The broad-specificity chitinases: their origin, characterization, and potential application
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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.
KeywordsChitinase Broad specificity N-Acetylglucosaminide Chitin conversion Biotechnology
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).
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Conflict of interest
The authors declare that they have no conflict of interest.
This article does not contain any studies with human or animals performed by any of the authors.
- 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
- 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