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Characteristics of the binding of a bacterial expansin (BsEXLX1) to microcrystalline cellulose

Authors
Kim, In JungKo, Hyeok-JinKim, Tae-WanChoi, In-GeolKim, Kyoung Heon
Issue Date
2월-2013
Publisher
WILEY
Keywords
bacterial expansin; BsEXLX1; carbohydrate-binding module; cellulose
Citation
BIOTECHNOLOGY AND BIOENGINEERING, v.110, no.2, pp.401 - 407
Indexed
SCIE
SCOPUS
Journal Title
BIOTECHNOLOGY AND BIOENGINEERING
Volume
110
Number
2
Start Page
401
End Page
407
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/104049
DOI
10.1002/bit.24719
ISSN
0006-3592
Abstract
Plant expansin proteins induce plant cell wall extension and have the ability to extend and disrupt cellulose. In addition, these proteins show synergistic activity with cellulases during cellulose hydrolysis. BsEXLX1 originating from Bacillus subtilis is a structural homolog of a beta-expansin produced by Zea mays (ZmEXPB1). The Langmuir isotherm for binding of BsEXLX1 to microcrystalline cellulose (i.e., Avicel) revealed that the equilibrium binding constant of BsEXLX1 to Avicel was similar to those of other Type A surface-binding carbohydrate-binding modules (CBMs) to microcrystalline cellulose, and the maximum number of binding sites on Avicel for BsEXLX1 was also comparable to those on microcrystalline cellulose for other Type A CBMs. BsEXLX1 did not bind to cellooligosaccharides, which is consistent with the typical binding behavior of Type A CBMs. The preferential binding pattern of a plant expansin, ZmEXPB1, to xylan, compared to cellulose was not exhibited by BsEXLX1. In addition, the binding capacities of cellulose and xylan for BsEXLX1 were much lower than those for CtCBD3. Biotechnol. Bioeng. 2013; 110: 401407. (c) 2012 Wiley Periodicals, Inc.
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