Novel preparation method for surfactant‐lipase complexes utilizing water in oil emulsions

Okazaki, Susumu; KAMIYA, NORIHO; Abe, Kojiro; Goto, Masahiro; Nakashio, Fumiyuki

doi:10.1002/(sici)1097-0290(19970720)55:2<455::aid-bit23>3.3.co;2-3

Cited by 7 publications

(9 citation statements)

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“…In particular, the homogeneous enzymatic reaction in a nonaqueous medium with an enzyme dissolved by means of various methods is more attractive than the heterogeneous reaction using an insoluble enzyme because of the higher catalytic activity. The external surface of the enzyme is converted into a hydrophobic property by chemical modification, such as coating with a surfactant [51,52], modification with an oil-soluble polymer (PEGylation) [53], and encapsulation by a supramolecular assembly (reversed micelle) [54].…”

Section: (Iii) Catalytic Oxidation By the Cytochrome C Extracted In Omentioning

confidence: 99%

Recognition of Lysine Residues on Protein Surfaces Using Calixarenes and its Application

Oshima¹,

Baba²,

Shimojo³

et al. 2007

CDDT

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A macrocyclic calix[6]arene carboxylic acid derivative is found to extract lysine-rich protein cytochrome c from aqueous media into organic media through the complexation between the calixarene molecules and lysine residues on the surface of the protein. This article summarizes both the mechanism of protein extraction by the calixarene as well as the potential applications of the extraction process. The extraction process can be used for the purification of proteins through selective extraction and back-extraction under optimized conditions. On the other hand, the extracted protein exhibits enzymatic activity in organic media. The formation of a supramolecular complex by recognizing the residues on a protein surface can be construed as a novel recognition and/or modification method for biomacromolecules.

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Section: (Iii) Catalytic Oxidation By the Cytochrome C Extracted In Omentioning

confidence: 99%

Recognition of Lysine Residues on Protein Surfaces Using Calixarenes and its Application

Oshima¹,

Baba²,

Shimojo³

et al. 2007

CDDT

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“…The surfactant−protease complex was formed by the novel preparation method utilizing the water‐in‐oil emulsion, while the surfactant‐coated protease was formed by a conventional preparation method which was first reported by Okahata and Ijiro (1988). The yield of the surfactant−protease complex is theoretically 100% (Okazaki et al, 1997), while those of surfactant‐coated proteases were 22−28%. A lyophilized protease was prepared by the following procedure: protease (10 g/L) was dissolved in 50 mL of phosphate buffer at optimum pH and lyophilized for 24 h. All enzyme preparations except for commercial samples (native proteases) were conducted with the same potassium phosphate buffer solution.…”

Section: Methodsmentioning

confidence: 99%

“…Recently, we have introduced the new and easy preparation method for surfactant−lipase complexes utilizing water‐in‐oil (W/O) emulsions. It was found that the complexes prepared by the novel method exhibited much higher activity compared with that of native powder lipase in anhydrous isooctane (Okazaki et al, 1997). This novel preparation method can be easily applied to many enzymes because this method does not need a special modifying technique for the enzyme.…”

Section: Introductionmentioning

confidence: 99%

Application of Novel Preparation Method for Surfactant-Protease Complexes Catalytically Active in Organic Media

1997

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We have applied the newly developed method of preparing surfactant-enzyme complexes to other different enzyme sources in order to study the efficacy of this technique in the catalyzed transesterification processes. Protease from varied material sources was modified with surfactant molecules utilizing water-in-oil (W/O) emulsions, and the complex so formed proved very effective in catalyzing vinyl butyrate transesterification with benzyl alcohol in organic media. By contrast, native commercial protease and a lyophilized protease from optimum buffer solution pH hardly catalyzed the above process. Although, conventionally prepared surfactant-coated protease had shown some catalytic activity, its performance was significantly lower than that of the surfactant-protease complex assembled in the novel preparation method. The typical transesterification rates catalytically induced by surfactantprotease complexes were in the range of 7-260-fold superior relative to other catalyzed reaction systems. The preparation and reaction conditions of the surfactant-protease P (Aspergillus melleus) have been optimized through studies of the effect of aqueous pH in the W/O emulsions, the nature of the organic solvents and surfactants, and the reaction temperature. The protease complex prepared from nonionic surfactant 2C 18 ∆ 9 -GE at optimized aqueous pH yielded the best results in isooctane at 45°C. This novel enzyme modification method is conceptually simple, and the resultant complexes are elucidable. It is hoped that this method will become useful, particularly in preparing enzymes that are nonaqueous media sensitive and soluble in organic solution.

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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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Novel preparation method for surfactant‐lipase complexes utilizing water in oil emulsions

Cited by 7 publications

References 0 publications

Recognition of Lysine Residues on Protein Surfaces Using Calixarenes and its Application

Recognition of Lysine Residues on Protein Surfaces Using Calixarenes and its Application

Application of Novel Preparation Method for Surfactant-Protease Complexes Catalytically Active in Organic Media

A two-step enzymatic resolution of glycidyl butyrate

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