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Microbial pectate lyases: characterization and enzymological properties


Pectate lyase plays an important role in plant pathogenesis. The enzyme is widely distributed in diverse families of microorganisms. The current knowledge including biochemical studies on microbial pectate lyases, such as isozymes, structure, reaction mechanism, purification and properties like molecular mass, pI, optimum pH and temperature, substrate specificity, metal ion requirement, inhibitors and activators, and kinetic parameters of the enzyme are reviewed.

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  1. Abbott DW, Boraston AB (2007) A family 2 pectate lyase displays a rare fold and transition metal-assisted β-elimination. J Biol Chem 282:35328–35336. doi:10.1074/jbc.M705511200

  2. Akita M, Suzuki A, Kobayashi T, Ito S, Yamane T (2001) The first structure of pectate lyase belonging to polysaccharide lyase family 3. Acta Crystallogr 57:1786–1792

  3. Barras F, Thurn KK, Chatterjee AK (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. doi:10.1007/BF00329660

  4. Barras F, Van Gijsegem F, Chatterjee AK (1994) Extracellular enzymes and pathogenesis of soft-rot Erwinia. Annu Rev Phytopathol 32:201–234

  5. Beaulieu C, Boccara M, Van Gijsegem F (1993) Pathogenic behavior of pectinase-defective Erwinia chrysanthemi mutants on different plants. Mol Plant Microbe Interact 6:197–202

  6. Bekri MYA, Desair J, Keijers V, Proost P, Leeuwen MS-V, Vanderleyden J, Broek AV (1999) Azospirillum irakense produces a novel type of pectate lyase. J Bacteriol 181:2440–2447

  7. Benen JAE, Kester HCM, Parenicova L, Visser J (2000) Characterization of Aspergillus niger pectate lyase A. Biochemistry 39:15563–15569. doi:10.1021/bi000693w

  8. Berensmeier S, Singh SA, Meens J, Buchholz K (2004) Cloning of the pelA gene from Bacillus licheniformis 14A and biochemical characterization of recombinant, thermostable, high-alkaline pectate lyase. Appl Microbiol Biotechnol 64:560–567. doi:10.1007/s00253-003-1446-9

  9. Boccara M, Diolez A, Rouve M, Kotoujansky A (1988) The role of individual pectate lyases of Erwinia chrysanthemi strain 3937 in pathogenicity on Saintpaulia plants. Physiol Mol Plant Pathol 33:95–104. doi:10.1016/0885-5765(88)90046-X

  10. Brooks AD, He SY, Gold S, Keen NT, Collmer A, Hutcheson SW (1990) Molecular cloning of the structural gene for exopolygalacturonate lyase from Erwinia chrysanthemi EC16 and characterization of the enzyme product. J Bacteriol 172:6950–6958

  11. 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. doi:10.1042/0264-6021:3550155

  12. Brühlmann F (1995) Purification and characterization of an extracellular pectate lyase from an Amycolata sp. Appl Environ Microbiol 61:3580–3585

  13. Brühlmann F, Keen NT (1997) Cloning, sequence and expression of the pel gene from an Amycolata sp. Gene 202:45–51. doi:10.1016/S0378-1119(97)00449-6

  14. Bush DA, Codner RC (1970) Comparison of the properties of the pectin trans-eliminases of Penicillium digitatum and Penicillium italicum. Phytochemistry 9:87–97. doi:10.1016/S0031-9422(00)86618-2

  15. Chatterjee AK, Buchanan GE, Behrens MK, Starr MP (1979) Synthesis and excretion of polygalacturonic acid-trans-eliminase in Erwinia, Yersinia and Klebsiella species. Can J Microbiol 25:94–102

  16. Collmer A, Keen T (1986) The role of pectic enzymes in plant pathogenesis. Annu Rev Phytopathol 24:383–409. doi:10.1146/

  17. Collmer A, Whalen CH, Beer SV, Bateman DF (1982) An Exo-poly-α-d-galacturonosidase implicated in the regulation of extracellar pectate lyase production in Erwinia chrysanthemi. J Bacteriol 149:626–634

