Skip to main content
SpringerLink
Log in

Pectic Enzymes

  • Chapter
Food Enzymes

Abstract

Pectic enzymes constitute a unique group of enzymes that catalyze the degradation of pectic polymers in plant cell walls. Depolymerization of pectin is generally associated with the process of fruit ripening. These enzymes therefore play a significant role in the changes occurring in postharvest storage of fruits and vegetables. The control of these enzymes in transgenic tomato fruit has become one of the successful examples in the application of antisense RNA to manipulate gene expression (Kramer et al. 1990).

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

Access this chapter

Log in via an institution
eBook
USD 16.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 109.99
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

  • Ali, Z. M., and Brady, C. J. 1982. Purification and characterization of the polygalacturonases of tomato fruits. Aust. J. Plant Physiol. 9, 155–169.

    Article  CAS  Google Scholar 

  • Anderson M. M., and Nagel, C. W. 1964. Effect of the unsaturated bond on the degradation of the tetragalacturonic acids by a transeliminase. Nature 203, 649.

    Article  CAS  Google Scholar 

  • Baron, A.; Romœouts, F.; Drilleau, J. F.; and Pilnik, W. 1980. Purification et propriétés de la pectinestérase produite par Aspergillus niger. Lebensm-Wiss. u.-Technol. 13, 330–333.

    CAS  Google Scholar 

  • Barras, F.; Thurn, K. K.; and Chatterjee, A. K. 1987. Resolution of four pectate lyase structural genes of Erwinia chrysanthemi (EC16) and characterization of the enzymes produced in Escherichia coli. Mol. Gen. Genet. 209, 319–325.

    Article  CAS  Google Scholar 

  • BeMiller, J N 1986. An introduction to pectins: Structure and properties. In: Chemistry and Function of Pectins, M. L. Fishman and J. J. Jen, eds., A CS Sym. Ser. 310, American Chemical Society, Washington, D.C.

    Google Scholar 

  • BeMiller, J N, and Kumari, G. V. 1972. Beta-elimination in uronic acids: Evidence for an E1cB mechanism. Carbohydr. Res. 25, 419–428.

    Article  CAS  Google Scholar 

  • Bertheau, Y.; Madgidi-Hervan, E.; Kotoujansky, A.; Nguyen, The, C.; Andro, T.; and Coleno, A. 1984. Detection of depolymerase isoenzymes after electro- phoresis or electrofocusing, or in titration curves. Anal. Biochem. 139, 383–389.

    Google Scholar 

  • Brady, C. J. 1976. The pectinesterase of the pulp of the banana fruit. Aust. J. Plant PhysioL 3, 163–172.

    Article  CAS  Google Scholar 

  • Brady, C. J.; Macalpine, G.; Mcglasson, W. B.; and Ueda, Y. 1982. Polygalacturonase in tomato fruits and the induction of ripening. Aust. J. Plant Physiol. 9, 171–178.

    Article  CAS  Google Scholar 

  • Brown, S. M., and Crouch, M. L. 1990. Characterization of a gene family abundantly expressed in Oenothera organensis pollen that shows sequence similarity to polygalacturonase. The Plant Cell 2, 263–274.

    CAS  Google Scholar 

  • Bussink, H. J. D.; Kester, H. C. M.; and Visser, J. 1990. Molecular cloning; nucleotide sequence and expression of the gene encoding prepro-polygalacturonase II of Aspergillus niger. FEBS Lett. 273, 127–130.

    Article  CAS  Google Scholar 

  • Castaldo, D.; Quagliuolo, L.; Servillo, L.; Balestrieri, C., and Giovane, A. 1989. Isolation and characterization of pectin methylesterase from apple fruit. J. Food Sci. 54, 653–655.

    Article  CAS  Google Scholar 

  • Chesson, A., and Codner, R. C. 1978. The maceration of vegetable tissue by a strain of Bacillus subtilus. J. AppL BacterioL 44, 347–364.

