2000Journal of Industrial Microbiology & BiotechnologyRequires access

Production and characterization of thermostable xylanase and pectinase from Streptomyces sp. QG-11-3

Qasim Khalil Beg, Bharat Bhushan, M. Kapoor, Gurinder Singh Hoondal

Open publisher page 188 citations

Abstract

Streptomyces sp. QG-11-3, which produces a cellulase-free thermostable xylanase (96 IU ml−1) and a pectinase (46 IU ml−1), was isolated on Horikoshi medium supplemented with 1% w/v wheat bran. Carbon sources that favored xylanase production were rice bran (82 IU ml−1) and birch-wood xylan (81 IU ml−1); pectinase production was also stimulated by pectin and cotton seed cake (34 IU ml−1 each). The partially purified xylanase and pectinase were optimally active at 60°C. Both enzymes were 100% stable at 50°C for more than 24 h. The half-lives of xylanase and pectinase at 70, 75 and 80°C were 90, 75 and 9 min, and 90, 53 and 7 min, respectively. The optimum pH values for xylanase and pectinase were 8.6 and 3.0, respectively, at 60°C. Xylanase and pectinase were stable over a broad pH range between 5.4 and 9.4 and 2.0 to 9.0, respectively, retaining more than 85% of their activity. Ca2+ stimulated the activity of both enzymes up to 7%, whereas Cd2+, Co2+, Cr3+, iodoacetic acid and iodoacetamide inhibited xylanase up to 35% and pectinase up to 63%; at 1 mM, Hg2+ inhibited both enzymes completely. Journal of Industrial Microbiology & Biotechnology (2000) 24, 396–402.

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Streptomyces sp. QG-11-3, which produces a cellulase-free thermostable xylanase (96 IU ml−1) and a pectinase (46 IU ml−1), was isolated on Horikoshi medium supplemented with 1% w/v wheat bran. Carbon sources that favored xylanase production were rice bran (82 IU ml−1) and birch-wood xylan (81 IU ml−1); pectinase production was also stimulated by pectin and cotton seed cake (34 IU ml−1 each). The partially purified xylanase and pectinase were optimally active at 60°C. Both enzymes were 100% stable at 50°C for more than 24 h. The half-lives of xylanase and pectinase at 70, 75 and 80°C were 90, 75 and 9 min, and 90, 53 and 7 min, respectively. The optimum pH values for xylanase and pectinase were 8.6 and 3.0, respectively, at 60°C. Xylanase and pectinase were stable over a broad pH range between 5.4 and 9.4 and 2.0 to 9.0, respectively, retaining more than 85% of their activity. Ca2+ stimulated the activity of both enzymes up to 7%, whereas Cd2+, Co2+, Cr3+, iodoacetic acid and iodoacetamide inhibited xylanase up to 35% and pectinase up to 63%; at 1 mM, Hg2+ inhibited both enzymes completely. Journal of Industrial Microbiology & Biotechnology (2000) 24, 396–402.

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Available abstract

Streptomyces sp. QG-11-3, which produces a cellulase-free thermostable xylanase (96 IU ml−1) and a pectinase (46 IU ml−1), was isolated on Horikoshi medium supplemented with 1% w/v wheat bran. Carbon sources that favored xylanase production were rice bran (82 IU ml−1) and birch-wood xylan (81 IU ml−1); pectinase production was also stimulated by pectin and cotton seed cake (34 IU ml−1 each). The partially purified xylanase and pectinase were optimally active at 60°C. Both enzymes were 100% stable at 50°C for more than 24 h. The half-lives of xylanase and pectinase at 70, 75 and 80°C were 90, 75 and 9 min, and 90, 53 and 7 min, respectively. The optimum pH values for xylanase and pectinase were 8.6 and 3.0, respectively, at 60°C. Xylanase and pectinase were stable over a broad pH range between 5.4 and 9.4 and 2.0 to 9.0, respectively, retaining more than 85% of their activity. Ca2+ stimulated the activity of both enzymes up to 7%, whereas Cd2+, Co2+, Cr3+, iodoacetic acid and iodoacetamide inhibited xylanase up to 35% and pectinase up to 63%; at 1 mM, Hg2+ inhibited both enzymes completely. Journal of Industrial Microbiology & Biotechnology (2000) 24, 396–402.

Key concepts: Xylanase, Pectinase, Xylan, Food science, Bran, Cellulase, Chemistry, Enzyme

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