دورية أكاديمية
A Recombinant Thermophilic and Glucose-Tolerant GH1 β-Glucosidase Derived from Hehua Hot Spring.
| العنوان: | A Recombinant Thermophilic and Glucose-Tolerant GH1 β-Glucosidase Derived from Hehua Hot Spring. |
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| المؤلفون: | Zhu, Qian, Huang, Yuying, Yang, Zhengfeng, Wu, Xingci, Zhu, Qianru, Zheng, Hongzhao, Zhu, Dan, Lv, Zhihua, Yin, Yirui |
| المصدر: | Molecules; Mar2024, Vol. 29 Issue 5, p1017, 15p |
| مصطلحات موضوعية: | HOT springs, GLUCOSIDASES, ESCHERICHIA coli, THERMAL stability, SEDIMENT sampling, LIGNOCELLULOSE, GLUCOSE |
| مستخلص: | As a crucial enzyme for cellulose degradation, β-glucosidase finds extensive applications in food, feed, and bioethanol production; however, its potential is often limited by inadequate thermal stability and glucose tolerance. In this study, a functional gene (lq-bg5) for a GH1 family β-glucosidase was obtained from the metagenomic DNA of a hot spring sediment sample and heterologously expressed in E. coli and the recombinant enzyme was purified and characterized. The optimal temperature and pH of LQ-BG5 were 55 °C and 4.6, respectively. The relative residual activity of LQ-BG5 exceeded 90% at 55 °C for 9 h and 60 °C for 6 h and remained above 100% after incubation at pH 5.0–10.0 for 12 h. More importantly, LQ-BG5 demonstrated exceptional glucose tolerance with more than 40% activity remaining even at high glucose concentrations of 3000 mM. Thus, LQ-BG5 represents a thermophilic β-glucosidase exhibiting excellent thermal stability and remarkable glucose tolerance, making it highly promising for lignocellulose development and utilization. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: | Complementary Index |
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