Properties of lactate dehydrogenase in a psychrophilic marine bacterium.
نویسندگان
چکیده
Lactate dehydrogenase (EC 1.1.1.27) from Vibrio marinus MP-1 was purified 15-fold and ammonium activated. The optimum pH for pyruvate reduction was 7.4. Maximum lactate dehydrogenase activity occurred at 10 to 15 degrees C, and none occurred at 40 degrees C. The crude-extract enzyme was stable between 15 and 20 degrees C and lost 50% of its activity after 60 min at 45 degrees C. The partially purified enzyme was stable between 8 and 15 degrees C and lost 50% of its activity after 60 min at 30 degrees C. The thermal stability of lactate dehydrogenase was increased by mercaptoethanol, with 50% remaining activity at 42 degrees C.
منابع مشابه
Complete Genome Sequence of Exiguobacterium sp. Strain N4-1P, a Psychrophilic Bioemulsifier Producer Isolated from a Cold Marine Environment in North Atlantic Canada
Here, we present the complete genome sequence of Exiguobacterium sp. strain N4-1P, a psychrophilic bacterium that produces bioemulsifier, isolated for the first time from petroleum hydrocarbon-contaminated sediment samples from shoreline Newfoundland, Canada. Many strains of the genus Exiguobacterium are extremophiles and have properties of biotechnological interest.
متن کاملActivity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments.
Lactate dehydrogenase (LDH) catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis. In the present study, we present a comparative biochemical and structural analysis of various LDHs adapted to function over a large temperature range. The enzymes were from Champsocephalus gunnari (an Antarctic fish), Deinococcus radioduran...
متن کاملStructure Analysis of a New Psychrophilic Marine Protease
A new psychrophilic marine protease was found from a marine bacterium Flavobacterium YS-80 in the Chinese Yellow Sea. The protease is about 49 kD with an isoelectric point about 4.5. It consists of 480 amino acids and is homologous to a psychrophilic alkaline protease (PAP) from an Antarctic Pseudomonas species. The protein was purified from the natural bacterium fermented and crystallized. Its...
متن کاملThe levels of Serum Alkaline Phosphatase and Lactate Dehydrogenase in Hodgkin Lymphoma
Background: Hodgkin’s disease (HD) is a neoplastic disease originating in lymphoid tissue, which spreads to lymphoid structures and ultimately nonlymphoid tissues. Lactate Dehydrogenase and Alkaline Phosphatase are increased in blood following membrane cell damage. The aim of this study was to compare Lactate Dehydrogenase and Alkaline Phosphatase levels in children in different stages of Hodg...
متن کاملAnalysis of the amino acid residues involved in the thermal properties of the monomeric isocitrate dehydrogenases of the psychrophilic bacterium Colwellia maris and the mesophilic bacterium Azotobacter vinelandii.
Cold-adapted monomeric isocitrate dehydrogenase of a psychrophilic bacterium, Colwellia maris, (CmIDH) showed a high degree of amino acid sequential identity (69.5%) to a mesophilic nitrogen-fixing bacterium, Azotobacter vinelandii, (AvIDH). In this study, three Ala residues of CmIDH and the corresponding Pro residues of AvIDH were exchanged by site-directed mutagenesis, and several properties ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Applied and environmental microbiology
دوره 49 5 شماره
صفحات -
تاریخ انتشار 1985