The Journal of General and Applied Microbiology
Online ISSN : 1349-8037
Print ISSN : 0022-1260
ISSN-L : 0022-1260
ETUDE D'UNE L-α-AMINOAMIDASE PARTICULAIRE DE BREVIBACTERIUM SP. EN VUE DE L'OBTENTION D'ACIDES α-AMINES OPTIQUEMENT ACTIFS
MARIE-PAULE KIENY-L'HOMMEALAIN ARNAUDPIERRE GALZY
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1981 年 27 巻 4 号 p. 307-325

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The L-α-aminoamidase of Brevibacterium A4 is a particle enzyme with a molecular weight of 135, 000; its optimum pH is 9.5 and its optimum temperature 60°. It is probably a metallo-enzyme with an SH group in the active site, and requiring the presence of Mg2+ or Mn2+. The purification tests showed that it hydrolyses a large number of α-aminoamides. The Michaelis constant Km varies little for the different substrates. On the other hand the Vm varies greatly, in particular according to the hydrocarbon chain length.
The use of the α-amidoamidasic activity for the preparation of optically active, natural or non-natural α-aminoacids has been considered.
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© The Microbiology Research Foundation
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