Selection of a versatile Lactobacillus plantarum for wine production and identification and preliminary characterisation of a novel histamine‐degrading enzyme. (10th February 2020)

• Record Type: Journal Article
• Authors: Sun, Shuyang; Jiang, Dongqi; Fan, Minting; Li, Huamin; Jin, Chengwu; Liu, Wenli
• Is Part Of: International journal of food science & technology. Volume 55:Number 6(2020)
• Page Start: 2608
• Page End: 2618
• Publication Date: 2020-02-10
• Subjects: Biogenic amine -- histamine‐degrading enzyme -- Lactobacillus plantarum -- wine; Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.14514
• Languages: English
• ISSNs: 0950-5423

Abstract

Summary: In this study, a desirable and versatile Lactobacillus plantarum strain possessing great ability of L‐malic acid consumption, biogenic amine degradation and resistance to wine harsh environment was obtained through successive screenings. Malolactic fermentation (MLF) in contaminated grape wine and cherry wine (supplemented with histamine, tyramine and cadaverine) conducted by this strain was finished within 24 and 18 days, respectively, and the concentration of histamine, tyramine and cadaverine was decreased by over 57% following MLF. The enzyme from L. plantarum responsible for the amine degradation was purified to homogeneity by four steps including cell disruption, ammonium sulphate fractionation, an anion chromatography and a gel filtration chromatography. Such enzyme was identified as glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) after N‐terminal sequence analysis and protein Blast, a tetramer enzyme with a subunit molecular weight of 36 kDa. The optimum values of pH and temperature of this enzyme were at pH 7.5 and 40 °C, and stable between pH 5.5–8.5 and 30–50 °C. Abstract : A versatile Lactobacillus plantarum possessing great ability of L‐malic acid consumption, biogenic amine degradation and resistance to wine harsh environment was obtained in this study. Moreover, the enzyme from L. plantarum responsible for the amine degradation was purified to homogeneity and identified as glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH).