Purification and characterization of extracellular tannin acyl hydrolase from Aspergillus heteromorphus MTCC 8818

• Published in: Biotechnology and bioprocess engineering Vol. 15; no. 5; pp. 793 - 799
• Main Authors: Chhokar, Vinod, Seema, Beniwal, Vikas, Salar, Raj Kumar, Nehra, K. S., Kumar, Anil, Rana, J. S.
• Format: Journal Article
• Language: English
• Published: Heidelberg The Korean Society for Biotechnology and Bioengineering 01.10.2010; Springer Nature B.V; 한국생물공학회
• Subjects: Acids; Ammonium; Ammonium sulfate; Aspergillus; Benzene; Biotechnology; Calcium; Cellulose; Chelating agents; Chemistry; Chemistry and Materials Science; Chromatography; Column chromatography; Copper; Edetic acid; Enzymatic activity; Enzyme inhibitors; Enzymes; Ethanol; Fermentation; Fungi; Glycerol; hydrolase; Industrial and Production Engineering; Ion exchange; Ions; Iron; isopentyl alcohol; Magnesium; Metals; Methanol; Organic solvents; pH effects; Precipitation; Purification; Research Paper; Sodium lauryl sulfate; Soil; Solvents; Studies; Sulfates; Surfactants; Tannase; Tannic acid; Temperature; Temperature effects; Toluene; Zinc; 생물공학; tannic acid; metal ion; tannase; organic solvent; DEAE-cellulose
• ISSN: 1226-8372; 1976-3816
• DOI: 10.1007/s12257-010-0058-3

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°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°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 Cd 2+ 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).