Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8327246 | International Journal of Biological Macromolecules | 2018 | 9 Pages |
Abstract
In this study, a novel recombinant amylosucrase from Truepera radiovictrix DSM 17093 was characterized and found to produce α-glucans from sucrose. The enzyme showed maximum total and transglucosylation activities at pHâ¯7.5 and maximum hydrolysis activity at pHâ¯5.5. The optimum temperature for total, transglucosylation, and hydrolysis activities were determined to be 45, 45, and 50â¯Â°C, respectively. When the conversion of 100â¯mM sucrose was catalyzed at 35, 45, and 55â¯Â°C for 24â¯h, TR-ASase produced α-(1,4) glucans with average DPs of 59, 45, and 37, respectively. TR-ASase displayed more than 90% of its original activity after incubation at 55â¯Â°C for 5â¯h, which was much higher than that of all other reported ASases. Melting temperature determination and homology modeling were also adopted to analyze the extreme thermostability of this enzyme, TR-ASase.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Xingtong Zhu, Yuqing Tian, Wei Xu, Yuxiang Bai, Tao Zhang, Wanmeng Mu,