    Article  CAS  Google Scholar 

  • Collmer, A., and Keen, N. T. 1986. The role of pectic enzymes in plant pathogenesis. Ann. Rev. PhytopathoL 24, 383–409.

    Article  CAS  Google Scholar 

  • Crawford, M. S., and Kolattukudy, P. E. 1987. Pectate lyase from Fusarium solani f. sp. pisi: Purification, characterization, in vitro translation of the mRNA, and involvement in pathogenicity. Arch. Biochem. Biophys. 258, 196–205.

    Article  CAS  Google Scholar 

  • Dave, B. A., and Vaughn, R. H. 1971. Purification and properties of a polygalacturonase acid trans-eliminase produced by Bacillus pumilus. J. Bacteriol. 108, 166–174.

    CAS  Google Scholar 

  • Dean, R. A., and Timberlake, W. E. 1989. Regulation of the Aspergillus nidulans pectate lyase gene (pelA). The Plant Cell 1, 275–284.

    CAS  Google Scholar 

  • DellaPenna, D., and Bennett, A. B. 1988. In vitro synthesis and processing of tomato fruit polygalacturonase. Plant Physiol. 86, 1057–1063.

    CAS  Google Scholar 

  • DellaPenna, D.; Lashbrook, C. C.; Toenjes, K.; Giovannori, J. J.; Fischer, R. L.; and Bennett, A. B. 1990. Polygalacturonase isozymes and pectin depolymerization in transgenic rin tomato fruit. Plant Physiol. 94, 1882–1886.

    Article  CAS  Google Scholar 

  • Demain, A. L., and Phaff, H. J. 1954. Hydrolysis of the oligogalacturonides and pectic acid by yeast. J. Biol. Chem. 210, 381–393.

    CAS  Google Scholar 

  • Doplco, B.; Lowe, A. L.; Wilson, I. D.; Merodio, C.; and Grierson, D. 1993. Cloning and characterization of avocado fruit mRNAs and their expression during ripening and low-temperature storage. Plant Mol. Biol. 21, 437–449.

    Article  Google Scholar 

  • Favey, S.; Bourbon, C.; Bertheau, Y.; Kotoujansky, A.; and Boccara, M. 1992. Purification of the acidic pectate lyase and nucleotide sequence of the corresponding gene (pelA) of Erwinia chrysanthemi strain 3937. J. Gen. Microbiol. 138, 499–508.

    Article  CAS  Google Scholar 

  • Forster, H., and Ranched, I. 1985. Purification and characterization of extracellular pectinesterases from Phytophthora infestans. Plant Physiol. 77, 109–112.

    Article  CAS  Google Scholar 

  • Garibaldi, A., and Bateman, D. F. 1971. Pectic enzymes produced by Erwinia chrysanthemi and their effects on plant tissue. Physiol. Plant Pathol. 1, 25–40.

    Article  CAS  Google Scholar 

  • Giovane, A.; Quagliuolo, L.; Castaldo, D.; Servillo, L.; and Balestrieri, C. 1990. Pectin methyl esterase from Actinidia chinensis fruits. Phytochemistry 29, 2821–2823.

    Article  CAS  Google Scholar 

  • Giovannoni, J. J.; DellaPenna, D.; Bennett, A. B.; and Fischer, R. L. 1989. Expression of a chimeric polygalacturonase gene in transgenic rin (ripening inhibitor) tomato fruit results in polyuronide degradation but not fruit softening. The Plant Cell 1, 53–63.

    CAS  Google Scholar 

  • Grierson, D.; Tucker, G. A.; Keen, J.; Ray, J.; Bird, C. R.; and Schuch, W. 1986. Sequencing and identification of a cDNA clone for tomato polygalacturonase. Nucl. Acids Res. 14, 8595–8603.

    Article  CAS  Google Scholar 

  • Harriman, R. W.; Tieman, D. M.; and Handa, A. K. 1991. Molecular cloning of tomato pectin methylesterase gene and its expression in Rutgers, ripening inhibitor, nonripening, and never ripe tomato fruits. Plant Physiol. 97, 80–87.

