Lipase-Catalyzed Production of 6-O-cinnamoyl-sorbitol from D-sorbitol and Cinnamic Acid Esters

Kim, Jung Ho; Bhatia, Shashi Kant; Yoo, Dongwon; Seo, Hyung-Min; Yi, Da-Hye; Kim, Hyun Joong; Choi, Kwon‐Young; Lee, Yoo Kyung; Yang, Yung‐Hun

doi:10.1007/s12010-015-1570-x

Cited by 8 publications

(4 citation statements)

References 22 publications

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“…Lipases also have the capacity to produce fragrance and thus may be used for the production of cosmetics and perfumes ( Gupta et al, 2015 ; Kim et al, 2015 ; Ugo et al, 2017 ; Uppada et al, 2017 ; Tufiño et al, 2019 ). Lipase has also been used as a major ingredient in topical creams and in oral medications to aid weight loss through removal fat ( Sonne et al, 2015 ); lipase is also in wide use for the production of curls ( Shafqat et al, 2015 ).…”

Section: Heterologous Expression and Molecular Modification Of Microbial Lipasesmentioning

confidence: 99%

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Yao

Liu

et al. 2021

Front. Microbiol.

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As a powerful factory, microbial cells produce a variety of enzymes, such as lipase. Lipase has a wide range of actions and participates in multiple reactions, and they can catalyze the hydrolysis of triacylglycerol into its component free fatty acids and glycerol backbone. Lipase exists widely in nature, most prominently in plants, animals and microorganisms, among which microorganisms are the most important source of lipase. Microbial lipases have been adapted for numerous industrial applications due to their substrate specificity, heterogeneous patterns of expression and versatility (i.e., capacity to catalyze reactions at the extremes of pH and temperature as well as in the presence of metal ions and organic solvents). Now they have been introduced into applications involving the production and processing of food, pharmaceutics, paper making, detergents, biodiesel fuels, and so on. In this mini-review, we will focus on the most up-to-date research on microbial lipases and their commercial and industrial applications. We will also discuss and predict future applications of these important technologies.

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Section: Heterologous Expression and Molecular Modification Of Microbial Lipasesmentioning

confidence: 99%

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Yao

Liu

et al. 2021

Front. Microbiol.

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“…In the cosmetic industry, lipase derived from P. cepacia and P. fluorescens has been involved in producing the menthol esters that provide a peppermint flavor in shaving creams and mouthwashes [165]. The esterification catalyzed by lipase has been used in synthesizing esters derived from wax, ellagic acid, cinnamic acid, and ferulic acid, as these products can be involved in cosmetics and sunscreens, precursors of pharmaceuticals and flavor/fragrance compounds industries [143,166,167].…”

Section: Major Challenges Of Implementing Wild Type Lipase In Industrial Applicationmentioning

confidence: 99%

Main Structural Targets for Engineering Lipase Substrate Specificity

et al. 2020

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Microbial lipases represent one of the most important groups of biotechnological biocatalysts. However, the high-level production of lipases requires an understanding of the molecular mechanisms of gene expression, folding, and secretion processes. Stable, selective, and productive lipase is essential for modern chemical industries, as most lipases cannot work in different process conditions. However, the screening and isolation of a new lipase with desired and specific properties would be time consuming, and costly, so researchers typically modify an available lipase with a certain potential for minimizing cost. Improving enzyme properties is associated with altering the enzymatic structure by changing one or several amino acids in the protein sequence. This review detailed the main sources, classification, structural properties, and mutagenic approaches, such as rational design (site direct mutagenesis, iterative saturation mutagenesis) and direct evolution (error prone PCR, DNA shuffling), for achieving modification goals. Here, both techniques were reviewed, with different results for lipase engineering, with a particular focus on improving or changing lipase specificity. Changing the amino acid sequences of the binding pocket or lid region of the lipase led to remarkable enzyme substrate specificity and enantioselectivity improvement. Site-directed mutagenesis is one of the appropriate methods to alter the enzyme sequence, as compared to random mutagenesis, such as error-prone PCR. This contribution has summarized and evaluated several experimental studies on modifying the substrate specificity of lipases.

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“…Various surfactants based on MAGs and diacylglycerols are produced through lipase‐catalyzed transesterification and resolution of racemic intermediates. Further the esters of wax, cinnamic acid, ellagic acid, ferulic acid are synthesized through lipase‐catalyzed esterification which can be used as flavor/fragrance compounds, precursors of pharmaceuticals, and as additives in cosmetics and sunscreens . Also, lipases are primary components in topical creams or orally administered drugs that assist in weight loss by fat removal .…”

Section: Applications Of Lipase‐catalyzed Reactionsmentioning

confidence: 99%

“…Further the esters of wax, cinnamic acid, ellagic acid, ferulic acid are synthesized through lipase-catalyzed esterification which can be used as flavor/fragrance compounds, precursors of pharmaceuticals, and as additives in cosmetics and sunscreens. 182,251,253 Also, lipases are primary components in topical creams or orally administered drugs that assist in weight loss by fat removal. 254 An example of the evolving patented lipase-catalyzed processes involved in the beauty industry entails using P. fluorescens-and P. cepacia-derived lipases to produce the menthol esters that provide a peppermint flavor in mouth washes and shaving creams.…”

Section: Cosmetics and Perfumerymentioning

confidence: 99%

Recent advances on sources and industrial applications of lipases

Sarmah

Revathi

Sheelu

et al. 2017

Biotechnology Progress

302

148

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Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications of lipases is ever growing and there exists a need to have a latest review on the research findings of lipases. The present review aims at giving the latest and broadest overall picture of research and development on lipases by including the current studies and progressions not only in the diverse industrial application fields of lipases, but also with regard to its structure, classification and sources. Also, a special emphasis has been made on the aspects such as process optimization, modeling, and design that are very critical for further scale-up and industrial implementation. The detailed tabulations provided in each section, which are prepared by the exhaustive review of current literature covering the various aspects of lipase including its production and applications along with example case studies, will serve as the comprehensive source of current advancements in lipase research. This review will be very useful for the researchers from both industry as well as academia in promoting lipolysis as the most promising approaches to intensified, greener and sustainable processes. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:5-28, 2018.

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Lipase-Catalyzed Production of 6-O-cinnamoyl-sorbitol from D-sorbitol and Cinnamic Acid Esters

Cited by 8 publications

References 22 publications

A Valuable Product of Microbial Cell Factories: Microbial Lipase

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Main Structural Targets for Engineering Lipase Substrate Specificity

Recent advances on sources and industrial applications of lipases

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