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Purification and Characterization of Extracellular Tannin Acyl Hydrolase from Aspergillus heteromorphus MTCC 8818
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  • Purification and Characterization of Extracellular Tannin Acyl Hydrolase from Aspergillus heteromorphus MTCC 8818
저자명
Chhokar. Vinod,Seema. Seema,Beniwal. Vikas,Salar. Raj Kumar,Nehra. K.S.,Kumar. Anil,Rana. J.S.
간행물명
Biotechnology and bioprocess engineering
권/호정보
2010년|15권 5호|pp.793-799 (7 pages)
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한국생물공학회
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

A tannase (E.C. 3.1.1.20) producing fungal strain was isolated from soil and identified as Aspergillus heteromorphus MTCC 8818. Maximum tannase production was achieved on Czapek Dox minimal medium containing 1% tannic acid at a pH of 4.5 and $30^{circ}C$ after 48 h incubation. The crude enzyme was purified by ammonium sulfate precipitation and ion exchange chromatography. Diethylaminoethyl-cellulose column chromatography led to an overall purification of 39.74-fold with a yield of 19.29%. Optimum temperature and pH for tannase activity were $50^{circ}C$ and 5.5 respectively. Metal ions such as $Ca^{2+}$, $Fe^{2+}$, $Cu^{1+}$, and $Cu^{2+}$ increased tannase activity, whereas $Hg^{2+}$, $Na^{1+}$, $K^{1+}$, $Zn^{2+}$, $Ag^{1+}$, $Mg^{2+}$, and $Cd2+$ acted as enzyme inhibitors. Various organic solvents such as isopropanol, isoamyl alcohol, benzene, methanol, ethanol, toluene, and glycerol also inhibited enzyme activity. Among the surfactants and chelators studied, Tween 20, Tween 80, Triton X-100, EDTA, and 1, 10-o-phenanthrolein inhibited tannase activity, whereas sodium lauryl sulfate enhanced tannase activity at 1% (w/v).