A review on thermo-alkalophilic bacterial lipase production and its applications

Document Type : Review articles

Authors

1 Botany and Microbiology Department, Faculty of Science, Al-Azhar University (Girls Branch), Cairo, Egypt

2 Lecturer of Environmental Biotechnology, Botany and Microbiology department, Science faculty, Al-Azhar University

3 Botany and Microbiology Department, Faculty of Science, Al-Azhar University (Boys Branch), Cairo, Egypt

Abstract

Bacterial lipases are dynamic enzymes that catalyze the hydrolysis and synthesis of ester bonds in triglycerides, resulting in the production of free fatty acids, glycerol, and mono- or diglycerides. The versatility of their mechanisms allows them to be used in diverse industrial and biotechnological applications. This review paper provides an overview regarding the function and structure of lipase enzymes. Thermo-alkalophilic bacterial lipases is characterized by their ability to maintain stability and catalytic efficiency under extreme environmental conditions, including high temperatures and alkaline pH. Also this paper explained thermo-alkalophilic bacterial lipase production. The most important thermo-alkalophilic bacterial lipase-producing genera, habitat, adaptation, physiological characteristics are presented. Bacterial lipases hold significant advantages over lipases derived from other sources, making them highly desirable for industrial applications. Isolation, screening, and identification of thermo-alkalophilic bacteria is discussed as well as optimization, and application of their lipase in many aspects of life. Engineering approaches, such as mutagenesis and immobilization, have been employed to further improve the thermal and pH stability of bacterial lipases, making them even more suitable for industrial applications in harsh environments

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