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Postępy Mikrobiologii - Advancements of Microbiology

Polish Society of Microbiologists

Subject: Microbiology


ISSN: 0079-4252
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VOLUME 56 , ISSUE 3 (April 2017) > List of articles


Anna Kisiel * / Ewa Kępczyńska

Keywords : N-acetylglucosamine, chitinolytic bacterial, biofungicides, bioinsecticides, chitin, chitinases, biological control

Citation Information : Postępy Mikrobiologii - Advancements of Microbiology. Volume 56, Issue 3, Pages 306-315, DOI:

License : (CC BY-NC-ND 4.0)

Published Online: 22-May-2019



Chitin, an insoluble linear β-1,4-linked polymer of N-acetylglucosamine, is the second most abundant polysaccharide in nature after cellulose. It is present in cell walls of several fungi, exoskeletons of insects and crustacean shells. Enzymatic hydrolysis of this polysaccharide is carried out in the presence of glycoside hydrolases-chitinases. They are produced by microorganisms, insects, plants, and animal, but it is the bacterial chitinases which play a fundamental role in degradation of the chitin. Chitinases and their products, chito-oligomers, have been of interest in recent years due to their wide range of applications in agriculture, medicine and industry. This review focuses on the enzymatic properties of the bacterial chitinases and their potential applications in various kinds of biotechnology.

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1. Aggarwal C., Paul S., Tripathi V., Paul B., Khan M.A.: Chitinolytic activity in Serratia marcescens (strain SEN) and potency against different larval instars of Spodoptera litura with effect of sublethal doses on insect development. BioControl, 60, 631–640 (2015)

2. Ajit N.S., Verma R., Shanmugam V.: Extracellular chitinases of fluorescent Pseudomonads antifungal to Fusarium oxysporum f. sp. dianthi causing carnation wilt. Curr. Microbiol. 52, 310–316 (2006)

3. Arora N.K., Kim M.J., Kang S.C., Maheshwari D.K.: Role of chitinase and β-1,3-glucanase activities produced by a fluorescent pseudomonad and in vitro inhibition of Phytophthora capsici and Rhizoctonia solani. Can. J. Microbiol. 53, 207–212 (2007)

4. Bao-qin H., Chang-ying Y., Wan-shun L., Ji-Xun D.: Purification and inhibition fungal growth of chitinases from Vibrio pacini. Wuhan Univ. J. Nat. Sci. 9, 973–978 (2004)

5. Cai Y., Yan J., Hu X., HanB., Yuan Z.: Improving the insecticidal activity against resistant Culex quinquefasciatus mosquitoes by expression of chitinase gene chiAC in Bacillus sphaericus. Appl. Environ. Microbiol. 73, 7744–7746 (2007)

6. Cantarel B.L., Coutinho P.M., Rancurel C., Bernard T., Lombard V., Henrissat B.: The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 37, 233–238 (2009)

7. Chang W.T., Chen M., Wang S.L.: An antifungal chitinase produced by Bacillus subtilis using chitin waste as a carbon source. World J. Microbiol. Biotechnol. 26, 945–950 (2010)

8. Chang W.T., Chen Y.C., Jao C.L.: Antifungal activity and enhancement of plant growth by Bacillus cereus grown on shellfish chitin wastes. Biores. Technol. 98, 1224–1230 (2007)

9. Chen L., Shen Z., Wu J.: Expression, purification and in vitro antifungal activity of acidic mammalian chitinase against Candida albicans, Aspergillus fumigatus and Trichophyton rubrum strains. Clin. Exp. Dermatol. 34, 55–60 (2009)

10. Choudhary B., Nagpure A., Gupta R.K.: Fungal cell wall lytic enzymes, antifungal metabolite (s) production, and characterization from Streptomyces exfoliates MT9 for controlling fruit-rotting fungi. J. Basic Microbiol. 54, 1295–1309 (2014)

