Title Byssochlamys fulca가 생성하는 펙틴질 분해효소에 관한 연구
Author 남영중 · 김남우 · 홍순우 *
Address 농어촌개발공사 식품연구소 · * 서울대학교 자연대 미생물학과
Bibliography Korean Journal of Microbiology, 21(2),86-94, 1983
DOI
Key Words Studies on the Pectolytic Enzymes from Byssochlamys fulva
Abstract Polygalacturonase of Byssochlamys fulva was purified and characterized. Specific activity increased from 2.21 units/mg protein to 10.47 units/mg protein through (NH₄)₂SO₄, treatment, SephadexG-100 gel filtration, and DEAE-Sephadex ion exchange chromatography. Divalent cations, such as Ca^++ and Cu^++, increased polygalacturonase activity greatly. Added as 10^-3 M concentration, Ca^++ ion enhanced enzyme activity 9.8folds. Optimum temperature was 50℃ and optimum pH was 5.0. Activation energy of reaction was 8.69 Kcal/mole. Michaelis-Menten constant(K_M) and V_max of reaction were 6.27 × 10^-3 moles/1 and 2.85umoles/min. Polygalacturonase of Byssochlamys fulva preferred polygalacturonic acid to pectin as substrate and was presumed as endo-type on the basis of the relationship between viscosity reduction and substrate degradation. Molecular weight of polygalacturonase was estimated as 55,000.
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