    Article  CAS  Google Scholar 

  • Hasegawa, S., and Nagel, C. W. 1962. The characterization of an a,ß-unsaturated digalacturonic acid. J. Biol. Chem. 237, 619–621.

    CAS  Google Scholar 

  • Hasegawa, S., and Nagel, C. W. 1966. A new pectic acid transeliminase produced exocellularly by a Bacillus. J. Food Sci. 31, 838–845.

    Article  CAS  Google Scholar 

  • Hsu, E. J., and Vaughn, R. H. 1969. Production and catabolite repression of the constitutive polygalacturonic acid trans-eliminase of Aeromonas liquefaciens. J. Bacteriol. 98, 172.

    CAS  Google Scholar 

  • Huang, J., and Schell, M. A. 1990. DNA sequence analysis of pglA and mechanisms of export of its polygalacturonase product from Pseudomonas solanacearum. J. Bacteriol. 172, 3879–3887.

    CAS  Google Scholar 

  • Huber, D. J. 1983. Polyuronide degradation and hemicellulose modifications in ripening tomato fruit. J. Am. Soc. Hort. Sci. 108, 405–409.

    CAS  Google Scholar 

  • Hugouvieux-Cotte-Pattat, N., and Robert-Baudouy, J. 1987. Hexuronate catabolism in Erwinia chrysanthemi. J. Bacteriol. 169, 1223–1231.

    CAS  Google Scholar 

  • Hultin, H. O.; Sun, B.; and Bulger, J. 1966. Pectin methyl esterases of the banana. Purification and properties. J. Food Sci. 31, 320–327.

    Article  CAS  Google Scholar 

  • Ishii, S.; Kiho, K.; Sugiyama, S.; and Sugimoto, H. 1979. Low-methoxyl pectin prepared by pectinesterase from Aspergillus japonicus. J. Food Sci. 44, 611–614.

    Article  CAS  Google Scholar 

  • Keen, N. T., and Tamaki, S. 1986. Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high-level expression in Escherichia coli. J. Bacteriol. 168, 595–606.

    CAS  Google Scholar 

  • Keubets, M. J. H., and Pilnik, W. 1974.13-Elimination of pectin in the presence of anions and cations. Carbohydr. Res. 33, 359–362.

    Google Scholar 

  • Keon, J. P. R., and Waksman, G. 1990. Common amino acid domain among endopolygalacturonases of Ascomycete fungi. Appl. Environ. Microbiol. 56, 2522–2528.

    CAS  Google Scholar 

  • Khanh, N. Q.; Albrecht, H.; Rutthowski, E.; Loffler, F.; Gottschalk, M.; and Jany K.-D. 1990. Nucleotide and derived amino acid sequence of a pectinesterase cDNA isolated from Aspergillus niger strain RH5344. Nucl. Acids Res. 18, 42–62.

    Article  Google Scholar 

  • Knegt, E.; Vermeer, E.; and Bruinsma, J. 1988. Conversion of the polygalacturonase isoenzymes from ripening tomato fruits. Physiologia Plantarum 72, 108–114.

    Article  CAS  Google Scholar 

  • Knegt, E.; Vermeer, E.; Pak, C.; and Bruinsma, J. 1991. Function of the polygalacturonase converter in ripening tomato fruit. Physiologia Plantarum 82,237–242.

    Google Scholar 

  • Kogoya, Y.; Setoguchi, M.; Yokohiki, K.; and Hatanaka, C. 1984. Affinity chromatography of exopolygalacturonate lyase from Erwinia carotovora subsp. carotovora. Agric. Biol. Chem. 48, 1055–1060.

    Article  Google Scholar 

  • Kohn, R.; Markovic, O.; and Machova, E. 1983. Deesterification mode of pectin by pectin esterases of Aspergillus foetidus, tomatoes and alfalfa. Collection Czechoslovak Chem. Comm. 48, 790–797.

