Characteristics of Thermostable Pullulanase from Bacillus stearothermophilus and the Nucleotide Sequence of the Gene
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概要
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Thermostable pullulanase was purified to homogeneity on sodium dodecyl sulfate-polyacrylamide gel from the culture supernatant of Bacillus stearothermophilus TRS128. However, multiformity of the pullulanase was suggested by activity staining on a pullulan-reactive red plate. The thermostability of the enzyme was tested. In the presence of Ca^<2+>, the optimum temperature of the pullulanase was 75℃, and nearly 100% of the enzyme activity was retained even after treatment at 68℃ for 60 min. Shince the thermostable pullulanase gene (pulT) has been cloned, the nucleotide sequence was determined. Although the DNA sequence revealed only one large open reading frame, two possible pairs of SD sequence and initiation codon were found in the frame. To analyze the regulatory region, several mutations (deletion, insertion and substitution of nucleotides) were introduced in the flanking region of pulT, using site-directed mutagenesis. A putative promoter, SD sequence and initiation codon were inferred. The pulT gene was composed of 1974 bases and 658 amino acid residues (molecular weight 75,375). The deduced amino acid sequence of the thermostable pullulanase exhibited a fairly low homology with that of the thermolabile pullulanase from Klebsiella aerogenes. However, four consensus sequences containing catalytic and/or substrate binding sites for amylolytic enzymes were also found in the themostable pullulanase and the thermolabile enzyme.
- 公益社団法人日本生物工学会の論文
- 1990-04-25
著者
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Park Jong-hyun
Department Of Fermentation Technology Faculty Of Engineering Osaka University
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Kuriki Takashi
Department Of Bioptechnology Faculty Of Engineering Osaka University
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Imanaka Tadayuki
Department Of Applied Biotechnology Faculty Of Engineering Osaka University
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Kuriki Takashi
Department Of Fermentation Technology Faculty Of Engineering Osaka University
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