Showing papers by "T.S. Chandra published in 1992"
TL;DR: An extracellular xylanase enzyme fraction A from a mesophilicClostridium strain SAIV was purified by ammonium sulfate precipitation, Sephadex G-50 gel filtration and DEAE-SephadeX A-50 ion exchange supporting the view that the multiplicity of xylanases is common in microorganisms.
Abstract: An extracellular xylanase enzyme fraction A from a mesophilicClostridium strain SAIV was purified by ammonium sulfate precipitation, Sephadex G-50 gel filtration and DEAE-Sephadex A-50 ion exchange. The xylanase exhibited a molecular weight of ≁30,000 and it was stable upto 55° C with an optimum temperature of 50° C. It was most stable between pH 5–7, with an optimum pH of around 6. The Km value was 7.0 mg·xylan ml-1 and Vmax was 36 μmol·xylose liberated mg-1 min-1. Carboxymethyl cellulose, filter paper cellulose and 4-p-nitrophenyl β-D-xylopyranoside were not hydrolysed. The specific activity of xylanase fraction A (9.8 U mg-1) is 2–10 fold higher than the specific activity of xylanase in other mesophilic, xylanolytic, obligate anaerobic bacteria. A minor fraction of xylanase activity designated as xylanase B was also obtained supporting the view that the multiplicity of xylanases is common in microorganisms.
7 citations