  18. Collmer A, Ried JL, Mount MS (1988) Assay methods for pectic enzymes. In: Wood WA, Kellogg ST (eds) Methods in enzymology, vol 161. Academic Press, San Diego, pp 329–335

  19. Colloc’h N, Cohen FE (1991) β-breakers: an aperiodic secondary structure. J Mol Biol 221:603–613

  20. Coutinho PM, Henrissat B (2000) Carbohydrate-active enzymes: a integrated data base approach. In: Gilbert HJ, Davies GJ, Henrissat B, Svenson B (eds) Recent advances in carbohydrate bioengineering. Royal Society of Chemistry, Cambridge, pp 3–12

  21. Crawford MS, Kolattukudy PE (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. doi:10.1016/0003-9861(87)90336-5

  22. Dehdashti SJ, Doan CN, Chao KL, Yoder MD (2003) Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16. Acta Crystallogr 59:1339–1342

  23. Dixit VS, Kumar AR, Pant A, Khan MI (2004) Low molecular mass pectate lyase from Fusarium moniliforme: similar mode of chemical and thermal denaturation. Biochem Biophys Res Commun 315:477–484. doi:10.1016/j.bbrc.2004.01.083

  24. Domingo C, Roberts K, Stacey NJ, Connerton I, Ruiz-Teran F, McCann MC (1998) A pectate lyase from Zinnia elegans is auxin inducible. Plant J 13:17–28. doi:10.1046/j.1365-313X.1998.00002.x

  25. Edstrom RD, Phaff HJ (1964) Purification and certain properties of pectin trans-eliminase from Aspergillus fonsecaeus. J Biol Chem 239:2403–2408

  26. Famurewa O, Oyede MA, Olutiola PO (1993) Pectin transeliminase complex in culture filterates of Aspergillus flavus. Folia Microbiol (Praha) 38:459–466. doi:10.1007/BF02814396

  27. Favey S, Bourson C, Bertheau Y, Kotoujansky A, 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

  28. Gardner JM, Kado DI (1976) Polygalacturonic acid trans-eliminase in the osmotic shock fluid of Erwinia rubrifaciens: characterization of the purified enzyme and its effect on plant cells. J Bacteriol 127:451–460

  29. Gonzalez-Candelas L, Kolattukudy PE (1992) Isolation and analysis of a novel inducible pectate lyase gene from the phytopathogenic fungus Fusarium solani f. sp. pisi (Nectria haematococca, mating population VI). J Bacteriol 174:6343–6349

  30. Guo W, Gonzalez-Candelas L, Kolattukudy PE (1995) Cloning of a novel constitutively expressed pectate lyase gene pelB from Fusarium solani f. sp. pisi (Nectria haematococca, mating type VI) and characterization of the gene product expressed in Pichia pastoris. J Bacteriol 177:7070–7077

  31. Hasegawa S, Nagel CW (1962) The characterization of an α,β-unsaturated digalacturonic acid. J Biol Chem 237:619–621

  32. Hatada Y, Higaki N, Saito K, Ogawa A, Sawada K, Ozawa T, Hakamada Y, Kobayashi T, Ito S (1999) Cloning and sequencing of a high alkaline pectate lyase gene from an alkaliphilic Bacillus isolate. Biosci Biotechnol Biochem 63:998–1005. doi:10.1271/bbb.63.998

  33. Hatada Y, Saito K, Koike K, Yoshimatsu T, Ozawa T, Kobayashi T, Ito S (2000) Deduced amino-acid sequence and possible catalytic residues of a novel pectate lyase from an alkaliphilic strain of Bacillus. Eur J Biochem 267:2268–2275. doi:10.1046/j.1432-1327.2000.01243.x

  34. Hatada Y, Kobayashi T, Ito S (2001) Enzymatic properties of the highly thermophilic and alkaline pectate lyase Pel-4B from alkaliphilic Bacillus sp. strain P-4-N and the entire nucleotide and amino acid sequences. Extremophiles 5:127–133. doi:10.1007/s007920100182

  35. 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. doi:10.1016/S0031-9422(97)00191-X

  36. Herron SR, Benen JAE, Scavetta RD, Visser J, Jurnak F (2000) Structure and function of pectic enzymes: virulence factors of plant pathogens. Proc Natl Acad Sci USA 97:8762–8769. doi:10.1073/pnas.97.16.8762

