Tailoring lipases as versatile food biocatalysts to enhance their comprehensive performance: A state-of-the-art review.

Abstract

Lipase is a valuable biocatalyst in food processing due to its ability to catalyze reactions like transesterification. However, its industrial application is hindered by its instability in non-natural environments such as organic solvents, extreme pH, and its frequent inefficiency with non-natural substrates. To overcome these limitations, lipase modification is employed to enhance its properties for practical use. Current modification strategies are primarily divided into two categories: protein engineering (rational design, directed evolution, semi-rational design) and in vitro methods (chemical modification, enzyme immobilization). This paper reviews recent advances in these areas, discussing the advantages and disadvantages of each approach. As a single method often fails to improve all desired properties, the future trend points toward the strategic combination of protein engineering and in vitro modification. This integrated approach allows for targeted structural changes to meet specific industrial demands, facilitating the development of advanced, versatile lipase food biocatalysts.