11. Cohen-Kupiec R., Chet I.: The molecular biology of chitin digestion. Curr. Opin. Biotechnol. 9, 270–277 (1998)

12. Comb D.G., Roseman S.: Glucosamine-6-phosphate deaminase. Biochim. Biophys. Acta, 21, 193–194 (1956)

13. Dahiya N., Tewari R., Hoondal G.S.: Biotechnological aspects of chitinolytic enzymes: a review. Appl. Microbiol. Biotech. 25, 1–10 (2006)

14. Dahiya N., Tewari R., Tiwari R.P., Hoondal G.S.: Production of an antifungal chitinase from Enterobacter sp. NRG4 and its application in protoplast production. World J. Microbiol. 21, 1611–1616 (2005)

15. Das S.N., Neeraja Ch., Sarma P.V.S.R.N., Madhu Prakash J., Purushotham P., Kaur M., Dutta S., Podile A.R.: Microbial chitinases for chitin waste management (w) Microorganism in Environmental Management, red. Satyanarayana T., Johri B.N., Prakash A., Springer, New York, 2012, s. 135–150

16. Deilamy A., Abbasipour H.: Comparative bioassay of different isolates of Bacillus thuringiensis subsp. kurstaki on the third larval instars of diamondback moth, Plutella xylostella (L.) (Lep.: Plutellidae). Arch. Phytopathol. Plant. Prot. 46, 1480–1487 (2013)

17. Erb S.L., Bourchier R.S., Frankenhuyzen K.V., Smith S.M.: Sublethal effects of Bacillus thuringiensis berliner subsp. kurstaki on Lymantria dispar (Lepidoptera: Lymantriidae) and the tachinid parasitoid Compsilura concinnata (Diptera: Tachinidae). Environ. Entomol. 30, 1174–1181 (2001)

18. Felse P.A., Panda T.: Production of microbial chitinases: a revisit. Bioprocess. Eng. 23, 127–134 (2000)

19. Felse P.A., Panda T.: Regulation and cloning of microbial chitinase genes. Appl. Microbiol. Biotechnol. 51, 141–151 (1999)

20. Ferrari A.R , Gaber Y., Fraaije M.W.: A fast, sensitive and easy colorimetric assay for chitinase and cellulose activity detection. Biotechnol. Biofuels. 7, 37–44 (2014)

21. Frederiksen R.F., Paspaliari D.K., Larsen T., Storgaard B.G., Larsen M.H., Ingmer H. Storgaard B.G., Larsen M.H., Ingmer H., Palcic M.M., Leisner J.J.: Bacterial chitinases and chitin-binding proteins as virulence factors. Microbiology, 159, 833–847 (2013)

22. Gadelhak G.G., El-Tarabily K.A., Al-Kaabi F.K.: Insect control using chitinolytic soil actinomycetes as biocontrol agents. Int. J. Agr. Biol. 7, 627–633 (2005)

23. Ghasemi S., Ahmadian G., Jelodar N.B., Rahimian H., Ghandili S., Dehestani A., Shariati P.: Antifungal chitinases from Bacillus pumilus SG2: preliminary report. World J. Microbiol. Biotechnol. 26, 1437–1443 (2010)

24. Gomaa E.Z.: Chitinase production by Bacillus thuringiensis and Bacillus licheniformis: their potential in antifungal biocontrol. J. Microbiol. 50, 103–111 (2012)

25. Gooday G.W.: The ecology of chitin degradation. Adv. Microbial. Ecol. 11, 387–430 (1990)

26. Gupta R., Saxena R.K., Chaturvedi P., Viridi J.S.: Chitinase production by Streptomyces viridificans: its potential in fungal cell wall lysis. J. Appl. Bacteriol. 78, 378–383 (1995)

27. Halder S.K., Maity Ch., Jana A., Das A., Paul T., Mohapatra P.K.D., Pati B.R., Mondal K.Ch.: Proficient biodegradation of shrimp shell waste by Aeromonas hydrophila SBK1 for the concomitant production of antifungal chitinase and antioxidant chitosaccharides. Int. Biodet. Biodeg. 79, 88–97 (2013)

