• Journal of Microbiology and Biotechnology
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• v.5 no.2
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• pp.92-95
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• 1995

Halophilic Pseudomonas sp.W7 isolated from laver in the southem sea of Korea showed alginate lyase activity. Gene (aly) encoding alginate lyase was cloned in E.coli JM83 and the N-terminal amino acid sequence of the enzyme was determined after purificaion. The recombinant enzyme has been shown to have a molecular weight of about 40kDa after 12% SDS-polyacrylamide gel electrophoresis.

• Journal of Microbiology
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• v.33 no.2
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• pp.109-114
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• 1995

Alkalophilic Cephalosporium sp. RYM-202 produced multiple xylanases extracellularly. One of these xylanases was purified to electrophoretical homogeneity by chromatography with DEAE-Sephadex A-50, Sephacryl S-200 HR and Superose 12 HR. The purified xylanase differed from most other microbial xylanases in that it had low-molecular weight and acidic isoelectric point. The molecular weight of the xylanase in that it had low-molecular weight and acidic isoelectric point. The molecular weight of the xylanase was 23 kDa by SDS-polyacrylamide electrophoresis and 24 kDa by gel permeation chromatography, and the isoelectric point was 4.3. The xylanase had the highest activity permentation chromatography, and the isoelectric point was 4.3. The xylanase had the highest activity permeation chromatography, and the isoelectric point was 4.3. The xylanase had the highest activity at pH 8.0 and 50 .deg.C. It was stable over a wide range of pH and retained more than 80% of its original activity after 24 h of incubation even at pH 12. The Km values of this enzyme on birchwood xylan and oat spelts xylan were 2.33 and 3.45 mg/ml, respectively. The complete inhibition of the enzyme of n-bromosuccinimide suggests the involvement of tryptophan in the active site. The sylanase lacked activity towards crystalline cellulose and carboxymethyl cellulose.