    Article  CAS  Google Scholar 

  • Koller, A., and Neukom, H. 1969. Untersuchungen über den Abbaumechanisms. einer gereinigten polygalakturonase aus Aspergillus niger. Eur. J. Biochem. 7, 485–489.

    Article  CAS  Google Scholar 

  • Kramer, M.; Sanders, R. A.; Sheehy, R. E.; Melts, M.; Kuehn, M.; and Hiatt, W. R. 1990. Field evaluation of tomatoes with reduced polygalacturonase of antisense RNA. Plant Biol. 11 (Horticultural Biotechnology) 347–355.

    CAS  Google Scholar 

  • Lee, M., and Macmillan, J. D. 1968. Mode of action of pectic enzymes. I. Purification and certain properties of tomato pectinesterase. Biochemistry 7, 4005–4010.

    Article  CAS  Google Scholar 

  • Lei, S.-P.; Lin, H.-C.; Wang, S.-S.; Callaway, J.; and Wilcox, G. 1987. Characterization of the Erwinia carotovora pelB gene and its product pectate lyase. J. Bacteriol. 169, 4379–4383.

    CAS  Google Scholar 

  • Liao, C.-H. 1991. Cloning of pectate lyase gene pel from Pseudomonas fluorescens and detection of sequences homologous to pel in Pseudomonas viridafiava and Pseudomonas putida. J. Bacteriol. 173, 4386–4393.

    CAS  Google Scholar 

  • Liao, C.-H.; Hung, H. Y.; and Chatteriee, A. K. 1988. An extracellular pectate lyase is the pathogenicity factor of the soft-rotting bacterium Pseudomonas viridiliava. Mol. Plant-Microbe Interact. 1, 199–206.

    Article  Google Scholar 

  • Liu, Y. K., and Lux, B. S. 1978. Purification and characterization of endo-polygalacturonase from Rhizopus arrhizus 1. Food Sci. 43, 721–726.

    Article  CAS  Google Scholar 

  • Markovic, O., and Jornvall, H. 1986. Pectinesterase. The primary structure of the tomato enzyme. Eur. J. Biochem. 158, 455–462.

    Article  CAS  Google Scholar 

  • Markovic, O., and Jornvall, H. 1992. Disulfide bridges in tomato pectinesterase: Variations from pectinesterases of other species; conservation of possible active site segments. Protein Science 1, 1288–1292.

    Article  CAS  Google Scholar 

  • Markovic, O., and Kohn, R. 1984. Mode of pectin deesterification by Trichoderma reesei pectinesterase. Experientia 40, 842–843.

    Article  CAS  Google Scholar 

  • Markovic, O., and Patocka, J. 1977. Action of iodine on the tomato pectinesterase. Experientia 33, 711–713.

    Google Scholar 

  • Martinez, M. J.; Alconada, M. T.; Guillen, F.; Vazquez, C.; and Reyes, F. 1991. Pectic activities from Fusarium oxysporum f. sp. melons: Purification and characterization of an exopolygalacturonase. FEMS Microbiol. Lett. 81, 145–150.

    Article  CAS  Google Scholar 

  • Matsui, I.; Ishikawa, K.; Miyairi, S.; Fuxui, S.; and Honda, K. 1992a. A mutant a-amylase with enhanced activity specific for short substrates. Biochemistry 31, 5232–5236.

    Article  CAS  Google Scholar 

  • Matsui, I.; Ishikawa, K.; Miyairi, S.; Fuxui, S.; and Honda, K. 1992b. Alteration of bond-cleavage pattern in the hydrolysis catalyzed by Saccharomycopsis a-amylase altered by site-directed mutagenesis. Biochemistry 31, 5232–5236.

    Article  CAS  Google Scholar 

  • Miyazaki, Y. 1991. Purification and characterization of endo-pectate lyase from Bacillus macerans. Agric. Biol. Chem. 55, 25–30.