  37. 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. doi:10.1074/jbc.M209306200

  38. Hinton JCD, Sidebotham JM, Gill DR, Salmond GPC (1989) Extracellular and periplasmic isoenzymes of pectate lyase from Erwinia carotovora subspecies carotovora belong to different gene families. Mol Microbiol 3:1785–1795. doi:10.1111/j.1365-2958.1989.tb00164.x

  39. Hla SS, Takuma K, Sakka M, Kimura T, Sakka K (2006) Enzymatic properties of two catalytic modules of Clostridium stercorarium pectate lyase Pel 9A. Biosci Biotechnol Biochem 70:667–671. doi:10.1271/bbb.70.667

  40. Huertas-Gonzàlez MD, Ruiz-Roldan MC, Garcia-Marceira FI, Roncero MI, Di-Pietro A (1999) Cloning and characterization of pl 1 encoding an in planta-secreted pectate lyase of Fusarium oxysporum. Curr Genet 35:36–40. doi:10.1007/s002940050430

  41. Hugouvieux-Cotte-Pattat N, Dominguez H, Robert-Baudouy J (1994) Environmental conditions affect the transcription of the pectinase gene of Erwinia chrysanthemi 3937. J Bacteriol 174:7806–7818

  42. Hugouvieux-Cotte-Pattat N, Condemine G, Nasser W, Reverchon S (1996) Regulation of pectinolysis in Erwinia chrysanthemi. Annu Rev Microbiol 50:213–257. doi:10.1146/annurev.micro.50.1.213

  43. Hurlbert JC, Preston JF (2000) Functional implication of the β-helical protein fold: differences in chemical and thermal stabilities of Erwinia chrysanthemi EC 16 pectate lyase B, C and E. Arch Biochem Biophys 381:264–272. doi:10.1006/abbi.2000.1982

  44. Ikotun T (1984) Cell wall degrading enzymes produced by Penicillium oxalicum. Mycopathologia 85:15–21

  45. Jenkins J, Shevchik VE, Hugouvieux-Cotte-Pattat N, Pickersgill RW (2004) The crystal structure of pectate lyase Pel9A from Erwinia chrysanthemi. J Biol Chem 279:9139–9145. doi:10.1074/jbc.M311390200

  46. Kamimiya S, Itoh Y, Izaki K, Takahashi H (1997) Purification and properties of pectate lyase in Erwinia aroideae. Agric Biol Chem 41:975–981

  47. Karaveg K, Siriwardena A, Tempel W, Liu ZJ, Glushka J, Wang BC, Moremen KW (2005) Mechanism of class 1 (glycosylhydrolase family 47) α-mannisidases involved in N-glycan processing and endoplasmic reticulum quality control. J Biol Chem 280:16197–16207. doi:10.1074/jbc.M500119200

  48. Karbassi A, Vaughn RH (1980) Purification and properties of polygalacturonic acid trans-eliminase from Bacillus stearothermophilus. Can J Microbiol 26:377–384

  49. Kegoya Y, Setoguchi M, Yokohiki K, Hatanaka C (1984) Affinity chromatography of exopolygalacturonate lyase from Erwinia carotovora sub sp. carotovora. Agric Biol Chem 48:1055–1060

  50. Kikuchi T, Shibuya H, Aikawa T, Jones JT (2006) Cloning and characterization of pectate lyases expressed in the esophageal gland of the pine wood nematode Bursaphelenchus xylophilus. Mol Plant Microbe Interact 19:280–287. doi:10.1094/MPMI-19-0280

  51. Kita N, Boyd CM, Garrett MR, Jurnak FJ, Keen NT (1996) Differential effect of site-directed mutations in pelC on pectate lyase activity, plant tissue maceration, and elicitor activity. J Biol Chem 271:26529–26535. doi:10.1074/jbc.271.43.26529

  52. Klug-Santner BG, Schnitzhofer W, Vršanská M, Weber J, Agrawal PB, Nierstrasz VA, Guebitz GM (2006) Purification and characterization of a new bioscouring pectate lyase from Bacillus pumilus BK2. J Biotechnol 121:390–401. doi:10.1016/j.jbiotec.2005.07.019

