Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PURIFICATION AND PARTIAL CHARACTERIZATION OF D-(-)-LACTATE DEHYDROGENASE FROM LACTOBACILLUS-HELVETICUS CNRZ-32
Autore:
BHOWMIK T; LUECK KM; STEELE JL;
Indirizzi:
UNIV WISCONSIN,DEPT FOOD SCI MADISON WI 53706 UNIV WISCONSIN,DEPT FOOD SCI MADISON WI 53706
Titolo Testata:
Journal of industrial microbiology
fascicolo: 1, volume: 12, anno: 1993,
pagine: 35 - 41
SICI:
0169-4146(1993)12:1<35:PAPCOD>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-LACTATE DEHYDROGENASE; LACTIC DEHYDROGENASES; FLAVOR DEVELOPMENT; ESCHERICHIA-COLI; GOUDA CHEESE; PROTEOLYSIS; CLONING; GENE;
Keywords:
LUCTOBACILLUS-HELVETICUS; LACTATE DEHYDROGENASE; PURIFICATION; CHARACTERIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
T. Bhowmik et al., "PURIFICATION AND PARTIAL CHARACTERIZATION OF D-(-)-LACTATE DEHYDROGENASE FROM LACTOBACILLUS-HELVETICUS CNRZ-32", Journal of industrial microbiology, 12(1), 1993, pp. 35-41

Abstract

D-(-)-Lactate dehydrogenase (LDH) was purified to homogeneity from a cell-free extract of Lactobacillus helveticus CNRZ 32. The native enzyme was determined to have a molecular weight of 152 000 and consisted of four identical subunits of 38 000. This enzyme was NAD dependent, fructose 1,6-diphosphate (FDP) and ATP independent. It was most active on pyruvate followed by beta-hydroxypyruvate as substrates. The K(m) values for Pyruvate and D-(-)-lactate were 0.64 and 68.42 mM respectively, indicating that the enzyme has a higher affinity for pyruvate. Theenzyme activity was completely inhibited by p-chloromercuribenzoate (1 mM) and partially by iodoacetate, suggesting the involvement of the sulfhydryl group (-SH) in catalysis. Optima for activity by the purified enzyme were pH 4.0 and 50-60-degrees-C. Limited inhibition of D-(-)-LDH was observed with several divalent cations. Additionally, HgCl2 was observed to strongly inhibit enzyme activity. The purified enzyme was not affected by dithiothreitol or any of the metal chelating agentsexamined.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:28:17