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Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme.
The crystal structure of the catalytic domain of alkaline cellulase K was determined and a mechanism similar to that previously proposed for alkaline proteases was suggested, which appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range.
Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237
Abstract Thermostable alkaline cellulase (endo-1,4-β-glucanase, EC activity was detected in the culture medium of a strictly alkaliphilic strain of Bacillus, designated KSM-S237. This novel
Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16
Alkaline protease (EC activity, suitable for use in detergents, was detected in the alkaline culture medium of Bacillus sp. KSM-K16, which was originally isolated from soil. The enzyme,
A novel alkaline endoglucanase from an alkaliphilic Bacillus isolate: enzymatic properties, and nucleotide and deduced amino acid sequences
Abstract. A highly alkaline endo-1,4-β-glucanase (Egl) was purified to homogeneity from a culture broth of alkaliphilic Bacillus sp. strain KSM-N252. The optimal pH for activity was as high as 10,
Cloning and sequencing of a high-alkaline pectate lyase gene from an alkaliphilic Bacillus isolate.
Pel-103 appeared to have a similar core and active site topology to the enzymes of known structure from Erwinia chrysanthemi and Bacillus subtilis, and physicochemical and catalytic properties of Pel-103 were different from those of other enzymes reported so far.
Purification and properties of mangano-superoxide dismutase from a strain of alkaliphilic Bacillus
A mangano-superoxide dismutase (EC 1.15.1) was purified to homogeneity from a strain of alkaliphilic Bacillus for the first time and the properties of the superoxide dismUTase were compared with those of the enzyme from thermophilic Bacillin stearothermophilus.
Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: its catalytic properties and deduced amino acid sequence
The purified recombinant enzyme had an isoelectric point of pH 9.7 and a molecular mass of 34 kDa, and exhibited a very high specific activity compared with known pectate lyases reported so far, and struck stabilization by 100 mM NaCl was observed in a pH range from 5 to 11.5.