  53. Kluskens LD, VanAlebeek GJWM, Voragen AGJ, DeVos WM, Vander Oost J (2003) Molecular and biochemical characterization of the thermoactive family 1 pectate lyase from the hyperthermophilic bacterium Thermotoga maritima. Biochem J 370:651–659. doi:10.1042/BJ20021595

  54. Kobayashi T, Hatada Y, Higaki N, Lusterio DD, Ozawa T, Koike K, Kawai S, Ito S (1999a) Enzymatic properties and deduced amino acid sequence of a high-alkaline pectate lyase from an alkaliphilic Bacillus isolate. Biochim Biophys Acta 1427:145–154

  55. Kobayashi T, Koike K, Yoshimatsu T, Higaki N, Suzumatsu A, Ozawa T, Hatada Y, Ito S (1999b) Purification and properties of a low-molecular-weight, high-alkaline pectate lyase from an alkaliphilic strain of Bacillus. Biosci Biotechnol Biochem 63:65–72. doi:10.1271/bbb.63.65

  56. Kotoujansky A (1987) Molecular genetics of pathogenesis by soft-rot Erwinias. Annu Rev Phytopathol 25:405–430. doi:10.1146/

  57. Kozianowski G, Canganella F, Rainey FA, Hippe H, Antranikian G (1997) Purification and characterization of thermostable pectate-lyases from a newly isolated thermophilic bacterium, Thermoanaerobacter italicus sp. nov. Extremophiles 1:171–182

  58. Liao C-H (1989) Analysis of pectate lyases produced by soft rot bacteria associated with spoilage of vegetables. Appl Environ Microbiol 55:1677–1683

  59. Liao C-H, Chatterjee AK (1988) An extracellular pectate lyase is the pathogenicity factor of the soft-rotting bacterium Pseudomonas viridi-flava. Mol Plant Microbe Interact 1:199–206

  60. Liao C-H, Wells JM (1986) Properties of Cytophaga johansonae strains causing spoilage of fresh produce at food markets. Appl Environ Microbiol 52:1261–1265

  61. Liao C-H, Sullivan J, Grady J, Wong L-JC (1997) Biochemical characterization of pectate lyases produced by fluorescent Pseudomonads associated with spoilage of fresh fruits and vegetables. J Appl Microbiol 83:10–16. doi:10.1046/j.1365-2672.1997.00158.x

  62. Liao C-H, William F, Sean-Shong T, Gabriel H (2006) Detection and sequence analysis of an altered pectate lyase gene in Pseudomonas syringae pv. glycinea and related bacteria. Can J Microbiol 52:1051–1059. doi:10.1139/W06-063

  63. 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

  64. Lojkowska EC, Reignault DP, Hugouvieux-Cotte-Pattat N, Robert-Baudouy J (1993) Use of GUS fusions to study the expression of Erwinia chrysanthemi pectinase genes during infection of potato tubers. Mol Plant Microbe Interact 6:488–494

  65. Macmillan JD, Vaughn RH (1964) Purification and properties of polygalacturonic acid trans-eliminase produced by Clostridium multifermentas. Biochemistry 3:564–572. doi:10.1021/bi00892a016

  66. Maŕin-Rodriguez MC, Smith DL, Manning K, Orchard L, Seymour GB (2003) Pectate lyase gene expression and enzyme activity in ripening banana fruit. Plant Mol Biol 51:851–857

  67. Masclaux C, Hugouvieux-Cotte-Pattat N, Expert D (1996) Iron is a triggering factor for differential expression of Erwinia chrysanthemi strain 3937 pectate lyases in pathogenesis of African violets. Mol Plant Microbe Interact 9:198–205

  68. 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

  69. Miyairi K, Ogasawara A, Tonouchi A, Hosaka K, Kudou M, Okuno T (2004) Low-molecular-weight pectate lyase from Streptomyces thermocarboxydus. J Appl Glycosci 51:1–7

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

  71. Nasser W, Awade AC, Reverchon S, Robert-Baudouy J (1993) Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme. FEBS Lett 335:319–326

