Isolation and Partial Characterization of Keratinase from Trichophyton sp.

被引：0

作者：

Parlak, Donay ^{[1
]}

Tanis, Huseyin ^{[1
]}

Aygan, Ashabil ^{[1
]}

机构：

[1] Kahramanmaras Sutcuimam Univ, Fen Edebiyat Fak, Biyol Bolumu, Avsar Kampusu, Onikisubat, K Maras, Turkey

来源：

KSU TARIM VE DOGA DERGISI-KSU JOURNAL OF AGRICULTURE AND NATURE | 2020年 / 23卷 / 05期

关键词：

Trichophyton sp; Keratinase; Purification; Characterization; EXTRACELLULAR PROTEINASE; KERATINOLYTIC ACTIVITY; FEATHER DEGRADATION; CHICKEN FEATHER; PURIFICATION; PROTEASE; ALKALINE; STRAIN; ENZYMES;

D O I：

10.18016/ksutarimdoga.vi.678756

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Keratinase enzyme production was accomplished from Trichophyton sp. Tr-9 in minmal medium containing feather meal. Enzyme was purified with Ammonium sulfate, Sephadeks G-100 and DEAE Sepharose column. Maxiumum keratinolitik activity was obtained at pH 7.5 and 37 degrees C. Enzyme was higly stabil between pH 5.5-7.5 and 20-40 degrees C. With the SDS-Page analysis of the enzyme, molecular weight of the enzyme was calculated as 34 kDa. CaCI2 (5mM) had a stimultory effect (148%) on enzyme. On the other hand, EDTA (5mM) and SDS (%1) inhibited enzyme acitivity up to 49% and 49%, respectively. PMSF (1-5mM) has strongly inhibited enzyme. As a result, physicochemical properties of the enzymeshowed that Trichophyton sp. Tr-9 could be useful in various industrial and biotechnological applications.

引用

页码：1135 / 1143

页数：9

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