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Purification and some properties of β-mannanase fromBacillussp.

✍ Scribed by T. Ooi; D. Kikuchi

Publisher
Springer
Year
1995
Tongue
English
Weight
476 KB
Volume
11
Category
Article
ISSN
1573-0972

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✦ Synopsis

p-Mannanase produced by Bucillus sp. W-2, isolated from decayed commercial konjak cake, was purified from the culture supernatant by (NHJZ SO4 precipitation, adsorption to konjak gel, and calm chromatography with DEAE-cellulose, Sephadex G-100 and Sephacryl S-200. Its molecular size was estimated by SDS-PAGE as 40 kDa, and by gel filtration as 36 kDa. The enzyme was most active at pH 7 and 7O'C and was stable for at least 1 h between pH 5 and 10 and below 6O'C. Its activity was completely inhibited by Hg". The enzyme hydrolysed galactomannan better than glucomannan and mainly produced mannose and mannobiose.

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Extracellular mannanase from Bacillus subtilis NM-39, an isolate from Philippine soil, was purified about 240-fold with a yield of 7.3% by ammonium sulphate fractionation, DEAE-Toyopearl chromatography and Sephacryl S-200 gel filtration. Its Mr was 38 kDa and it had a pI of 4.8 and optimum activity