. and Diekmann, H. (1999) Exopolygalacturonate lyase from a thermophulic Bacillus sp. Enzyme Microbiol. Technol. 25, 420–425.

    Article  CAS  Google Scholar 

  • Soriano, M., Diaz, P. and Pastor, F.I.J. (2005) Pectinolytic systems of two aerobic sporogenous bacterial strains with high activity on pectin. Curr. Microbio. 50, 114–118.

    Article  CAS  Google Scholar 

  • 2Sozzi-Quiroga, G.O. and Fraschina, A.A. (1997) Evaluation of sensory attributes and biochemical parameters in transgenic tomato fruit with reduced polygalacturonase activity. Food Sci. Technol. Int. 3, 93–102.

    Article  CAS  Google Scholar 

  • Spiers, J.M., Braswell, J.M. and Hegwood, C.P. (1985) Establishment of rabbiteye blueberries. Mississippi Agr. Expt. Sta. Bul. 941.

    Google Scholar 

  • Takao, M., Nakaniwa, T., Yoshikawa, K., Terashita, T. and 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.

    Article  PubMed  CAS  Google Scholar 

  • Takebe, I., Otsuki, Y., Aoki, S. (1968) Isolation of tobacco mesophyll cells in intact and active state. Plant Cell Physiol. 9, 115.

    Google Scholar 

  • Tanabe, H., Yoshihara, K., Tamura, K., Kobayashi, Y., Akamatsu, I., Niyomwan, N. and Footrakul, P. (1987) Pretreatment of pectic wastewater from orange canning process by an alkalophilic Bacillus sp. J. Fermentation Technol. 65, 243–246.

    Article  CAS  Google Scholar 

  • Ten Have, A., Mulder, W., Visser, J. and Van Kan, J.A.L. (1998) The endopolygalacturonase gene Bcpg1 is required for full virulence of Botrytis cinerea. Mol. Plant Microbe. Interact. 11, 1084–1097.

    Article  Google Scholar 

  • Thomas, L.M., Doan, C.N., Oliver, R.L. and Yoder, M.D. (2002) Structure of pectate lyase A: comparison to other isoforms. Acta Crystallogr D. 58, 1008–1015.

    Article  PubMed  CAS  Google Scholar 

  • Truong, L.V., Tuyen, H., Helmke, E., Binh, L.T. and 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.

    Article  PubMed  CAS  Google Scholar 

  • Van Pouderoyen, G., Snijder, H.J., Benen, J.A. and Dijkstra, B.W. (2003) Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger. FEBS Lett. 554, 462–466.

    Article  PubMed  CAS  Google Scholar 

  • Van Santen, Y., Benen, J.A.E., Schroter, K.H., Kalk, K.H., Armand, S., Visser, J. and Dijkstra, B.W. (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.

    Article  PubMed  Google Scholar 

  • Vincent-Sealy, L.V., Thomas, J.D., Commander, P. and Salmond, G.P. (1999) Erwinia carotovora DsbA mutants: evidence for a periplasmic-stress signal transduction system affecting transcription of genes encoding secreted proteins. Microbiology. 145, 1945–1958.

    Article  PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  • Walkinshaw, M.D. and 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.

    Article  CAS  Google Scholar 

  • Walkinshaw, M.D. and 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.

    Article  CAS  Google Scholar 

  • Whitaker, J.R. (1984) Pectic substances, pectic enzymes and haze formation in fruit juices. Enzyme Microbial. Technol. 6, 341–347.

    Article  CAS  Google Scholar 

  • Whitaker, J.R. (1991) Microbial Enzymes and Biotechnology, Second edition. In: Fogarty, M. Kelly, C.T. (Eds.), Elsevier Applied Science, London, pp. 133–176.

    Google Scholar 

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

    Article  PubMed  ADS  CAS  Google Scholar 

  • Zheng, L., Du, Y. and Zhang, J. (2001) Degumming of ramie fibers by alkalophilic bacteria and their polysaccharide degrading enzymes. Bioresour. Technol. 78, 89–94

    Article  PubMed  ADS  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2007 Springer

About this chapter

Cite this chapter

Gummadi, S.N., Manoj, N., Kumar, D.S. (2007). Structural and Biochemical Properties of Pectinases. In: Polaina, J., MacCabe, A.P. (eds) Industrial Enzymes. Springer, Dordrecht. https://doi.org/10.1007/1-4020-5377-0_7

Download citation

Publish with us

Policies and ethics