Streptomyces lividans에 재조합된 L-1,3 glucanase의 특성
The Characteristics of α-1,3 Glucanase from Transformant Streptomyces lividans T1027
윤정원, 한홍근,
소속 상세정보
윤정원 ( ) - 수원대학교
한홍근 ( ) - 수원대학교
KMID : 0355419950190040409
Abstract
The α-1,3 glucanase gene from Streptomyces sp. SW403 was cloned into Streptomyces lividans 1326JI with plasmid pIJ702 for high and stable production of α-1,3 glucanase. Genomic DNA from Streptomyces sp. SW403 was partially digested with the
transformation into Streptomyces lividans 1326JI. This transfromant encoded α-1,3 glucanase and was named Streptomyces lividans T1027. The enzyme was partially purfied by 30-70% (NH4) 2SO4 precipitation. The cloned enzyme activity was higer and
more
stable than the enzyme from Streptomyces sp. SW403. The optimum pH and temperature of the wild and cloned enzyme were pH 6.5 and 37%, respectively. The activity of cloned enzyme was more stable than wild enzyme at 60℃ below, respectively.
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