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首页> 外文期刊>Applied Microbiology and Biotechnology >Expression and characterization of a glucose-tolerant beta-1,4-glucosidase with wide substrate specificity from Cytophaga hutchinsonii
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Expression and characterization of a glucose-tolerant beta-1,4-glucosidase with wide substrate specificity from Cytophaga hutchinsonii

机译：来自Cytophaga Hutchinsonii宽底物特异性血糖耐受β-1,4-葡糖苷酶的表达及表征

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摘要

Cytophaga hutchinsonii is a gram-negative bacterium that can efficiently degrade crystalline cellulose by a novel strategy without cell-free cellulases or cellulosomes. Genomic analysis implied that C. hutchinsonii had endoglucanases and beta-glucosidases but no exoglucanases which could processively digest cellulose and produce cellobiose. In this study, BglA was functionally expressed in Escherichia coli and found to be a beta-glucosidase with wide substrate specificity. It can hydrolyze pNPG, pNPC, cellobiose, and cellodextrins. Moreover, unlike most beta-glucosidases whose activity greatly decreases with increasing length of the substrate chains, BglA has similar activity on cellobiose and larger cellodextrins. The K (m) values of BglA on cellobiose, cellotriose, and cellotetraose were calculated to be 4.8 x 10(-2), 5.6 x 10(-2), and 5.3 x 10(-2) mol/l, respectively. These properties give BglA a great advantage to cooperate with endoglucanases in C. hutchinsonii in cellulose degradation. We proposed that C. hutchinsonii could utilize a simple cellulase system which consists of endoglucanases and beta-glucosidases to completely digest amorphous cellulose into glucose. Moreover, BglA was also found to be highly tolerant to glucose as it retained 40 % activity when the concentration of glucose was 100 times higher than that of the substrate, showing potential application in the bioenergy industry.
机译：Cytophaga Hutchinsonii是一种革兰氏阴性细菌，可以通过无细胞纤维素酶或纤维素的新策略有效地降解结晶纤维素。基因组分析暗示C. Hutchinsonii具有内切葡聚糖酶和β-葡糖苷酶，但没有食用酶，其可以处理纤维素并产生纤维素。在本研究中，BGLA在大肠杆菌中功能性地表达，发现是具有宽底物特异性的β-葡糖苷酶。它可以水解PNPG，PNPC，Cellobiose和Cellodextrins。此外，与大多数β-葡糖苷酶不同，其活性随着底链的长度的增加而大大降低，Bgla在纤维生物糖和较大的蜂窝旋汀的活性相似。将BglA的K（m）在纤维二糖，细胞酮和细胞同时糖上的k（m）值分别计算为4.8×10（-2），5.6×10（-2）和5.3×10（-2）mol / l。这些性质使BGLA在C. Hutchinsonii中与纤维素降解中的C. Hutchinsonii合作有很大的优势。我们提出了C. Hutchinsonii可以利用简单的纤维素酶系统，该系统由内切葡聚糖酶和β-葡糖苷酶组成，以将无定形纤维素完全消化成葡萄糖。此外，当葡萄糖浓度高于基质的100倍时，也发现Bgla对葡萄糖保持高度耐受，因为它在底物的浓度高100倍时，显示在生物能源行业中的潜在应用。

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