28. Hammami I., Siala R., Jridi M., Ktari N., Nasri M., Mohamedali T.: Partial purification and characterization of chiIO8, a novel antifungal chitinase produced by Bacillus cereus IO8. J. Appl. Microbiol. 115, 358–366 (2013)

29. Hartl L., Zach S., Seidl-Seiboth V.: Fungal chitinases: diversity, mechanistic properties and biotechnological potential. Appl. Microbiol. Biotechnol. 93, 533–543 (2012)

30. Hernández-León R., Rojas-Solís D., Contreras-Pérez M., del Carmen Orozco-Mosqueda M., Macías-Rodríguez L.I., Reyes-de la Cruz H., Valencia-Cantero E., Santoyo G.: Characterization of the antifungal and plant growth-promoting effects of diffusible and volatile organic compounds produced by Pseudomonas fluorescens strains. Biol. Control, 81, 83–92 (2015)

31. Hoang K.C., Lai T.H., Lin C.S., Chen Y.T., Liau C.Y.: The chitinolytic activities of Streptomyces sp. TH-11. Int. J. Mol. Sci. 12, 56–65 (2011)

32. Howard M.B., Ekborg N.A., Weiner R.M., Hutcheson S.W.: Detection and characterization of chitinases and other chitin-modifying enzymes. J. Ind. Microbiol. Biotechnol. 30, 627–635 (2003)

33. Inbar J., Che, I.: Evidence that chitinase produced by Aeromonas caviae is involved in biological control of soil borne plant pathogen by this bacterium. Soil Biol. Biochem. 23, 973–978 (1991)

34. Itoh Y., Takahashi K., Takizawa H., Nikaidou N., Tanaka H., Nishihashi H., Watanabe T., Nishizawa Y.: Family 19 chitinase of Streptomyces griseus HUT6037 increases plant resistance to the fungal disease. Biosci. Biotechnol. Biochem. 67, 847–855 (2003)

35. Johnson E.A., Villa T.G., Lewis M.J., Phaff H.J.: Lysis of cell wall of yeast Phaffia rhodozyme by a lytic complex from Bacillus circulans WL-12. J. Appl. Biochem. 1, 272–282 (1979)

36. Kasprzewska A.: Plant chitinases – regulation and function. Cell. Mol. Biol. Lett. 8, 809–824 (2003)

37. Keyhani N.O., Roseman S.: Physiological aspects of chitin catabolism in marine bacteria. Biochim. Biophys. Acta, 1473, 108–122 (1999)

38. Kezuka Y., Ohishi M., Itoh Y., Watanabe J., Mitsutomi M., Watanabe T., Nonaka T.: Structural studies of a two-domain chitinase from Streptomyces griseus HUT6037. J. Mol. Biol. 358, 472–484 (2006)

39. Khandelwal P., Bhatnagar N.B.: Insecticidal activity associated with the outer membrane vesicles of Xenorhabdus nematophilus. Appl. Environ. Microbiol. 69, 2032–2037 (2003)

40. Kim K.J., Yang Y.J., Kim J.G.: Purification and characterization of chitinase from Streptomyces sp. M-20. J. Biochem. Mol. Biol. 36, 185–189 (2003)

41. Kishore G.K., Pande S., Podile A.R.: Biological control of late leaf spot of peanut (Arachis hypogaea) with chitinolytic bacteria. Phytopathology, 95, 1157–1165 (2005)

42. Kisiel A., Jęckowska K., Kępczyńska E.: Rola chitynaz w rozwoju roślin. Post. Biol. Kom. 44, 273–288 (2016)

43. Kurita K.: Controlled functionalization of the polysaccharide chitin. Prog. Polym. Sci. 26, 1921–1971 (2001)

44. Larsen T., Petersen B.O., Storgaard B.G., Duus J.O., Palcic M.M., Leisner J.J.: Characterization of a novel Salmonella typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate. Glycobiology, 21, 426–436 (2011)

