Yeast lipases: enzyme purification, biochemical properties and gene cloning

ABSTRACT

Lipases are placed only after proteases and carbohydrases in world enzyme market and share about 5% of enzyme market. They occur in plants, animals and microorganisms and are accordingly classified as plant, animal and microbial lipases. Wherever they exist, they function to catalyze hydrolysis of triglycerides to glycerol and fatty acid. Like carbohydrases and proteases, lipases of microbial origin enjoy greater industrial importance as they are more stable (compared to plant and animal lipases) and can be obtained in bulk at low cost. Majority of yeast lipases are extracelluar, monomericglycoproteins with molecular weight ranging between ~33 to ~65 kD. More than 50% reported lipases producing yeast, produce it in the forms of various isozymes. These lipase isozymes are in turn produced by various lipase encoding genes. Among many lipase producing yeasts Candida rugosa is most frequently used yeast as the source of lipase commercially. This review is aimed at compiling the information on properties of various yeast lipases and genes encoding them.