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ISOLATION AND PURIFICATION OF LACTASE FROM LACTOBACILLUS ACIDOPHILUS

Linh Thi Van Nguyen 1, *
Dung Thi Thuy Nguyen 2
Lam Bich Tran 2
  1. Nguyen Tat Thanh University
  2. University of Technology, VNU-HCM
Correspondence to: Linh Thi Van Nguyen, Nguyen Tat Thanh University. Email: pvphuc@hcmuns.edu.vn.
Volume & Issue: Vol. 15 No. 3 (2012) | Page No.: 65-72 | DOI: 10.32508/stdj.v15i3.1818
Published: 2012-09-30

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Copyright The Author(s) 2023. This article is published with open access by Vietnam National University, Ho Chi Minh city, Vietnam. This article is distributed under the terms of the Creative Commons Attribution License (CC-BY 4.0) which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. 

Abstract

The enzyme β-galactosidase (β-D-galactoside galactohydrolase, EC 3.2.1.23) commonly known as lactase, has important applications in the dairy industry. From culture of strain Lactobacillus acidophilus having high and stable β-galactosidase activity, the study of crude enzyme isolation were carried out by ultrasonical extraction and precipitation by neutral salts and organic solvents. Best precipitant was isopropanol with enzyme recovery 89,93%, and enzyme purity increased 4,5 folds. Further β-galactosidase purification was carried out using gel permeation chromatography on Ultrahydrogel 250 to increase purity in 14,3 folds. The molecular weight of β-galactosidase was 40 kDa. The purified enzyme had optimum activity at 40oC, pH 7 – 7,5 and kinetic parameters of Vmax and Km were 2,3 μmol/min and 0,73 mM.

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