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Three-dimensional Structure Analysis of Affinity between Enzyme and Substrate affecting on Enzyme Activity

한국키틴키토산학회지 2020년 25권 3호 p.117 ~ 125
구본근, 박제권,
소속 상세정보
구본근 ( Goo Bon-Geun ) - Chonbuk National University School of Dentistry Department of Preventive Dentistry
박제권 ( Park Jae-Kweon ) - Gachon University College of BioNano Department of Life Science

Abstract


Chitooligosaccharides (COSs) that have a different molecular weight ranging approximately from 360 to 2,500 Da has been focused as potent biologically active substances. A lot of challenges for producing COS have been performed, however, less is known about the techniques of how COS bigger than Hexa-glucosamine (GlcN)6 can be produced in either chemical or enzymatic degradation in industrial scale. In this study, we strived to elucidate the mode of action in terms of an interaction between enzyme and substrate affecting enzyme activity based on the three-dimensional analysis. Based on the results, we hypothesis that COS bigger than (GlcN)6 may hardly be made upon the action of the active site of an enzyme, which has highly potent energy concentrated around the active site that can degrade bigger COS into shorter than (GlcN)6. Therefore, it is very difficult to make such a big COS under the optimal conditions for the enzyme. As a result of observing the stability of each molecular size of COS in aqueous solution and the structural characteristics change in the reaction with the enzyme, the instability of the substrate is increased according to the substrate specificity of the enzyme, the behavior is weakened, and decomposition is accelerated by exposure to the active site. Therefore, it is emphasized that the difference in size and stability of the molecule of COS must be considered separately from the affinity for the enzyme.

키워드

Chitosan; Chitosanase; Three-dimension; Active site; Affinity and stability

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