  72. Nasuno S, Starr MP (1966) Pectic enzymes of Pseudomonas marginalis. Phytopathology 56:1414–1415

  73. Nasuno S, Starr MP (1967) Polygalacturonic acid transeliminase of Xanthomonas campestris. Biochem J 104:178–185

  74. Payasi A, Sanwal GG (2003) Pectate lyase activity during ripening of banana fruit. Phytochemistry 63:243–248

  75. Payasi A, Misra PC, Sanwal GG (2006) Purification and characterization of pectate lyase from banana (Musa acuminata) fruits. Phytochemistry 67:861–869

  76. 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

  77. Pissavin C, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1996) Regulation of pelZ, a gene of the pelB-pelC cluster encoding a new pectate lyase of Erwinia chrysanthemi 3937. J Bacteriol 178:7187–7196

  78. Pissavin C, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1998) Biochemical characterization of the pectate lyase Pel Z of Erwinia chrysanthemi 3937. Biochim Biophys Acta 1383:188–196

  79. Preston JF, Rice JD, Ingram LO, Keen NT (1992) Differential depolymerization mechanisms of pectate lyases secreted by Erwinia chrysanthemi EC16. J Bacteriol 174:2039–2042

  80. Pua EC, Ong CK, Liu P, Liu JZ (2001) Isolation and expression of two pectate lyase genes during fruit ripening of banana (Musa acuminata). Physiol Plant 113:92–99

  81. Quantick P, Cervone F, Wood RKS (1983) Isoenzymes of a polygalacturonate trans-eliminase produced by Erwinia attroseptica in potato tissue and in liquid culture. Physiol Plant Pathol 22:77–86

  82. Rao MN, Kembhavi AA, Pant A (1996) Role of lysine, tryptophan and calcium in the β-elimination activity of a low-molecular mass pectate lyase from Fusarium moniliformae. Biochem J 319:159–164

  83. Sato M, Kaji A (1975) Purification and properties of pectate lyase produced by Streptomyces fradie IFO 3439. Agric Biol Chem 39:819–824

  84. Sato M, Kaji A (1977) Purification and properties of pectate lyase produced by Streptomyces nitrosporeus. Agric Biol Chem 41:2193–2197

  85. Sawada K, Ogawa A, Ozawa T, Sumitomo N, Hatada Y, Kobayashi T, Ito S (2000) Nucleotide and amino acid sequence of a new type pectate lyase from alkaliphillic strain of Bacillus. Eur J Biochem 267:1510–1515

  86. Shevchik VE, Bortoli-Gernnan I, Robert-Baudouy J, Robinet S, Barras F, Condemine G (1995) Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi. Mol Microbiol 16:745–753

  87. Shevchik VE, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1997) Pectate lyase PelI of Erwinia chrysanthemi 3937 belongs to a new family. J Bacteriol 179:7321–7330

  88. Shevchik VE, Kester HCM, Benen JAE, Visser J, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1999a) Characterization of the exopolygalacturonate lyase PelX of Erwinia chrysanthemi 3937. J Bacteriol 181:1652–1663

  89. Shevchik VE, Condemine G, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1999b) The exopolygalacturonate lyase PelW and oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J Bacteriol 181:3912–3919

  90. Soriano M, Blanco A, Diaz P, Pastor FIJ (2000) An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization. Microbiology 146:89–95

  91. Soriano M, Diaz P, Pastor FIJ (2006) Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin. Microbiology 152:617–625

  92. Starr ME, Moran P (1962) Eliminative split of pectic substances by phytopathogenic soft-rot bacteria. Science 135:920–921

  93. Stutzenberger FJ (1987) Inducible thermoalkalophilic polygalacturonate lyase from Thermomonospora fusca. J Bacteriol 169:2774–2780

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

  95. Sukhumsirichart W, Sakamoto T, Chansiri K, Deesukon W, Kawasaki H (2007) Purification, characterization and overexpression of thermostable pectate lyase of Bacillus sp. RN1 isolated from hot spring in Thailand. Biosci Biotechnol Biochem (in press)

  96. Takami H, Nakasona K, Takaki Y, Maeno G, Sasaki R, Masui N, Fuji F, Hirama C, Nakamura Y, Ogaswara N, Kuhara S, Horikoshi K (2000) Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis. Nucleic Acids Res 28:4317–4331