    Article  CAS  Google Scholar 

  • Moshrefi, M., and Lux, B. S. 1983. Carbohydrate composition and electrophoretic properties of tomato polygalacturonase isoenzymes. Eur. J. Biochem. 135, 511–514.

    Article  CAS  Google Scholar 

  • Moustacas, A.-M.; Nabi, J.; Diamantidis, G.; Noat, G.; and Crasnier, M. 1986. Electrostatic effects and the dynamics of enzyme reactions at the surface of plant cells. 2. The role of pectin methyl esterase in the modulation of electrostatic effects in soybean cell walls. Eur. J. Biochem. 155, 191–197.

    Article  CAS  Google Scholar 

  • Nari, J.; Noat, G.; and Ricard, J. 1991. Pectin methylesterase, metal ions and plant cell-wall extension. Biochem. J. 279, 343–350.

    CAS  Google Scholar 

  • Nasser, W.; Chalet, F.; and Robert-Baudouy, J. 1990. Purification and characterization of extracellular pectate lyase from Bacillus subtilis. Biochimie 72, 689–695.

    Article  CAS  Google Scholar 

  • Nasuno, S., and Starr, M. P. 1967. Polygalacturonic acid trans-eliminase of Xanthomonas campestris. Biochem. J. 104, 178.

    CAS  Google Scholar 

  • Niogret, M.-F.; Dubald, M.; Mandaron, P.; and Mache, R. 1991. Characterization of pollen polygalacturonase encoded by several cDNA clones in maize. Plant Mol. Biol. 17, 1155–1164.

    Article  CAS  Google Scholar 

  • Patel, D. S., and Phaff, H. J. 1959. On the mechanism of action of yeast endopolygalacturonase on oligogalacturonides and their reduced and oxidized derivatives. J. Biol. Chem. 234, 237–241.

    CAS  Google Scholar 

  • Perombelon, M. C. M., and Kelman, A. 1980. Ecology of the soft rot Erwinias. Ann. Rev. Phytopathol. 18, 361–387.

    Article  Google Scholar 

  • Pilnik, W., and Rombouts, F. M. 1979. Ultilization of pectic enzymes in food production. In: Proceedings of the Fifth Internal Congress of Food Science and Technology, Hideochiba, ed., Kodansha, Ltd., and Elsevier Scientific Publ. Co.

    Google Scholar 

  • Pilnik, W., and Voragen, A. G. J. 1993. Pectic enzymes in fruit and vegetable juice manufacture. In: Enzymes in Food Processing. 3d ed., T. Nagodawithana and G. Reed, eds., Academic Press, New York and San Diego.

    Google Scholar 

  • Plastow, G. S. 1988. Molecular cloning and nucleotide sequence of the pectin methyl esterase gene of Erwinia chrysanthemi B374. Mol. Microbiol. 2, 247–254.

    Article  CAS  Google Scholar 

  • Pogson, B. J.; Brady, C. J.; and Orr, G. R. 1991. On the occurrence and structure of subunits of endopolygalacturonase isoforms in mature-green and ripening tomato fruits. Aust. J. Plant Physiol. 18, 65–79.

    Article  CAS  Google Scholar 

  • Polizeli, M. L. T. M.; Jorge, J. A.; and Terenzi, H. F. 1991. Pectinase production by Neurospora crassa: Purification and biochemical characterization of extra-cellular polygalacturonase activity. J. Gen. Microbiol. 137, 1815–1823.

    Article  CAS  Google Scholar 

  • Pressey, R. 1986. Changes in polygalacturonase isoenzymes and converter in tomatoes during ripening. HortScience 21, 1183–1185.

    CAS  Google Scholar 

  • Pressey, R. 1988. Reevaluation of the changes in polygalacturonases in tomatoes during ripening. Planta 174, 39–43.

    Article  CAS  Google Scholar 

  • Pressey, R., and Avants, J. K. 1973. Two forms of polygalacturonase in tomatoes. Biochim. Biophys. Acta 309, 363–369.

