Recent advances in stability studies of microbial lipase

Abstract:

Lipases are widely used in industries, such as food, pharmaceuticals, biofuels, diagnostics, bioremediation, chemicals, cosmetics, detergents, feed, leather and biosensors and so on, microbial lipases are the most important source of commercial lipases. The harsh industrial production environments, e.g. high temperature, acidity, alkalinity and organic solvents, limit the further industrial application of lipases, to obtain stable lipases becomes a key link to break this limitation. This paper focuses on the main strategies to improve the stability of lipases are as follow: excavating extreme microbial lipase resources; using protein engineering strategies, such as directed evolution, rational design and semi-rational design to modify lipases; utilizing immobilization technologies of enzymes such as physical adsorption, encapsulation, covalent bonding and cross-linking to improve the stability of lipases; taking advantage of physical/chemical modification, surface display, and a combination of multiple improvement strategies to increase lipases stability. Combined with the author's previous research on enzyme engineering, it was found that the acquisition of new enzyme catalysts should be based on clear design ideas and combined with a variety of modification methods: combined modification methods based on directed evolution-rational design, directed evolution-semi-rational design, protein engineering-enzyme immobilization, protein engineering-physical/chemical modification and enzyme immobilization-physical/chemical modification, etc., which are more efficient than single modification method.