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Biochemical Properties of Thermostable d‐Hydantoinase from Bacillus thermocatenulatus GH‐2
Author(s) -
PARK JOOHO,
KIM GEUNJOONG,
LEE SEUNGGOO,
KIM HAKSUNG
Publication year - 1998
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1998.tb10334.x
Subject(s) - library science , biological sciences , annals , biology , computer science , geography , microbiology and biotechnology , archaeology
D-Hydantoinase is currently employed as a biocatalyst for the production of optically pure D-amino acids, which are intermediates for the synthesis of semisynthetic antibiotics, peptide hormone, pyrethroids, and pesticides. In the process developed by the Yamada group,1,2 DL-5-substituted hydantoin is asymmetrically hydrolyzed to the N-carbamoyl-D-amino acid by D-specific hydantoinase, and this product is further chemically or biologically converted to the corresponding D-amino acid. The operational stability of the enzyme is considered as one of the most important factors because the short half-life of the enzyme often limits the development of the enzymatic process. As an effective way of producing thermostable enzymes with great biotechnological potential, isolation of an enzyme from thermophiles has attracted much attention. We have been focusing on the screening of thermostable D-hydantoinase-producing thermophiles3 and have attempted to isolate a thermostable D-hydantoinase with high affinity toward hydantoins with an aromatic group at the 5 -position. A thermostable D-hydantoinase was isolated from Bacillus thermocatenulatus GH-2 and purified to homogeneity by using immunoaffinity chromatography. Biochemical characteristics of the enzyme were investigated.