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.