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KMID : 1101320050370020078
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Korean Journal of Clinical Laboratory Science
2005 Volume.37 No. 2 p.78 ~ p.83
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A Study on the Purification and Characteristics of Branched-Chain Amino Acid Aminotransferase in Cultural Mycelia of Cordyceps militaris
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Kim Sung-Tae
Park Chung-Oh
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Abstract
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The optimum conditions of Cordyceps militaris mycelial growth, purification and characteristics of branched-chain amino acid aminotransferase [BCAT(EC 2.6.1.42)] in this mycelium were studied. Optimum pH, temperature and medium of culture of mycelia were 5.5, 22.5℃ and Hamada medium (HM), respectively. BCAT in homogenate of this mycelia was precipitated by 20-40% saturated solution of ammonium sulfate and then purified by DEAE (diethylaminoethyl)-Sephadex A-50 column chromatography with linear concentration gradient and Sephadex G-200 gel filtration. A single band of purified enzyme was detected on SDS-PAGE (sodium dodecylsulfate-polyacrylamide gel electrophoresis). Optimum pH and temperature of BCAT were found to be 7.8 and 29℃, respectively. It showed activity toward L-leucine, L-isoleucine and L-valine as a substrate. The Km values of this enzyme for L-leucine were determined to be 5.88 mM for L-leucine.
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KEYWORD
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Cordyceps militaris, Branched-chain amino acid aminotransferase, Purification, Cultural mycelia
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