Purification and Properties of a Malolactic Enzyme from a Strain of Leuconostoc mesenteroides Isolated from Grapes | Zendy

Aline LonvaudFunel | Zendy; Ana M. Strasser de Saad | Zendy

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Purification and Properties of a Malolactic Enzyme from a Strain of Leuconostoc mesenteroides Isolated from Grapes

Author(s) -

Aline LonvaudFunel,

Ana M. Strasser de Saad

Publication year - 1982

Publication title -

applied and environmental microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.552

H-Index - 324

eISSN - 1070-6291

pISSN - 0099-2240

DOI - 10.1128/aem.43.2.357-361.1982

Subject(s) - leuconostoc mesenteroides , malolactic fermentation , isoelectric point , leuconostoc , strain (injury) , isoelectric focusing , fructose , enzyme , biochemistry , chemistry , tartrate , non competitive inhibition , enzyme assay , bacteria , chromatography , biology , lactic acid , lactobacillus , genetics , anatomy , fermentation

An enzymatic complex able to transforml -malate tol -lactate was obtained from aLeuconostoc mesenteroides strain isolated from grapes. The molecular weight was about 235,000, the isoelectric point was at pH 4.35, and the optimal pH for activity was 5.75. The malolactic activity followed a sequential pattern concerning the involved substrates. At pH values substantially different from the optimum, a positive cooperativity between malate molecules was observed. Oxamate, fructose-1, 6-diphosphate, andl -lactate acted as noncompetitive inhibitors, whereas succinate, citrate, and tartrate isomers produced a competitive inhibition.

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