Advertisement

The broad-specificity chitinases: their origin, characterization, and potential application

  • Jie Zhou
  • Jianhao Chen
  • Ning Xu
  • Alei Zhang
  • Kequan Chen
  • Fengxue Xin
  • Wenming Zhang
  • Jiangfeng Ma
  • Yan Fang
  • Min JiangEmail author
  • Weiliang DongEmail author
Mini-Review
  • 112 Downloads

Abstract

Chitinases are hydrolases that catalyze the cleavage of the β-1,4-O-glycosidic linkages in chitin, a polysaccharide abundantly found in nature. Although numerous chitinolytic enzymes have been studied in detail, relatively little is known about chitinases capable of broad specificity. Broad-specificity chitinases are a sort of novel chitinases possessing two or three different catalytic activities among exochitinase, endochitinase, and N-acetylglucosaminidase. In the light of the difference of module composition and catalytic mechanism, the broad-specificity chitinases included two broad categories, broad-specificity chitinases with a single catalytic domain or multi-catalytic domains. This broad-specificity chitinases have great potential in chitin conversion. In this review, we summarize all reported cases of broad-specificity chitinases and provide an overview of the recent findings on their origin, characterization, catalytic mechanism, and potential application. Moreover, in-depth study into these chitinases could contribute to our understanding of other broad-specificity enzymes which may have some benefits on progress of biotechnology.

Keywords

Chitinase Broad specificity N-Acetylglucosaminide Chitin conversion Biotechnology 

Notes

Funding information

This work was financially supported by the National Natural Science Foundation of China (No. 31700092, No. 21727818, No. 21706125, No. 21706124), the Jiangsu Province Natural Science Foundation for Youths (BK20170997, BK20170993), the China Postdoctoral Innovative Talents Support Program (BX20180140), the China Postdoctoral Science Foundation (No. 2018M642238), and the Jiangsu Synergetic Innovation Center for Advance Bio-Manufacture (No. XTE1834).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

This article does not contain any studies with human or animals performed by any of the authors.