45. Li J.G., Jiang Z.Q., Xu L.P., Sun F.F., Guo J.H.: Characterization of chitinase secreted by Bacillus cereus strain CH2 and evaluation of its efficacy against Verticillium wilt of eggplant. Biocontrol, 53, 931–944 (2008)

46. Liang T.W., Chen Y.J., Yen Y.H., Wang S.L.: The antitumor activity of the hydrolysates of chitinous materials hydrolyzed by crude enzyme from Bacillus amyloliquefaciens V656. Process. Biochem. 42, 527–534 (2007)

47. Liu D., Cai J., Xie Ch.-Ch., Liu Ch., Chen Y.-H.: Purification and partial characterization of a 36-kDa chitinase from Bacillus thuringiensis spp. colmeri, and its biocontrol potential. Enzyme Microb. Technol. 46, 252–256 (2010)

48. Liu M., Cai Q.X., Liu H.Z., Zhang B.H., Yan J.P., Yuan Z.M.: Chitinolytic activities in Bacillus thuringiensis and their synergistic effects on larvicidal activity. J. Appl. Microbiol. 93, 374–379 (2002)

49. Martínez-Absalón S., Rojas-Solís D., Hernández-León R., Orozco-Mosqueda Ma. del C., Peña-Cabriales J.J., Sakuda S., Valencia-Cantero E., Santoyo G.: Potential use and mode of action of the new strain Bacillus thuringiensis UM96 for the biological control of the gray mould phytopathogen Botrytis cinerea. Biocontrol Sci. Technol. 24, 1349–1362 (2014)

50. Mohan M., Sushil S.N., Bhatt J.C., Gujar G.T., Gupta H.S.: Synergistic interaction between sublethal doses of Bacillus thuringiensis and Campoletis chlorideae in managing Helicoverpa armigera. BioControl, 53, 375–386 (2008)

51. Morimoto K., Karita S., Kimura T., Sakka K., Ohmiya K.: Cloning, sequencing and expression of the gene encoding Clostridium paraputrificum chitinases ChiB and analysis of the functions of novel cadherinlike domains and chitin-binding domain. J. Bacteriol. 179, 7306–7314 (1997)

52. Nagpure A., Choudhary B., Gupta R.K.: Chitinases: in agriculture and human healthcare. Crit. Rev. Biotechnol. 34, 215–232 (2013)

53. Nagpure A., Choudhary B., Kumar S., Gupta R.K.: Isolation and characterization of chitinolytic Streptomycessp. MT7 and its antagonism towards wood-rotting fungi. Ann. Microbiol. 64, 531–541 (2013)

54. Nawani N.N., Kapadnis B.P.: Production dynamics and characterization of chitinolytic system of Streptomyces sp. NK 1057,
a well equipped chitin degrader. World J. Microbiol. Biotechnol. 20, 487–494 (2004)

55. Novotna Z., Fliegerova K., Simunek J.: Characterization of chitinases of polycentric anaerobic rumen fungi. Folia Microbiol. 53, 241–245 (2008)

56. Ohnuma T., Numata T., Osawa T., Mizuhara M., Lampela O., Juffer A.H., Skriver K., Fukamizo T.: A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis. Planta, 234, 123–137 (2011)

57. Patil R.S., Ghormade V., Deshpande M.V.: Chitinolytic enzymes: An exploration. Enzyme Microb. Technol. 26, 473–483 (2000)

58. Payne J.M., Davidson E.W.: Insecticidal activity of crystalline parasporal inclusions and other components of the Bacillus sphaericus 1593 spore complex. J. Invertebr. Pathol. 43, 383–388 (1984)

59. Prapagdee B., Kuekulvong C., Mongkolsuk S.: Antifungal potential of extracellular metabolites produced by Streptomyces hygroscopicus against phytopathogenic fungi. Int. J. Biol. Sci. 4, 330–337 (2008)

