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D‐Amino acid oxidase activity form Rhodosporiduim toruloides
Author(s) -
Lee Y.H.,
Chu W.S.
Publication year - 1996
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1996.tb00190.x
Subject(s) - oxidase test , benzoic acid , enzyme , chemistry , amino acid , side chain , alanine , d amino acid oxidase , biochemistry , stereochemistry , organic chemistry , polymer
The D‐amino acid oxidase activity of Rhodosporidium toruloides CCRC 20306 was studied. The enzyme could be induced by D‐alanine, and had pH and temperature optima of 8.5 and 60d̀C, respectively. D‐Amino acids with polar uncharged and/or nonpolar side chain were good substrates for the D‐amino acid oxidase of CCRC 20306, whereas those with polar charged side chain were poor substrates. Benzoic acid and its derivatives were inhibitory to the enzyme activity.