References

  1. Bhattacharya D, Nagpure A, Gupta RK (2007) Bacterial chitinases: properties and potential. Crit Rev Biotechnol 27(1):21–28CrossRefGoogle Scholar
  2. Brameld KA, Goddard WA (1998) Substrate distortion to a boat conformation at subsite −1 is critical in the mechanism of family 18 chitinases. J Am Chem Soc 120(15):3571–3580CrossRefGoogle Scholar
  3. Chen JK, Shen CR, Liu CL (2010) N-acetylglucosamine: production and applications. Mari Drugs 8(9):2493–2516CrossRefGoogle Scholar
  4. Dahiya N, Tewari R, Hoondal GS (2006) Biotechnological aspects of chitinolytic enzymes: a review. Appl Microbiol Biotechnol 71(6):773–782CrossRefGoogle Scholar
  5. Donzelli BGG, Ostroff G, Harman GE (2003) Enhanced enzymatic hydrolysis of langostino shell chitin with mixtures of enzymes from bacterial and fungal sources. Carbohydr Res 338(18):1823–1833CrossRefGoogle Scholar
  6. Fu X, Yan Q, Yang S, Yang X, Guo Y, Jiang Z (2014) An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin to N-acetyl glucosamine. Biotech Biofuel 7(1):174CrossRefGoogle Scholar
  7. Gao C, Zhang A, Chen K, Hao Z, Tong J, Ouyang P (2015) Characterization of extracellular chitinase from Chitinibacter sp. GC72 and its application in GlcNAc production from crayfish shell enzymatic degradation. Biochem Eng J 97:59–64CrossRefGoogle Scholar
  8. Haran S, Schickler H, Oppenheim A, Chet I (1996) Differential expression of Trichoderma harzianum chitinases during mycoparasitism. Phytopathology 86(9):980–985CrossRefGoogle Scholar
  9. Howard MB, Ekborg NA, Taylor LE, Hutcheson SW, Weiner RM (2004a) Identification and analysis of polyserine linker domains in prokaryotic proteins with emphasis on the marine bacterium Microbulbifer degradans. Protein Sci 13(5):1422–1425CrossRefGoogle Scholar
  10. Howard MB, Ekborg NA, Taylor LE, Weiner RM, Hutcheson SW (2004b) Chitinase B of “Microbulbifer degradans” 2-40 contains two catalytic domains with different chitinolytic activities. J Bacteriol 186(5):1297–1303CrossRefGoogle Scholar
  11. Huang QS, Xie XL, Liang G, Gong F, Wang Y, Wei X-Q, Wang Q, Ji Z-L, Chen Q-X (2011) The GH18 family of chitinases: their domain architectures, functions and evolutions. Glycobiology 22(1):23–34CrossRefGoogle Scholar
  12. Huang L, Shizume A, Nogawa M, Taguchi G, Shimosaka M (2012) Heterologous expression and functional characterization of a novel chitinase from the chitinolytic bacterium Chitiniphilus shinanonensis. Biosci Biotechnol Biochem 76(3):517–522CrossRefGoogle Scholar
  13. Itoh T, Sugimoto I, Hibi T, Suzuki F, Matsuo K, Fujii Y, Taketo A, Kimoto H (2014) Overexpression, purification, and characterization of Paenibacillus cell surface-expressed chitinase ChiW with two catalytic domains. Biosci Biotechnol Biochem 78(4):624–634CrossRefGoogle Scholar
  14. Kudan S, Eksittikul T, Pichyangkura R, Park RD (2010) Preparation of N-acetyl-D-glucosamine and N, N′-acetylchitobiose by enzymatic hydrolysis of chitin with crude chitinases. J Biotechnol 150:89CrossRefGoogle Scholar
  15. Lee YS, Park IH, Yoo JS, Chung S-Y, Lee Y-C, Cho Y-S, Ahn S-C, Kim C-M, Choi Y-L (2007) Cloning, purification, and characterization of chitinase from Bacillus sp. DAU101. Bioresour Technol 98(14):2734–2741CrossRefGoogle Scholar
  16. Li ZK, Wang T, Luo X, Li XM, Xia CY, Zhao YQ, Ye XF, Huang Y, Gu XY, Cao H, Cui ZL, Fang JQ (2018) Biocontrol potential of Myxococcus sp. strain BS against bacterial soft rot of calla lily caused by Pectobacterium carotovorum. Biol Control 126:36–44CrossRefGoogle Scholar
  17. Mesnage S, Fontaine T, Mignot T, Delepierre M, Mock M, Fouet A (2000) Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation. EMBO J 19(17):4473–4484CrossRefGoogle Scholar
  18. Nagaoka I, Igarashi M, Sakamoto K (2012) Biological activities of glucosamine and its related substances. Advances in food and nutrition research. Acad. Press, 65: 337–352Google Scholar
  19. Pichyangkura R, Kudan S, Kuttiyawong K, Sukwattanasinitt M, Aiba S (2002) Quantitative production of 2-acetamido-2-deoxy-D-glucose from crystalline chitin by bacterial chitinase. Carbohydr Res 337(6):557–559CrossRefGoogle Scholar
  20. Shi P, Tian J, Yuan T, Liu X, Huang H, Bai Y, Yang P, Chen X, Wu N, Yao B (2010) Paenibacillus sp. strain E18 bifunctional xylanase-glucanase with a single catalytic domain. Appl Environ Microbiol 76(11):3620–3624CrossRefGoogle Scholar
  21. Tanaka T, Fukui T, Imanaka T (2001) Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J Biol Chem 276(38):35629–35635CrossRefGoogle Scholar
  22. van Aalten DM, Komander D, Synstad B, Gåseidnes S, Peter MG, Eijsink VG (2001) Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc Natl Acad Sci 98(16):8979–8984CrossRefGoogle Scholar
  23. Vrzheshch P (2007) Steady-state kinetics of bifunctional enzymes. Taking into account kinetic hierarchy of fast and slow catalytic cycles in a generalized model. Biochemistry 72(9):936–943Google Scholar
  24. Yang S, Fu X, Yan Q, Jiang Z, Wang J (2016) Biochemical characterization of a novel acidic exochitinase from Rhizomucor miehei with antifungal activity. J Agric Food Chem 64(2):461–469CrossRefGoogle Scholar
  25. Zhang A, Gao C, Wang J, Chen K, Ouyang P (2016) An efficient enzymatic production of N-acetyl-D-glucosamine from crude chitin powders. Green Chem 18(7):2147–2154CrossRefGoogle Scholar
  26. Zhang A, He Y, Wei G, Zhou J, Dong W, Chen K, Ouyang P (2018) Molecular characterization of a novel chitinase CmChi1 from Chitinolyticbacter meiyuanensis SYBC-H1 and its use in N-acetyl-d-glucosamine production. Biotechnol Biofuels 11(1):179CrossRefGoogle Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  • Jie Zhou
    • 1
    • 2
  • Jianhao Chen
    • 1
  • Ning Xu
    • 1
  • Alei Zhang
    • 1
    • 2
  • Kequan Chen
    • 1
    • 2
  • Fengxue Xin
    • 1
    • 2
  • Wenming Zhang
    • 1
    • 2
  • Jiangfeng Ma
    • 1
    • 2
  • Yan Fang
    • 1
    • 2
  • Min Jiang
    • 1
    • 2
    Email author
  • Weiliang Dong
    • 1
    • 2
    Email author
  1. 1.State Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical EngineeringNanjing Tech UniversityNanjingPeople’s Republic of China
  2. 2.Jiangsu National Synergetic Innovation Center for Advanced Materials (SICAM)Nanjing Tech UniversityNanjingPeople’s Republic of China

Personalised recommendations