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Functional characterization of a GH62 family α-L-arabinofuranosidase from Eupenicillium parvum suitable for monosaccharification of corncob arabinoxylan in combination with key enzymes

阿拉伯木聚糖 玉米芯 木糖 化学 阿拉伯糖 纤维素酶 木聚糖酶 水解 糖苷水解酶 生物化学 食品科学 发酵 有机化学 原材料
作者
Liangkun Long,Lu Sun,Zhen Liu,Qunying Lin,Jing Wang,Shaojun Ding
出处
期刊:Enzyme and microbial technology [Elsevier BV]
卷期号:154: 109965-109965 被引量:9
标识
DOI:10.1016/j.enzmictec.2021.109965
摘要

Corncob rich in arabinoxylan is an important raw material widely used in bio-refinery. Complete saccharification of arabinoxylan depends on the synergism of different enzymes including α- L -arabinofuranosidase (ABF). This study aimed to investigate the functional characteristics of a new ABF EpABF62A belonging to glycoside hydrolase (GH) 62 family from the fungus Eupenicillium parvum , and to explore its potential in the saccharification of corncob arabinoxylan. The recombinant EpABF62A showed high activity against wheat arabinoxylan and rye arabinoxylan, with the optimal temperature of 55 °C and pH of 4.5. The protein contains an N-terminal cellulose-binding domain family 1 (CBM_1) domain, and displayed a 59.5% absorption rate to phosphoric acid swollen cellulose. Regioselectivity analysis indicated that the enzyme selectively removed α-1,2 or α-1,3 linked arabinofuranosyl residues on mono-substituted xylose residues on arabinoxylan. Corncob arabinoxylans (CAX1 or CAX2) with different (low or high) branching degrees were extracted from the raw material by alkaline hydrogen peroxide pretreatment and graded ethanol precipitation. Single EpABF62A removed 69.5% or 67.1% arabinose from CAX1 or CAX2, respectively. EpABF62A combined with a GH10 xylanase, a GH43 β- D -xylosidase and a GH67 α-glucuronidase released 75.0% or 64.5% xylose from CAX1 or CAX2, respectively. The addition of the four hemicellulases enhanced the saccharification the solid fraction of the pretreated corncob by the commercial cellulase Cellic® CTec2, and the conversion ratios of glucose, xylose and arabinose were up to 94.0%, 91.8% and 82.6%, respectively. • A new α- L -arabinofuranosidase with a CBM_1 domain from E. parvum was characterized. • The enzyme efficiently released arabinose from highly branched corncob arabinoxylan. • High-efficient saccharification of corncob was achieved by combination of key enzymes.
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