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      • SCIESCOPUSKCI등재

        New Action Pattern of a Maltose-forming α-Amylase from Streptomyces sp. and its Possible Application in Bakery

        ( Youssef Ben Ammar ),( Takayoshi Matsubara ),( Kazuo Ito ),( Masaru Lizuka ) 생화학분자생물학회 2002 BMB Reports Vol.35 No.6

        An α-amylase(EC 3.2.1.1) was purified that catalyses the production of a high level of maltose from starch without the attendant production of glucose. The enzyme was produced extracellularly by thermophilic Streptomyces sp. that was isolated from Thailand`s soil. Purification was achieved by alcohol precipitation, DEAE-Cellulose, and Gel filtration chromatographies. The purified enzyme exhibited maximum activity at PH 6-7 and 60℃. It had a relative molecular mass of 45 kDa, as determined by SDS-PAGE. The hydrolysis products from starch had α-anomeric forms, as determined by ^1H-NMR. This-maltose-forming α-amylase completely hydrolyzed the soluble starch to produce a high level of maltose, representing up to 90%. It hydrolyzed maltotetrose and maltotriose to primarily produce maltose (82% and 62%, respectively) without the attendant production of glucose. The high maltose level as a final end-product from starch and maltooligosaccharides, and the unique action pattern of this enzyme, indicate an unusual maltose-forming system. After the addition of the enzyme in the bread-baking process, the bread`s volume increased and kept its softness longer than when the bread had no enzyme.

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