文献类型： 外文期刊
第一作者： Wang, Y.
作者： Wang, Y.;Deng, Y. -D.;Zhang, W. H.;Gong, Z. -H.;Qian, C.;Peng, R. -H.;Yao, Q. -H.;Tian, Y. -S.;Han, H. -J.;Zhang, W. -Y.;Wang, Y.;Han, H. -J.
作者机构：
关键词： alkali-tolerant; codon optimization; thermostability; xylanases
期刊名称：APPLIED BIOCHEMISTRY AND MICROBIOLOGY （ 影响因子：0.8； 五年影响因子：1.1 ）
ISSN： 0003-6838
年卷期： 2023 年 59 卷 2 期
页码：
收录情况： SCI
摘要： A novel alkaline xylanase gene (xynAI) from Bacillus amyloliquefaciens was highly expressed in Pichia pastoris, and the enzyme was purified and characterized. Sequence analysis indicated that XynAI belongs to xylanases family GH11 with 5 potential N-glycosylation sites and 3 salt bridges. The purified XynAI had molecular weight of 22 kDa, the optima temperature and pH of 55 degrees C and pH 8.6, respectively. Furthermore, XynAI has high thermal (30-70 degrees C) and pH (pH 5.0-10.0) stability.Mg2+, Ni2+, Ca2+ and Fe2+ at concentration of 1 mM enhanced the xylanase activity by 6.2, 6.5, 7.9 and 202.6%, respectively. Under optimal conditions, the K-M and V-max values of XynAI for beechwood xylan were 8 mg/mL and 83.3 mu mol min(-1) mg of protein(-1), respectively. In the culture supernatant, the maximal protein concentration and xylanase activity of XynAI reached 3.98 mg/mL and 292 U/mg, respectively. The biochemical properties of XynAI showed that it may be a promising candidate for industrial applications.
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