Novel bacterial ferulic acid esterase from Cellvibrio japonicus and its application in ferulic acid release and xylan hydrolysis

被引：15
|
作者：
McClendon, Shara D. [1 ]
Shin, Hyun-Dong [1 ]
Chen, Rachel R. [1 ]
机构：
[1] Georgia Inst Technol, Sch Chem & Biomol Engn, Atlanta, GA 30332 USA
来源：
BIOTECHNOLOGY LETTERS | 2011年 / 33卷 / 01期
基金：
美国农业部; 美国国家科学基金会;
关键词：
Carbohydrate-binding module; Ferulic acid esterase; Lignocellulose bioprocessing; CLOSTRIDIUM-THERMOCELLUM CELLULOSOME; ENZYMATIC DEGRADATION; CELL-WALLS; ARABINOXYLAN; HYDROLASE; SEQUENCE; MAIZE;
D O I：
10.1007/s10529-010-0394-6
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Recent genome sequencing of Cellvibrio japonicas revealed the presence of two highly homologous ferulic acid esterases (FAEs), encoded by fee1A and fee1B. In this work, the putative FAE, Fee1B, was successfully cloned and expressed in an E. coli system and the purified enzyme was characterized as a type-D FAE with a pH and temperature optima of 6.5 and 35-40 degrees C, respectively. Additionally, the two tandem N-terminal carbohydrate binding modules of the multi-domain enzyme were shown to be crucial for optimum enzyme activity. The potential of the enzyme in biomass processing was demonstrated with its high synergy with a xylanase in the release of reducing sugar from arabinoxylan and its ability to liberate ferulic acid from various complex xylan substrates.
引用
收藏
页码：47 / 54
页数：8
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