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Preston III, J. F.; Rice, J. D.; Chow, M. C.; and Brown, B. J. 1991. Kinetic comparisons of trimer-generating pectate and alginate lyases by reversed-phase ion-pair liquid chromatography. Carbohydr. Res. 215, 147–157.

    Article  CAS  Google Scholar 

  • Preston III, J. F.; Rice, J. D.; Ingram, L. O.; and Keen, N. T. 1992. Differential depolymerization mechanisms of pectate lyases secreted by Erwinia chrysanthemi EC16. J. Bacteriol. 174, 2039–2042.

    CAS  Google Scholar 

  • Pupillo, P.; Mazzucchi, U.; and Pierini, G. 1976. Pectic lyase isozymes produced by Erwinia chrysanthemi Burkh. et al. in polypectate broth or in Dieffenbachia leaves. Physiol. Plant Pathol. 9, 113–120.

    Article  CAS  Google Scholar 

  • Quantick, P.; Cervone, F.; and Wood, R. K. S. 1983. Isoenzymes of a polygalacturonate trans-eliminase produced by Erwinia atroseptica in potato tissue and in liquid culture. Physiol. Plant Pathol. 22, 77–86.

    CAS  Google Scholar 

  • Ray, J.; Knapp, J.; Grierson, D.; Bird, C.; and Schuch, W. 1988. Identification and sequence determination of a cDNA clone for tomato pectin esterase. Eur. J. Biochem. 174, 119–124.

    Article  CAS  Google Scholar 

  • Reverchon, S.; Huang, Y.; Bourson, C.; and Robert-Baudouy, J. 1989. Nucleotide sequences of Erwinia chrysanthemi ogl and pelE genes negatively regulated by the kdgR gene product. Gene 85, 125–134.

    Article  CAS  Google Scholar 

  • Rexova-Benkova, L., and Markovic, O. 1976. Pectic enzymes. Adv. Carbohydr. Chem. Biochem. 33, 323–385.

    Article  CAS  Google Scholar 

  • Ruttkowski, E.; Labitzke, R.; Khanh, N. W.; Loffler, F.; Gottschalk, M.; and Jany, K.-D. 1990. Cloning and DNA sequence analysis of a polygalacturonase cDNA from Aspergillus niger RH5344. Biochim. Biophys. Acta 1087, 104–106.

    Article  CAS  Google Scholar 

  • Sakellaris, G.; Níkdlaropoulqb, S.; and Evangelopoulos, A. E. 1989. Purification and characterization of an extracellular polygalacturonase from Lactobacillus plantarum strain BA11. J. Appl. Bacteriol. 67, 77–85.

    Article  CAS  Google Scholar 

  • Scott-Craig, J. S.; Panaccione, D. G.; Cervone, F.; and Walton, J. D. 1990. Endopolygalacturonase is not required for pathogenicity of Cochliobolus car-bonum on maize. The Plant Cell 2, 1191–1200.

    CAS  Google Scholar 

  • Sheehy, R. E.; Pearson, J.; Bardy, C. J.; and Hiatt, W. R. 1987. Molecular characterization of tomato fruit polygalacturonase. Mol. Gen. Genet. 208, 30–36.

    Article  CAS  Google Scholar 

  • Spok, A.; Stubenrauch, G.; Schorgendorfer, K.; and Schwab, H. 1991. Molecular cloning and sequencing of a pectinesterase gene from Pseudomonas solanacearum. J. Gen. Microbiol. 137, 131–140.

    Article  CAS  Google Scholar 

  • Sugiura, J.; Yasuda, M.; Kamimiya, S.; Izaki, K., and Takahashi, H. 1984. Purification and properties of two pectate lyases produced by Erwinia carotovora. J. Gen. Appl. Microbiol. 30, 167–175.

    Article  CAS  Google Scholar 

  • Tamaki, S. J.; Robeson, G. M.; Manulis, S.; and Keen, N. T. 1988. Structure and organization of the pel genes from Erwinia chrysanthemi EC16. J. Bacteriol. 170, 3468–3478.

