Open AccessCrystallisation and molecular properties of d ‐2‐hydroxyisocaproate dehydrogenase from Lactobacillus casei
Author(s) -
Kallwass Helmut,
Tsai Hsin,
Schütte Horst
Publication year - 1987
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1987.tb02155.x
Subject(s) - lactobacillus casei , lactobacillus , microbiology and biotechnology , lactobacillaceae , chemistry , dehydrogenase , crystallization , biology , food science , biochemistry , enzyme , fermentation , organic chemistry
d ‐2‐Hydroxyisocaproate dehydrogenase ( d ‐HicDH) from Lactobacillus casei ssp. pseudoplantarum (DSM 20008) has been purified by liquid‐liquid extraction in aqueous two‐phase systems, ion‐exchange chromatography on DEAE ‐ cellulose, hydrophobic ionic chromatography on Amberlite CG‐50I and interfacial salting out on Sepharose CL‐4B columns. The homogeneous d ‐HicDH has been crystallised. N‐terminal sequence analysis of the crystalline enzyme molecules established that d ‐HicDH is a dimeric enzyme composed of two identical polypeptide chains of 38 kDa. No cysteine or cystine residue was found in the purified enzyme.