Atomic insights into the mechanism of trace water influence on lipase catalysis in organic media

Wang, Zhaoxin; Wen, Jinlan; Zhang, Jihang; Deng, Jiawei; Zhuang, Wei; Liu, Jinle; Wang, Zhi; Rao, Yuan; Zhu, Yudan; Ying, Hanjie

doi:10.1016/j.cej.2023.142610

Cited by 9 publications

(3 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Additionally, altering the enzyme's surface properties through protein engineering may improve its stability, activity, or selectivity in the immobilized state. Besides, given the intrinsic complexity of lipase/phospholipase catalytic systems, which differ from homogeneous enzyme catalytic systems, there is a need for engineering the reaction medium (Cao et al 2022 ; Wang et al 2023 ). The integration of multiple technologies, including protein engineering, immobilization techniques, and reaction medium engineering, represents a method to extend the industrial application of enzyme-mediated lipid modification.…”

Section: Discussionmentioning

confidence: 99%

Enzyme engineering for functional lipids synthesis: recent advance and perspective

Guan,

Hou,

Yang

et al. 2024

Bioresour. Bioprocess.

View full text Add to dashboard Cite

Functional lipids, primarily derived through the modification of natural lipids by various processes, are widely acknowledged for their potential to impart health benefits. In contrast to chemical methods for lipid modification, enzymatic catalysis offers distinct advantages, including high selectivity, mild operating conditions, and reduced byproduct formation. Nevertheless, enzymes face challenges in industrial applications, such as low activity, stability, and undesired selectivity. To address these challenges, protein engineering techniques have been implemented to enhance enzyme performance in functional lipid synthesis. This article aims to review recent advances in protein engineering, encompassing approaches from directed evolution to rational design, with the goal of improving the properties of lipid-modifying enzymes. Furthermore, the article explores the future prospects and challenges associated with enzyme-catalyzed functional lipid synthesis.

show abstract

Section: Discussionmentioning

confidence: 99%

Enzyme engineering for functional lipids synthesis: recent advance and perspective

Guan,

Hou,

Yang

et al. 2024

Bioresour. Bioprocess.

View full text Add to dashboard Cite

show abstract

“…The presence of water in organic media can significantly change lipase activity. [15] The aminolysis activity of Ndbn was thus recorded as a function of increasing water content. While the specific activity increases linearly up to a water content of 5 %, the conversion rate peaks at ~2 % water (Figure S3); a similar trend for the rate of aminolysis has also been observed for the lipase SpL.…”

Section: Effect Of the Water Content On Ndbn-catalyzed Aminolysismentioning

confidence: 99%

“…However, as its content increases, a layer of water may accumulate on the enzyme surface, making it more difficult for the substrate to reach the catalytic site, thus slowing down reaction rates. [15] In contrast for the majority of known lipases (except SpL), water is largely detrimental to aminolysis reactions, with even small quantities of water in the reaction system resulting in the undesired hydrolysis of the acyl donor (including CALB and Pseudomonas stutzeri lipase (PSL)). [16] In order to achieve strict anhydrous conditions, all reactants and solvents need to be dried over activated molecular sieves prior to use and the reaction itself also needs to be performed in the presence of molecular sieves to prevent significant ester hydrolysis.…”

Section: Effect Of the Water Content On Ndbn-catalyzed Aminolysismentioning

confidence: 99%

Discovery and Mechanistic Understanding of a Lipase from Rhizorhabdus dicambivorans for Efficient Ester Aminolysis in Aromatic Amines

Wang,

Huang,

et al. 2024

ChemSusChem

View full text Add to dashboard Cite

The formation of amide bonds via aminolysis of esters by lipases generates a diverse range of amide frameworks in biosynthetic chemistry. Few lipases have satisfactory activity towards bulky aromatic amines despite numerous attempts to improve the efficiency of this transformation. Here, we report the discovery of a new intracellular lipase (Ndbn) with a broad substrate scope. Ndbn turns over a range of esters and aromatic amines in the presence of water (2%; v/v), producing a high yield of multiple valuable amides. Remarkably, a higher conversion rate was observed for the synthesis of amides from substrates with aromatic amine rather than aliphatic amines. Molecular dynamics (MD) and quantum mechanical/molecular mechanical (QM/MM) studies showcase the mechanism for the preference for aromatic amines, including a more suitable orientation, shorter catalytic distances in the active site pocket and a lower reaction barrier for aromatic than for aliphatic amines. This unique lipase is thus a promising biocatalyst for the efficient synthesis of aromatic amides.

show abstract

In-situ stabilized lipase in calcium carbonate microparticles for activation in solvent-free transesterification for biodiesel production

Sik Choi,

Won Jeon,

Taek Hwang

2024

Bioresource Technology

View full text Add to dashboard Cite

Atomic insights into the mechanism of trace water influence on lipase catalysis in organic media

Cited by 9 publications

References 50 publications

Enzyme engineering for functional lipids synthesis: recent advance and perspective

Enzyme engineering for functional lipids synthesis: recent advance and perspective

Discovery and Mechanistic Understanding of a Lipase from Rhizorhabdus dicambivorans for Efficient Ester Aminolysis in Aromatic Amines

In-situ stabilized lipase in calcium carbonate microparticles for activation in solvent-free transesterification for biodiesel production

Contact Info

Product

Resources

About