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Enzyme Research
Data on enzyme research described by researchers at Kasetsart University
May 21st, 2008
According to recent research from Bangkok, Thailand, "Purification of beta-1,3-1,4-glucanase from the cell-free culture fluid of Bacillus subtilis GN156 by affinity chromatography of epoxy-activated sepharose 6B and ultrafiltration technique resulted in homogeneous J1 and partially purified pJ2 enzymes. The molecular weight and pI of J1 were 25 kDa and 3.5, respectively, while those for J2 were 90 kDa and 3.6, respectively." "Both beta-1,3-1,4-glucanase J1 and pJ2 had optimum pH values of 6-6.5 and an optimum temperature of 60 C. Both enzymes were not inhibited by Li2+ but were inhibited significantly by Ca2+, Cu2+, Mn2+ and Zn2+. However, J1 was slightly inhibited by...
Source: Fitness & Wellness Business Week (2008-05-21)
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