60. Price N.P.J., Naumann T.A.: A high-throughput matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry-based assay of chitinase activity. Anal. Biochem. 411, 94–99 (2011)

61. Rabeeth M., Anitha A., Srikanth G.: Purification of an antifungal endochitinase from a potential biocontrol agent Streptomyces griseus. Pak. J. Biol. Sci. 14, 788–797 (2011)

62. Ramírez-Coutiño L., Marín-Cervantes M.D.C., Huerta S., Revah S., Shirai K.: Enzymatic hydrolysis of chitin in the production of oligosaccharides using Lecanicillium fungicola chitinases. Process Biochemistry, 41, 1106–1110 (2006)

63. Regev A., Keller M., Strizhov N., Sneh B., Prudovsky E., Chet I., Ginzberg I., Koncz-Kalman Z., Koncz C., Schell J., Zilberstein A.: Synergistic activity of a Bacillus thuringiensis delta-endotoxin and a bacterial endochitinase against Spodoptera littoralis larvae. Appl. Environ. Microbiol. 62, 3581–3586 (1996)

64. Revah-Moiseev S., Carroad P.A.: Conversion of enzymatic hydrolysate of shellfish waste chitin to SCP. Biotechnol. Bioeng. 23, 1067–1078 (1981)

65. Sahai A.S., Manocha M.S.: Chitinases of fungi and plants: their involvement in morphogenesis and host parasite interaction. FEMS Microbiol. Rev. 11, 317–338 (1993)

66. Sakai K., Yokota A., Kurokawa H., Wakayama M., Moriguchi M.: Purification and characterization of three thermostable endochitinases of a noble Bacillus strain, MH-1, isolated from chitin-containing compost. Appl. Environ. Microbiol. 64, 3397–3402 (1998)

67. Saks E., Jankiewicz U.: Aktywność chitynolityczna bakterii. Post. Bioch. 56, 427–434 (2010)

68. Schales O., Schales S.S.: Simple method for the determination of glucose in blood. Proc. Am. Fed. Clin. Res. 2, 78 (1945)

69. Sharma N., Sharma K.P., Gaur R.K., Gupta V.K.: Role of chitinase in plant defense. Asian J. Biochem. 6, 29–37 (2011)

70. Sindhu S.S., Dadarwal K.R.: Chitinolytic and cellulolytic pseudomonas antagonistic to fungal pathogens enhance nodulation by Mesorhizobium sp in chickpea. Microbiol. Res. 156, 353–358 (2001)

71. Skujins J.J., Potgeiter H.J., Alexander M.: Dissolution of fungal cell walls by Streptomyces chitinase and β-1,3-glucanase. Arch. Biochem. Biophys. 111, 358–364 (1965)

72. Someya N., Nakajima M., Hirayae K., Hibi T., Akutsu K.: Synergistic antifungal activity of chitinolytic enzymes and prodigiosin produced by the biocontrol bacterium Serratia marcescens strain B2 against the gray mold pathogen, Botrytis cinerea.
J. Gen. Plant. Pathol. 67, 312–317 (2001)

73. Sridevi M., Mallaiah K.V.: Factors effecting chitinase activity of Rhizobium sp. from Sesbania sesban. Biologia, 63, 307–312 (2008)

74. Suma K., Podile A.R.: Chitinase A from Stenotrophomonas maltophilia shows transglycosylation and antifungal activities. Biores. Technol. 133, 213–220 (2013)

75. Suzuki K., Sugawara N., Suzuki M., Uchiyama T., Katouno F., Nikaidou N., Watanabe T.: Chitinases, A, B and C1 of Serratia marcescens 2170 produced by recombinant E. coli: enzymatic properties and synergism on chitin degradation. Biosci. Biotechnol. Biochem. 66, 1075–1083 (2002)

76. Swiontek-Brzezinska M., Jankiewicz U., Burkowska A., Walczak M.: Chitinolytic microorganisms and their possible application in environmental protection. Curr. Microbiol. 68, 71–81 (2014)

