Purification and Characterization of Thermostable Pullulanase from Bacillus stearothermophilus and Molecular Cloning and Expression of the Gene in Bacillus subtilis
AUTOR(ES)
Kuriki, Takashi
RESUMO
A thermostable pullulanase (α-dextrin 6-glucanohydrolase [EC 3.2.1.41]) from a newly isolated Bacillus stearothermophilus strain (TRS128) was purified and characterized. The enzyme hydrolyzed (1→6)-α-d-glucosidic linkages of pullulan to produce maltotriose, and the optimum temperature was 65°C. About 90% of the enzyme activity was retained after treatment at 65°C for 60 min. By using pTB522 as a vector plasmid, the pullulanase gene was cloned and expressed in Bacillus subtilis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=204393Documentos Relacionados
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