Open Access Original article

Heterologous expression of Oenococcus oeni malolactic enzyme in Lactobacillus plantarum for improved malolactic fermentation

Christina Schümann12, Herbert Michlmayr1, Reinhard Eder2, Andrés M del Hierro1, Klaus D Kulbe1, Geir Mathiesen3 and Thu-Ha Nguyen1*

Author Affiliations

1 Food Biotechnology Lab, Department of Food Sciences and Technology, University of Natural Resources and Life Sciences, Vienna, Austria

2 Federal College and Research Institute for Viticulture and Pomology (HBLAuBA), Klosterneuburg, Austria

3 Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway

For all author emails, please log on.

AMB Express 2012, 2:19  doi:10.1186/2191-0855-2-19

Published: 27 March 2012

Abstract

Lactobacillus plantarum is involved in a multitude of food related industrial fermentation processes including the malolactic fermentation (MLF) of wine. This work is the first report on a recombinant L. plantarum strain successfully conducting MLF. The malolactic enzyme (MLE) from Oenococcus oeni was cloned into the lactobacillal expression vector pSIP409 which is based on the sakacin P operon of Lactobacillus sakei and expressed in the host strain L. plantarum WCFS1. Both recombinant and wild-type L. plantarum strains were tested for MLF using a buffered malic acid solution in absence of glucose. Under the conditions with L-malic acid as the only energy source and in presence of Mn2+ and NAD+, the recombinant L. plantarum and the wild-type strain converted 85% (2.5 g/l) and 51% (1.5 g/l), respectively, of L-malic acid in 3.5 days. Furthermore, the recombinant L. plantarum cells converted in a modified wine 15% (0.4 g/l) of initial L-malic acid concentration in 2 days. In conclusion, recombinant L. plantarum cells expressing MLE accelerate the malolactic fermentation.

Keywords:
L. plantarum; Oenococcus oeni; Malolactic fermentation; Malolactic enzyme