Enantioselective recognition mechanism of secondary alcohol by surfactant-coated lipases in nonaqueous media

Kamiya, Noriho; Kasagi, Hideaki; Inoue, Masahito; Kusunoki, Kenichi; Goto, Masahiro

doi:10.1002/(sici)1097-0290(19991020)65:2<227::aid-bit14>3.0.co;2-u

Cited by 21 publications

(3 citation statements)

References 29 publications

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“…Moreover, the loss of some activity of the enzyme in its contact with DMSO suggested directions for improving the enzymatic acetylation on cellulose in organic media. For example, modification of the enzyme by surfactant or lipid coating may protect the enzyme from denaturation or inactivation from its direct contact with solvents such as DMSO (51 − 53). Proper adjustment of the water content or activity in organic media in terms of the partition of water between the enzyme and organic solvents may satisfy the varied requirement for water by the enzyme in its contact with solvents of different polarity (16, 28, 54, 55).…”

Section: Discussionmentioning

confidence: 99%

Lipase‐Catalyzed Cellulose Acetylation in Aqueous and Organic Media

Yang

Wang

2003

Biotechnology Progress

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Screening for lipases capable of catalyzing acetylation of cellulosic substrates was conducted in aqueous buffer solution using water-soluble carboxymethyl cellulose (CMC) as substrate. Lipase A12 from Aspergillus niger (A. niger) showed the most promising acetylation activity among 11 tested commercial microbial lipases and was further applied to catalyzing acetylation of solid cellulose in aqueous solution. This reaction was shown to be feasible with an acetylation extent of 0.16 wt % achieved compared with no detectable acetylation in the absence of enzyme. Pretreatments on cellulose substrate by ultrasonic irradiation and surfactant solution only slightly improved the acetylation extent by 44 and 27%, respectively. Alternatively, this lipase-catalyzed acetylation was remarkably improved with solubilized cellulose as substrate in the dimethyl sulfoxide/paraformaldehyde solvent system, with an acetylation extent (7.87 wt %) nearly 50 times higher than that achieved in aqueous solution. This improvement was attributed to (1) the absence of bulk water and the increase in substrate solubility by the transition of reaction media from aqueous solution to organic solvents and (2) the ability of lipase A12 to remain catalytically active in highly polar DMSO. This discovery that the A. niger lipase was capable of surviving its contact with polar solvents was further confirmed by its considerably preserved catalytic activity on CMC acetylation in aqueous media after enzyme pretreatments with organic solvents of various polarities and in mixture media with the aqueous phase partially replaced by organic solvents.

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Section: Discussionmentioning

confidence: 99%

Lipase‐Catalyzed Cellulose Acetylation in Aqueous and Organic Media

Yang

Wang

2003

Biotechnology Progress

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“…This amphiphilic cover consists of polar amino acids on the outside and nonpolar amino acids on the inner side, in contact with the active site [39]. It has been reported that lipases with the lid covering the active site are in a closed conformation and, in the presence of an emulsion (upon contact with the interface formed by the lipid lipases), undergo a conformational change in the lid region exposing their active site for the hydrolysis of triacylglycerol molecules [40]. The active site is only exposed when the cover opens, i.e.…”

Section: Structural Characteristicsmentioning

confidence: 99%

REVIEW: Novel sources and functions of microbial lipases and their role in the infection mechanisms

Pascoal

Estevinho

Martins

et al. 2018

Physiological and Molecular Plant Pathology

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Lipases belong to the family of serine hydrolases, which in turn include various esterase enzymes (E.C.3.1.1.1). They are involved in the cleavage of triacylglycerols to free fatty acids and glycerol in many important biological processes, as for instance routine metabolism of dietary triglycerides to cell signalling and inflammation. Lipases constitute a ubiquitous group of enzymes able to catalyse a number of different reactions, many of them of industrial interest. Particularly, microbial lipases exhibit a wide range of industrial applications, namely in pharmaceutical, food and detergents industry. The aim of this review is to summarize the recent achievements illustrating the importance and the versatility of microbial lipases, including their involvement in infection mechanisms.

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“…Under the optimum additive condition (30 mg/ml CTAB), the activity of PPL was about 1.8-fold than that in pure buffer medium. It was well known that lipases displayed a very complex mechanism of action, including the process of ''interfacial activation'' [32][33][34]. Lipases may exist in two different forms.…”

Section: Effect Of Surfactantmentioning

confidence: 99%

A two-step enzymatic resolution of glycidyl butyrate

Wang

et al. 2007

Process Biochemistry

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Enantioselective recognition mechanism of secondary alcohol by surfactant-coated lipases in nonaqueous media

Cited by 21 publications

References 29 publications

Lipase‐Catalyzed Cellulose Acetylation in Aqueous and Organic Media

Lipase‐Catalyzed Cellulose Acetylation in Aqueous and Organic Media

REVIEW: Novel sources and functions of microbial lipases and their role in the infection mechanisms

A two-step enzymatic resolution of glycidyl butyrate

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