Determination of Mode of Chitosanase Action by Matrix Associated Laser Desorption Ionization - Time of Flight Mass Spectrometry Analysis
- Authors
- 이춘근; 김주원; 박주리; 박용일; 황유진; 박제권
- Issue Date
- 2016
- Publisher
- 한국키틴키토산학회
- Keywords
- Active molecular chitosan; Chitosanase; Degradation mechanism; Action mode; MALDI-TOF MS
- Citation
- Journal of Chitin and Chitosan, v.21, no.2, pp.100 - 108
- Journal Title
- Journal of Chitin and Chitosan
- Volume
- 21
- Number
- 2
- Start Page
- 100
- End Page
- 108
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/9410
- DOI
- 10.17642/jcc.21.2.5
- ISSN
- 1229-4160
- Abstract
- A detailed knowledge about the mode of enzyme action is critical to get better understanding the productivity of target molecules. The present study was then performed to elucidate the mode of enzyme action and hydrolysis pattern of chitosanase toward high molecular weight chitosan. Hydrolysates derived from the reaction condition were then analyzed by Matrix Associated Laser Desorption Ionization - Time of Flight mass spectrometry (MALDI-TOF MS) analysis to define the real size of hydrolysates. Also, the sequence of linking pattern of hydrolysates derived from the action of chitosanase was determined based on the identification of both glucosamine (GlcN) and N-acetylglucosamine (GlcNAc). The results demonstrate that both homogeneous and heterogeneous chitooligosaccharides, designated as active molecular chitosan (AMC) can be produced without such a big differences. According to these results, we suggest that GlcNAc may not be a terminator for enzymatic hydrolysis processing as a key molecule in chitosanase reaction to determine the length of AMC. Upon identifying the type of linkage and size of AMC, nevertheless, these can be used as potent materials in various research fields including cosmeceutical and pharmaceutical applications.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - 바이오나노대학 > 생명과학과 > 1. Journal Articles
- 보건과학대학 > 의용생체공학과 > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.