  97. 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 64:2360–236

  98. Tamaki SJ, Gold S, Robeson M, Manulis S, Keen NT (1988) Structure and organization of the pel genes from Erwinia chrysanthemi EC 16. J Bacteriol 170:3468–3478

  99. Tamaru Y, Doi RH (2001) Pectate lyase A, an enzymatic subunit of the Clostridium cellulovorans cellulosome. Proc Natl Acad Sci USA 98:4125–4129

  100. Tardy F, Nasser W, Robert-Baudouy J, Hugouvieux-Cotte-Pattat N (1997) Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: enzyme characteristics and potential inhibitors. J Bacteriol 179:2503–2511

  101. Tempel W, Karaveg K, Liu ZJ, Rose J, Wang BC, Moremen KW (2004) Structure of mouse golgi α-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) α-1,2 mannosidases. J Biol Chem 279:29774–29786

  102. Thurn KK, Barras F, Kegoya-Yoshino Y, Chatterjee AK (1987) Pectate lyases of Erwinia chrysanthemi: Pel E-like polypeptides and Pel E homologous sequences in strains isolated from different plants. Physiol Mol Plant Pathol 31:429–439

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

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

  105. Walker MJ, Pemberton JM (1987) Construction of a transposon containing a gene for polygalacturonate transeliminase from Klebsiella oxytoca. Arch Microbiol 146:390–395

  106. Walker SG, Ryan ME (2003) Cloning and expression of pectate lyase from oral spirochete Treponema pectnovorum ATCC 33768. FEMS Microbiol Lett 226:385–390

  107. Waravdekar VS, Saslow LD (1957) A sensitive colorimetric method for the estimation of 2-deoxy sugars with the use of the malonaldehyde thiobarbituric acid reaction. J Biol Chem 234:1945–1950

  108. Wattad C, Dinoor R, Prusky D (1994) Purification of pectate lyase produced by Colletotrichum gloeosporioides and its inhibition by epicatechin: a possible factor involved in the resistance of unripe avocado fruits to anthracnose. Mol Plant Microbe Interact 7:293–297

  109. Weissbach A, Hurwitz J (1959) The formation of 2-keto-3-deoxyheptonic acid in extracts of Escherichia coli B. J Biol Chem 234:705–709

  110. Wilmot CM, Thornton JM (1990) ß-Turns and their distortions: a proposed new nomenclature. Protein Eng 3:479–493

  111. Yoder MD, Jurnak F (1995) The refined three-dimensional structure of pectate lyase C from Erwinia chrysanthemi at 2.2 Å resolution. Plant Physiol 107:349–364

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

  113. Yoder MD, Lietzke SE, Jurnak F (1993b) Unusual structural features in the parallel β-helix in pectate lyases. Structure 1:241–251

  114. Zhai C, Cao J, Wang Y (2003) Cloning and expression of a pectate lyase gene from Bacillus alcalophillus NTT33. Enzyme Microb Technol 33:173–178

  115. Zhao Q, Yuan S, Zhang Y, Zhu H, Dai C, Yang F, Han F (2007) Expression, purification and characterization of pectate lyase A from Aspergillus nidulans in Escherichia coli. World J Microbiol Biotechnol 23:1057–1064

  116. Zhuge B, Du G-C, Shen W, Zhuge J, Chen J (2007) Efficient secretory expression of an alkaline pectate lyase gene from Bacillus subtilis in E. coli and the purification and characterization of the protein. Biotechnol Lett 29:405–410

  117. Zucker M, Hankil L (1970) Regulation of pectate lyase synthesis in Pseudomonas fluorescens and Erwinia caortovora. J Bacteriol 104:13–18

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Grant under Fund for Improvement of Science and Technology—Department of Science and Technology Programme, New Delhi, to Lucknow University is gratefully acknowledged.

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Payasi, A., Sanwal, R. & Sanwal, G.G. Microbial pectate lyases: characterization and enzymological properties. World J Microbiol Biotechnol 25, 1–14 (2009).

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  • Enzymology
  • Microbial enzyme
  • Pectate lyase
  • Plant pathogenesis
  • Pectin degradation