Exploring Sequence Conservation and Functional Diversity in Beta- Galactosidase Enzymes: A Comparative Analysis of Mesophilic and Thermophilic Bacterial Species
Abstract
Abstract:
The structural comparative analysis of β-Galactosidase in Sulfolobus acidocaldarius and Escherichia coli highlights its thermostable nature and potential industrial applications under extreme conditions. This study investigates the 3D structure of β-Galactosidase in the thermophilic archaeon Sulfolobus acidocaldarius and compares it with the mesophilic bacterium Escherichia coli. The aim is to highlight the distinct structural features of the thermostable β-Galactosidase in S. acidocaldarius, emphasizing its potential for industrial applications under extreme conditions. The absence of a known 3D structure for this enzyme in S. acidocaldarius prompted modeling efforts. The findings reveal significant structural differences, particularly in thermal stability, making S. acidocaldarius β-Galactosidase promising for applications in the dairy industry, pharmaceuticals, and biotechnology. This study underscores the importance of understanding extremophile enzymes' adaptability to extreme environments and their potential for biotechnological advancements. The comparative analysis lays the foundation for future research aimed at harnessing thermostable β- Galactosidase enzymes' unique properties, offering innovative possibilities across various industries.
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