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Characteristics of the binding of a bacterial expansin ( Bs EXLX1) to microcrystalline cellulose
Author(s) -
Kim In Jung,
Ko HyeokJin,
Kim TaeWan,
Choi InGeol,
Kim Kyoung Heon
Publication year - 2013
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.24719
Subject(s) - expansin , microcrystalline cellulose , cellulose , cellulase , xylan , chemistry , cell wall , biochemistry , hydrolysis , gene expression , gene
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. Bs EXLX1 originating from Bacillus subtilis is a structural homolog of a β‐expansin produced by Zea mays ( Zm EXPB1). The Langmuir isotherm for binding of Bs EXLX1 to microcrystalline cellulose (i.e., Avicel) revealed that the equilibrium binding constant of Bs EXLX1 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 Bs EXLX1 was also comparable to those on microcrystalline cellulose for other Type A CBMs. Bs EXLX1 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, Zm EXPB1, to xylan, compared to cellulose was not exhibited by Bs EXLX1. In addition, the binding capacities of cellulose and xylan for Bs EXLX1 were much lower than those for Ct CBD3. Biotechnol. Bioeng. 2013; 110: 401–407. © 2012 Wiley Periodicals, Inc.