纤维素分解芽孢杆菌可能或可能不产生β -葡萄糖苷酶由于其环境来源-一个案例研究

Lutfun Neesa, N. Jahan, Md. Abdullah Al Noman Khan, Mohammad Shahedur Rahman
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引用次数: 1

摘要

微生物纤维素酶已经引起了全世界的关注,因为它们具有将最丰富的纤维素生物质加工成可持续生物燃料和其他有价值产品的巨大能力。有益的生物质转化过程高度依赖于使用有效的酶来降解木质纤维素。在纤维素降解酶中,β-葡萄糖苷酶通过减少纤维素二糖的积累来减轻对纤维素生物水解酶和内切葡聚糖酶的抑制,是有效水解纤维素生物质所必需的。本研究从贾汉格尔纳格尔大学校园附近的沼气厂废水和乳业废水中分离和筛选了具有β-葡萄糖苷酶活性的纤维素水解菌。经初步筛选,共有16株菌株具有纤维素水解活性,其中3株(B1、B5、D4)因效果较好而被筛选出。根据形态、生化和分子特征,鉴定为枯草芽孢杆菌(B. subtilis, B1)、解淀粉芽孢杆菌(Bacillus olimyquefaciens, B5)和枯草芽孢杆菌(B. subtilis, D4)。以pNPG为底物,通过测定PNP的释放量来测定这三种潜在的纤维素水解菌的β-葡萄糖苷酶活性,有趣的是,D4菌株的β-葡萄糖苷酶活性为阴性,而B1菌株的β-葡萄糖苷酶活性较高。
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Cellulolytic Bacillus May or May Not Produce β -Glucosidase Due to Their Environmental Origin – A Case Study
Microbial cellulases have been drawing attention worldwide because of their massive capacity to process the most abundant cellulosic biomass into sustainable biofuels and other valuable products. Profitable biomass conversion processes are highly dependent on the use of efficient enzymes for lignocellulose degradation. Among the cellulose degrading enzymes, β-glucosidases are essential for efficient hydrolysis of cellulosic biomass as they relieve the inhibition of the cellobiohydrolases and endoglucanases by reducing cellobiose accumulation. In this study, cellulolytic bacteria with potential β-glucosidases activity were isolated and screened from biogas plant effluent and dairy effluent near Jahangirnagar University campus. From initial screening, a total of 16 isolates were found to have cellulolytic activity, among them three isolates (B1, B5, D4) were selected based on their superior results. All the three bacterial isolates were identified as B. subtilis (B1), Bacillus amyloliquefaciens (B5) and B. subtilis (D4) respectively based on their morphological, biochemical and molecular characteristics. The βglucosidases activity of these three potential cellulolytic bacteria was performed by measuring the release of PNP using pNPG as a substrate and interestingly D4 strain was resulted with β-glucosidases negative where B1 strain was found to have efficient for β-glucosidases activity.
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