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Biotechnological relevance of the lipase A from Candida antarctica

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TLDR
This review intends to present some of the latest studies on the lipase A from Candida antarctica (CALA), which is among the most stable ones and has some capability to attack the sn-2 position of triglycerides.
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This article is published in Catalysis Today.The article was published on 2021-02-15. It has received 67 citations till now. The article focuses on the topics: Lipase & Immobilized enzyme.

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Tosylated cloisite as a new heterofunctional carrier for covalent immobilization of lipase and its utilization for production of biodiesel from waste frying oil

TL;DR: In this article, cloisite 30B (CL) was converted to tosylated cloisites (TCL) as new heterofunctional support and used to produce biodiesel from waste frying oil.
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An overview on the conversion of glycerol to value-added industrial products via chemical and biochemical routes.

TL;DR: In this article, the authors present a critical evaluation of the innovative technologies based on the use of residual glycerol in different industries, including the pharmaceutical, textile, food, cosmetic, and energy sectors.
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Biodiesel production from microalgae using lipase-based catalysts: Current challenges and prospects

TL;DR: In this paper , the main aspects associated with biodiesel production from microalgae, highlighting the fundamentals of the technique, the immobilization processes followed, the use of solvents to optimize reaction media, bioreactor systems, as well as the performance optimization of micro-algae biodiesel-based engines, while considering important economic and environmental aspects.
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Taguchi design-assisted co-immobilization of lipase A and B from Candida antarctica onto chitosan: Characterization, kinetic resolution application, and docking studies

TL;DR: In this paper , the simultaneous co-immobilization by covalent binding of lipase A from Candida antarctica (CALA) and lipase B from CALB in glutaraldehyde activated chitosan (CHI) was optimized using the Taguchi method.
References
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Improvement of enzyme activity, stability and selectivity via immobilization techniques

TL;DR: In all cases, enzyme engineering via immobilization techniques is perfectly compatible with other chemical or biological approaches to improve enzyme functions and the final success depend on the availability of a wide battery of immobilization protocols.
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Green Chemistry: Principles and Practice

TL;DR: The concepts of design and the scientific philosophy of Green Chemistry are covered with a set of illustrative examples and the challenge of using the Principles as a cohesive design system is discussed.
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Enzyme immobilisation in biocatalysis : Why, what and how

TL;DR: An overview of the why, what and how of enzyme immobilisation for use in biocatalysis is presented and emphasis is placed on relatively recent developments, such as the use of novel supports such as mesoporous silicas, hydrogels, and smart polymers, and cross-linked enzyme aggregates (CLEAs).
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Engineering the third wave of biocatalysis

TL;DR: Applications of protein-engineered biocatalysts ranging from commodity chemicals to advanced pharmaceutical intermediates that use enzyme catalysis as a key step are discussed.
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The α/β hydrolase fold

TL;DR: The alpha/beta hydrolase fold as mentioned in this paper is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function, including the serine protease catalytic triad.
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