A low-temperature-active alkaline pectate lyase from xanthomonas campestris aCCC 10048 with high activity over a wide ph range
文献类型： 外文期刊
第一作者： Yuan, Peng
作者： Yuan, Peng;Meng, Kun;Wang, Yaru;Luo, Huiying;Shi, Pengjun;Huang, Huoqing;Tu, Tao;Yang, Peilong;Yao, Bin
作者机构：
关键词： Alkaline pectate lyase;Bioscouring;Xanthomonas campestris ACCC 10048
期刊名称：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY （ 影响因子：2.926； 五年影响因子：2.685 ）
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收录情况： SCI
摘要： Alkaline pectate lyases are favorable for the textile industry. Here, we report the gene cloning and expression of a low-temperature-active alkaline pectate lyase (PL D) from Xanthomonas campestris ACCC 10048. Deduced PL D consists of a putative 27-residue signal peptide and a catalytic domain of 320 residues belonging to family PF09492. Recombinant PL D (r-PL D) produced in Escherichia coli was purified to electrophoretic homogeneity with a single step of Ni~(2+)-NTA affinity chromatography and showed an apparent molecular weight of ?38 kDa. The pH and temperature optima of r-PL D were found to be 9.0 °C and 30 °C, respectively. Compared with its microbial counterparts, r-PL D had higher activity over a wide pH range (>45%of themaximum activity at pH 3.0-12.0) and at lower temperatures (7gt;35%of activity even at 0 °C). The K_m and V_(max) values of r-PL D for polygalacturonic acid were 4.9 gl-1 and 30.1 μmolmin~(-1) mg~(-1), respectively. Compared with the commercial compound pectinase from Novozymes, r-PL D showed similar efficacy in reducing the intrinsic viscosity of polygalacturonic acid (35.1 % vs. 36.5 %) and in bioscouring of jute (10.25 % vs. 10.82 %). Thus, r-PL D is a valuable additive candidate for the textile industry.
分类号： Q5
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