A chimeric membrane enzyme and an engineered whole-cell biocatalyst for efficient 1-alkene production

Iqbal, T and Murugan, S and Das, D (2024) A chimeric membrane enzyme and an engineered whole-cell biocatalyst for efficient 1-alkene production. In: Science Advances, 10 (26).

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Abstract

Bioproduction of 1-alkenes from naturally abundant free fatty acids offers a promising avenue toward the next generation of hydrocarbon-based biofuels and green commodity chemicals. UndB is the only known membrane-bound 1-alkene�producing enzyme, with great potential for 1-alkene bioproduction, but the enzyme exhibits limited turnovers, thus restricting its widespread usage. Here, we explore the molecular basis of the limitation of UndB activity and substantially improve its catalytic power. We establish that the enzyme undergoes peroxide-mediated rapid inactivation during catalysis. To counteract this inactivation, we engineered a chimeric membrane enzyme by conjugating UndB with catalase that protected UndB against peroxide and enhanced its number of turnovers tremendously. Notably, our chimeric enzyme is the only example of a membrane enzyme successfully engineered with catalase. We subsequently constructed a whole-cell biocatalytic system and achieved remarkable efficiencies (up to 95) in the biotransformation of a wide range of fatty acids (both aliphatic and aromatic) into corresponding 1-alkenes with numerous biotechnological applications. copyright © 2024 the Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. no claim to original U.S. Government Works. distributed under a creative commons Attribution noncommercial license 4.0 (cc BY-nc).

Item Type:	Journal Article
Publication:	Science Advances
Publisher:	American Association for the Advancement of Science
Additional Information:	The copyright for this article belongs to authors.
Keywords:	Fatty acids; Oxidation; Peroxides, 1-alkenes; Alkene production; Bio-production; Catalytic power; Commodity chemicals; Free fatty acid; Membrane enzymes; Membrane-bound; Molecular basis; Whole cell biocatalysts, Enzymes, alkene; catalase; fatty acid; fusion protein, biocatalysis; Escherichia coli; genetics; metabolism; procedures; protein engineering, Alkenes; Biocatalysis; Catalase; Escherichia coli; Fatty Acids; Protein Engineering; Recombinant Fusion Proteins
Department/Centre:	Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited:	18 Dec 2024 08:40
Last Modified:	18 Dec 2024 08:40
URI:	http://eprints.iisc.ac.in/id/eprint/85852

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