77. Swiontek-Brzezinska M., Lalke-Porczyk E., Donderski W.: Occurrence and activity of microorganisms in shrimp waste. Curr. Microbiol. 57, 580–587 (2008)

78. Swiontek-Brzezinska M., Lalke-Porczyk E., Donderski W.: Chitinolytic activity of bacteria and fungi isolated from shrimp exoskeletons. Ocean. Hydrob. Studies, 36, 101–111 (2007)

79. Swiontek-Brzezinska M., Lalke-Porczyk E., Donderski W.: The role of chitinolytic bacteria and fungi in biodegradation of crustacean remains in lacustrine habitats. Pol. J. Ecol. 56, 335–342 (2008)

80. Tokoro A., Tatewaki N., Suzuki K., Mikami T., Suzuki S., Suzuki M.: Growth-inhibitory effect of hexa-N-acetylchitohexaose and chitohexaose against meth-A solid tumor. Chem. Pharm. Bull. 36, 784–790 (1988)

81. Tsujibo H., Minoura K., Miyamoto K., Moriwaki M., Inamori Y.: Purification and properties of a thermostable chitinase from Streptomyces thermoviolaceus OPC-520. Appl. Environ. Microbiol. 59, 620–622 (1993)

82. Tsukada K., Matsumoto T., Aizawa K., Tokoro A., Naruse R., Suzuki S., Suzuki M.: Antimetastatic and growth-inhibitory effects of N-acetylchitohexaose in mice bearing Lewis lung carcinoma. Jpn. J. Cancer Res. 81, 259–265 (1990)

83. Vaidya R.J., Shah I.M., Vyas P.R., Chatpar H.S.: Production of chitinase and its optimization from a novel isolate Alcaligenes xylosoxydans: potential antifungal biocontrol. World J. Microbiol. Biotechnol. 1, 62–69 (2001)

84. Wang S.L., Chang W.T.: Purification and characterization of two bifunctional chitinases/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in shrimp and crab shell powder medium. Appl. Environ. Microbiol. 63, 380–386 (1997)

85. Wang S.L., Chao C.H., Liang T.W., Chen C.C.: Purification and characterization of protease and chitinase from Bacillus cereus TKU006 and conversion of marine wastes by these enzymes. Mar. Biotechnol. 11, 334–344 (2009)

86. Wiweger M., Farbos I., Ingouff M., Langercrantz U., Von Arnold S.: Expression of Chia4-Pa chitinase genes Turing somatic and zygotic embryo development in Norway spruce (Picea abies): similarities and differences between gymnosperm and angiosperm class IV chitinases. J. Exp. Bot. 54, 2691–2699 (2003)

87. Xiao-Jing X., Li-Qun Z., You-Yong Z., Wen-Hua T.: Improving biocontrol effect of Pseudomonas fluorescens P5 on plant diseases by genetic modification with chitinase gene. Chin. J. Agric. Biotechol. 2, 23–27 (2005)

88. Yan Q., Fong S.S.: Bacterial chitinase: nature and perspectives for sustainable bioproduction. Biores. Bioproc. 2, 31 (2015)

89. Yano S., Rattanakit N., Honda A., Noda Y., Wakayama M., Plikomol A., Tachiki T.: Purification and characterization of chitinase A of Streptomyces cyaneus SP-27: an enzyme participates in protoplast formation from Schizophyllum commune mycelia. Biosci. Biotechnol. Biochem. 72, 54–61 (2008)

90. Yano S., Rattanakit N., Wakayama M., Tachiki T.: A chitinase indispensable for formation of protoplast of Schizophyllum commune in basidiomycete-lytic enzyme preparation produced by Bacillus circulans KA-304. Biosci. Biotechnol. Biochem. 68, 1299–1305 (2004)

91. Zarandi H.S., Bagheri A., Baghizadeh A., Moshtaghi N.: Quantitative analysis of chitinase gene expression in chickpea. Russ. J. Plant. Physl. 58, 681–685 (2011)