Journal of Carbohydrate Chemistry p. 414 - 430 (2018)
Update date:2022-08-16
Topics:
Xue, Yemin
Zhang, Zonghui
Hou, Jingjing
Cao, Zhigang
Zhang, Lingxian
Lou, Fen
Xu, Puxu
For preparation of resveratrol and arctigenin from peanut hulls and arctium lappa fruits, respectively, a recombinant β-glucosidase (TmBglA) from hyperthermophile Thermotoga maritima was purified and characterized. The hydrolytic activity was the highest at 90 °C and pH 6.2 for arctiin with Km of 1.61 mM and kcat of 197.4 s?1, and 90 °C and 5.8 for polydatin with Km of 0.38 mM and kcat of 47.6 s?1. The enzyme produced 215.4 mg L?1 resveratrol and 355.7 mg L?1 arctigenin from 400 mg L?1 polydatin and 540 mg L?1 arctiin after 60 min of incubation at 80 °C, with capable of hydrolyzing up to 92.1 and 94.9% of polydatin and arctiin, respectively. The enzymatic hydrolysis of peanut hulls and fructus arctii displayed a conversion yield of 3.8 and 0.33 mg resveratrol and arctigenin per gram of substrate material flour, respectively. Of the reported β-glucosidase, TmBglA exhibited the highest thermostability, kcat, kcat/Km, and conversion productivity for hydrolyzing polydatin and arctiin, and has great potential applications in functional food and medicine production.
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