文献类型： 外文期刊

作者： Wang, Y. ¹ ; Deng, Y. -D. ¹ ; Zhang, W. H. ¹ ; Gong, Z. -H. ¹ ; Qian, C. ¹ ; Peng, R. -H. ¹ ; Yao, Q. -H. ¹ ; Tian, Y. -S. ¹ ; Zhang, W. -Y. ² ; Han, H. -J. ¹ ;

作者机构： 1.Shanghai Acad Agr Sci, Shanghai Key Lab Agr Genet & Breeding, Biotechnol Res Inst, Shanghai 201106, Peoples R China

2.Shanghai Ctr Agriprod Qual & Safety, Shanghai 201708, Peoples R China

3.Minist Agr & Rural Affairs, Key Lab Safety Assessment Environm Agr Genet Modif, Shanghai 201106, Peoples R China

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.