An alkaline-active and alkali-stable pectate lyase from Streptomyces sp. S27 with potential in textile industry.

Peng Yuan, Kun Meng, Pengjun Shi, Huiying Luo, Huoqing Huang, Tao Tu, Peilong Yang, Bin Yao

Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun South Street, Beijing 100081, People's Republic of China.

Journal of industrial microbiology & biotechnology 2012 Jun

filter terms:

A pectate lyase gene (pl-str) was cloned from Streptomyces sp. S27 and expressed in Escherichia coli Rosetta. The full-length pl-str consists of 972 bp and encodes for a protein of 323 amino acids without signal peptide that belongs to family PF00544. The recombinant enzyme (r-PL-STR) was purified to electrophoretic homogeneity using Ni²⁺-NTA chromatography and showed apparent molecular mass of ~35 kDa. The pH optimum of r-PL-STR was found to be 10.0, and it exhibited >70% of the maximal activity at pH 12.0. After incubation at 37°C for 1 h without substrate, the enzyme retained more than 55% activity at pH 7.0-12.0. Compared with the commercial complex enzyme Scourzyme(@)301L from Novozymes, purified r-PL-STR showed similar efficacy in reducing the intrinsic viscosity of polygalacturonic acid (49.0 vs. 49.7%). When combined with cellulase and α-amylase, r-PL-STR had comparable performance in bioscouring of jute fabric (22.39 vs. 22.99%). Thus, r-PL-STR might represent a good candidate for use in alkaline industries such as textile.

Citation

Peng Yuan, Kun Meng, Pengjun Shi, Huiying Luo, Huoqing Huang, Tao Tu, Peilong Yang, Bin Yao. An alkaline-active and alkali-stable pectate lyase from Streptomyces sp. S27 with potential in textile industry. Journal of industrial microbiology & biotechnology. 2012 Jun;39(6):909-15