Purification and properties of L-methionine γ-lyase from Aeromonas sp.
Purification and properties of L-methionine γ-lyase from Aeromonas sp.
复制标题
气单胞菌 L-蛋氨酸 γ-裂解酶的纯化和性质。
DOI:
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发表时间:
1984
期刊:
影响因子:
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通讯作者:
K. Soda
中科院分区:
文献类型:
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作者:
Torn Nakayama;N. Esaki;Woon Joo Lee;I. Tanaka;Hidehiko Tanaka;K. Soda
methanethiol and ammonia. We have purified the enzyme from Pseudomonasputida ( = Ps. ovalis) to characterize it. 1 >2) Based on the multi-catalytic function of the enzyme it is applicable to the production of various optically active sulfur and selenium amino acids as reviewed previously.3) This usefulness of the enzymehas shownthe necessity of obtaining an microorganism that produces the enzyme effectively. We have isolated bacterial strain from lake water that shows 10-times higher L-methionine y-lyase activity (per wet weight of cells) than Ps. putida, and identified it as Aeromonas sp. in the present study. Wehere describe the purification of the enzyme from the bacterial cells to homogeneity and its characterization. We have made many attempts to isolate microorganisms that can grow in a medium (pH 7.2) containing 0.5% L-methionine as a sole carbon and nitrogen source. Several bacterial strains isolated from soil, and drainage, river and lake water showed high L-methionine y-lyase