An alkaline-active and alkali-stable pectate lyase from Streptomyces sp. S27 with potential in textile industry
作者： Peng Yuan , Kun Meng , Pengjun Shi , Huiying Luo , Huoqing Huang
DOI: 10.1007/S10295-012-1085-1
关键词: Substrate (chemistry) 、 Cellulase 、 Biochemistry 、 Amino acid 、 Enzyme 、 Biology 、 Molecular mass 、 Escherichia coli 、 Pectate lyase 、 Streptomyces
摘要: 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 encodes for a protein 323 amino acids without signal peptide that belongs to family PF00544. recombinant enzyme (r-PL-STR) purified electrophoretic homogeneity using Ni2+–NTA chromatography showed apparent molecular mass ~35 kDa. pH optimum r-PL-STR found be 10.0, it exhibited >70% the maximal activity at 12.0. After incubation 37°C 1 h substrate, retained more than 55% 7.0–12.0. Compared with commercial complex Scourzyme@301L Novozymes, similar efficacy reducing intrinsic viscosity polygalacturonic acid (49.0 vs. 49.7%). When combined cellulase α-amylase, had comparable performance bioscouring jute fabric (22.39 22.99%). Thus, might represent good candidate use alkaline industries such as textile.
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