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2022731 
Journal Article 
Biochemical studies of beta-galactosidase from Kluyveromyces lactis 
Pal, A; Pal, V; Ramana, K; Bawa, AS 
2009 
Yes 
Journal of Food Science and Technology
ISSN: 0022-1155 
46 
3 
217-220 
English 
WOS:000267381800007 
β-Galactosidase was extracted from yeast, Kluyveromyces lactis isolated from curd using ammonium sulphate precipitation (0-55%) and gel permeation chromatography (Sephacryl-200). The enzyme was optimally active at pH 6.8 and temperature 40°C when assayed with o-nitrophenyl-β-D- galactopyranoside (ONPG) as substrate. The enzyme was sensitive to temperature >40°C. The divalent cations (Mn+2, Mg+2) increased the enzyme activity maximally followed by monovalent cations (Na+1, K+1, Li+1) while Ca+2 and EDTA inhibited the activity. Higher concentrations (>10 mM) of galactose inhibited the enzyme activity competitively. Activity of the enzyme could be enhanced by providing reducing environment to the assay mixture. These properties of β-galactosidase suggest its potential use for the production of lactose free milk for lactose intolerant population. 
beta-Galactosidase; Kluyveromyces lactis; Lactose intolerance; Thermostability; Reductant; Inhibition