Malolactic enzyme of Lactobacillus plantarum. Purification, properties, and distribution among bacteria.
Year: 1983
Type: article
Abstract: The malolactic enzyme of Lactobacillus plantarum was purified from 5.5 units/mg to a specific activity of 265 units/mg of protein. The enzyme has an isoelectric point of pH 4.4. The molecular weight is Mr = 140,000 as determined by gradient gel electrophoresis. The enzyme consists of two probably identical subunits (Mr = 70,000) that were observed after treatment with sodium dodecyl sulfate. Malolactic enzyme catalyzes the NAD- and manganese-dependent reaction L-malate leads to CO2 + L-lactate. Therefore, this enzyme can be distinguished from the well known malic enzymes (L-malate: NAD+ oxidoreductase, oxalacetate-decarboxylating EC 1.1.1.38 or 1.1.1.39). Malolactic enzyme is found in most lactic acid bacteria (Lactobacteriaceae); it has not been detected in other bacteria.
Source: Journal of Biological Chemistry
Authors: G Caspritz, F Radler
Institution: Johannes Gutenberg University Mainz
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1660877423