    CAS  Google Scholar 

  • Tanabe, H.; Kobayashi, Y.; Matuo, Y.; Nishi, N., and Wada, F. 1984. Isolation and fundamental properties of endo-pectate lyase pI — isozymes from Erwinia carotovara. Agric. Biol. Chem. 48, 2113–2120.

    Article  CAS  Google Scholar 

  • Termote, F.; Rombouts, F. M.; and Pilniki, W. 1977. Stabilization of cloud in pectinesterase active orange juice by pectic acid hydrolysates. J. Food Biochem. 1, 15–34.

    Article  CAS  Google Scholar 

  • Tucker, G. A.; Robertson, N. G.; and Grierson, D. 1980. Changes in polygalacturonase isoenzymes during the “ripening” of normal and mutant tomato fruit. Eur. J. Biochem. 112, 119–124.

    Article  CAS  Google Scholar 

  • Tucker, G. A.; Robertson, N. G.; and Grierson, D. 1981. The conversion of tomato-fruit polygalacturonase isoenzyme 2 into isoenzyme 1 in vitro. Eur. J. Biochem. 115, 87–90.

    Article  CAS  Google Scholar 

  • Tucker, G. A.; Robertson, N. G.; and Grierson, D. 1982. Purification and changes in activities of tomato pectinesterase isoenzymes. J. Sci. Food Agric. 33, 396–400.

    Article  CAS  Google Scholar 

  • Van Gijsegem, F. 1986. Analysis of the pectin-degrading enzymes secreted by three strains of Erwinia chrysanthemi. J. Gen. Microbiol. 132, 617–624.

    Google Scholar 

  • Versteeg, C.; Rombouts, F. M.; and Pilnik, W. 1978. Purification and some characteristics of two pectinesterase isoenzymes from orange. Lebensm-Wiss. u.Technol. 11, 267–274.

    CAS  Google Scholar 

  • Voragen, A. G. J.; Schols, H. A.; Siliha, H. A. I.; and Pilnik, W. 1986. Enzymic lysis of pectic substances in cell walls: Some implications for fruit juice technology. In: Chemistry and Function of Pectins, M. L. Fishman, and J. J. Jen, eds., ACS Sym. Ser. 310, American Chemical Society, Washington, D.C.

    Google Scholar 

  • Yoder, M. D.; Dechaine, D. A.; and Jurnak, F. 1990. Preliminary crystallographic analysis of the plant pathogenic factor, pectate lyase C from Erwinia chrysanthemi. J. Biol. Chem. 265, 11429–11431.

    CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Yoder, M. D.; Lietzke, S. E.; and Jurnak, F. 1994. Unusual structural features in the parallel 0-helix in pectate lyases. Structure 1, 241–251.

    Article  Google Scholar 

  • Yoshida, A.; Ito, K.; Kamio, Y.; and Izaki, K. 1991A. Purification and properties of pectate lyase III of Erwinia carotovora Er. Agric. Biol. Chem. 55,601–602.

    Google Scholar 

  • Yoshida, A.; Izuta, M.; Ito, K.; Kamio, Y.; and Izaki, K. 1991B. Cloning and characterization of the pectate lyase III gene of Erwinia carotovora Er. Agric. Biol. Chem. 55, 933–940.

    Google Scholar 

  • Zheng, L.; Heupel, R. C.; and DellaPenna, D. 1992. The ß subunit of tomato fruit polygalacturonase isoenzyme 1: Isolation, characterization, and identification of unique structural features. The Plant Cell 4, 1147–1156.

    CAS  Google Scholar 

Download references

Authors
  1. Dominic W. S. Wong
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 1995 Springer Science+Business Media Dordrecht

About this chapter

Cite this chapter

Wong, D.W.S. (1995). Pectic Enzymes. In: Food Enzymes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2349-6_7

Download citation

  • DOI: https://doi.org/10.1007/978-1-4757-2349-6_7

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4419-4722-2

  • Online ISBN: 978-1-4757-2349-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation