Abstract

Hydrolases, being most prominent enzymes used in industrial processes have left no stone unturned in fascinating the pharmaceutical industry. Lipases, being a part of acyl hydrolases are the ones that function similarly to esterases (except an interfacial action) wherein they generally catalyze the hydrolysis of ester bonds. Be it in terms of stereoselectivity or regioselectivity, lipases have manifested their promiscuous proficiency in rendering biocatalytic drug synthesis and intermediates thereof. Industrial utilization of lipases is prevalent since decades ago, but their distinctive catalytic competencies have rendered them suitable for maneuverability in various tides of biocatalytic industrial process development. Numbers of exquisite catalysts have been fabricated out of lipases using nanobiotechnology whereby enzyme reusability and robustness have been conferred to many of the organic synthesis procedures. This marks a considerable achievement of lipases in the second wave of biocatalysis. Furthermore, in the third wave an advent of genetic engineering has fostered an era of customized lipases for suitable needs. Be it stability or an enhanced efficacy, genetic engineering techniques have ushered an avenue for biocatalytic development of drugs and drug intermediates through greener processes using lipases. Even in the forthcoming concept of co-modular catalytic systems, lipases may be the frontiers because of their astonishing capability to act along with other enzymes. The concept may render feasibility in the development of cascade reactions in organic synthesis. An upcoming wave demands fulfilling the vision of tailored lipase whilst a far-flung exploration needs to be unveiled for various research impediments in rendering lipase as a custom fit biocatalyst in pharmaceutical industry.

Highlights

  • Biocatalysis–a denotation that pertains to the utilization of enzymes in chemical syntheses or conversions

  • With the utilization of commercial Fermase CALB 10,000 (Candida antarctica lipase B immobilized on glycidyl methacrylate terdivinylbenzene-ter-ethylene glycol dimethacrylate nanosupports), authors have achieved more than 95% conversion of butyl acetate to the corresponding propyl acetamide in lesser time and at higher temperature with the use of ultrasonic waves

  • We aimed to make the readers of this review aware about the evolution of lipases in the field of drug synthesis

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Summary

Introduction

Biocatalysis–a denotation that pertains to the utilization of enzymes in chemical syntheses or conversions. Lipases differ from esterases in a way they function by acting on interface in contrast to a homogenous solution This distinctive competence befits them for industrial and biotechnological applications ranging from detergent industry to chiral organic synthesis of fine chemicals and drugs. There has been a consistent rising demand for the production of lipases which matches with a pace in their utility in industrially relevant processes [5] Their capability of being acting in harsh conditions with thorough stability in organic solvents along with broad substrate specificity as well as high regioselectivity and/or stereoselectivity in catalytic processes potentiates them as one of the most widely used group of biocatalysts for biotechnological processes [6]. The structural properties facilitate the stereoselectivity, chemoselectivity and regioselectivity in lipase action [11,12]

Lipases: A Versatile Manifesto
Second Wave of Lipase Mediated Drug Synthesis
Third Wave of Lipase Mediated Drug Synthesis
Findings
Conclusions and Perspectives
Full Text
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