Enzymatic Functions of Fatty Acid-modified Chymotrypsin and Trypsin in Aqueous-organic Media

Kawasaki, Yuki; Takahashi, Yoshinori; Nakatani, Masami; Murakami, Mototake; Dosako, Shun’ichi; Okai, Hideo

doi:10.1271/bbb.58.512

Cited by 9 publications

(3 citation statements)

References 6 publications

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“…In this context, the in vivo post-translational modification of proteins by the covalent attachment of fatty acids and lipids is a widespread phenomenon in nature but as yet not completely understood (Schultz et aL, 1988). Several methods for the acylation of proteins in vitro have been described (PIou and Ballesteros, 1994;Kawasaki et aL, 1994).…”

Section: Introductionmentioning

confidence: 99%

Effect of chemical modification of isoenzymes A and B from C. rugosa on their activity and stability

1995

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Section: Introductionmentioning

confidence: 99%

Effect of chemical modification of isoenzymes A and B from C. rugosa on their activity and stability

1995

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“…11) Kawasaki et al proposed that the addition of hydrophobicity to an enzyme molecule by chemical modification contributes to reduction of the attractive forces between enzyme and solvent molecules. 13) Similarly, addition of hydrophobicity to the LiP is thought to decrease interaction between the enzyme and high viscosity solvent molecules. Therefore, the modified LiP having a high hydrophobicity can move easily in high-viscosity organic solvents, so that the modification of LiP may increase the affinity of enzyme to a substrate dissolved in high-viscosity organic solvents.…”

Section: Reaction Of Modified Lip In the Presence Of Organic Solventsmentioning

confidence: 99%

Reaction of Chemically Modified Lignin Peroxidase ofPhanerochaete chrysosporiumin Water-miscible Organic Solvents

Yoshida¹,

Watanabe²,

Honda³

et al. 1996

Bioscience, Biotechnology, and Biochemistry

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LiP of Phanerochaete chrysosporium was chemically modified with MPSS, and acetic and benzoic acid N-hydroxysuccinimide esters to increase the activity in organic solvents. IEF demonstrated the LiP was chemically modified with these modifers. The modification of LiP was also confirmed by GFC and anion-exchange chromatography analyses. In addition, the modified LiP retained its original activity in aqueous solution. Furthermore, these modified LiPs had higher 3,3' -dimethoxybenzidine oxidation activity than the native LiP in aqueous 70% water-miscible organic solutions including ethylene glycol and diethylene glycol. However, the activities of these modified enzymes were found to be negligibly low in water-immiscible organic solvents such as benzene and toluene. Furthermore, the effects of these introducing groups and the properties of organic solvents on the reaction of LiP in water-miscible organic solvents were investigated. The reaction of LiP modified with aliphatic acid was found to depend on the viscosity of the reaction system containing 70% water-miscible organic solvents. This suggests that the viscosity of the reaction system containing water-miscible organic solvents is important for the reaction of LiP modified with aliphatic acids.

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“…The aqueous -organic two-phase reaction system is also important for carrying out enzymatic conversion of hydrophobic compounds, and various hydrophobic useful substances, such as peptides (Cassells and Halling, 1988;D'cunha et al, 1994;Kasche and Galunsky, 1995;Kawasaki et al, 1994), epoxides (Kawakami, 1990), aldehydes (Mitarai and Kawakami, 1994), and other compounds (Fukui et al, 1992;Gargouri et al, 1996;Hernandez-Justiz et al, 1998;Shimizu et al, 1990) can be produced in aqueous -organic two-phase systems. In the aqueous -organic two-phase system employed in this study, both HLADH and NAD þ could be entrapped in an aqueous phase and used repeatedly with coenzyme regeneration.…”

Section: Introductionmentioning

confidence: 99%

Efficient Repeated Use of Alcohol Dehydrogenase with NAD + Regeneration in an Aqueous-organic Two-phase System

Suye

Kamiya

Kawamoto

et al. 2002

Biocatalysis and Biotransformation

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Bioconversion of cinnamyl alcohol to cinnamaldehyde was carried out in an aqueous -organic two-phase reaction system by the repeated use of horse liver alcohol dehydrogenase (HLADH) and NAD 1 with coenzyme regeneration. Both HLADH and the coenzyme were efficiently entrapped in the aqueous phase, while the substrate was supplied successively from the organic phase and the product was accumulated in the organic phase. Optimum conditions for cinnamaldehyde production in the aqueous -organic two-phase system were also examined, including substrate concentration, pH, and organic solvent type. Under suitable conditions, both HLADH and NAD 1 in the aqueous-organic twophase system could be reused, and NAD 1 cycling numbers of 3040 were obtained after repeated operation for 40 h.

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Enzymatic Functions of Fatty Acid-modified Chymotrypsin and Trypsin in Aqueous-organic Media

Cited by 9 publications

References 6 publications

Effect of chemical modification of isoenzymes A and B from C. rugosa on their activity and stability

Effect of chemical modification of isoenzymes A and B from C. rugosa on their activity and stability

Reaction of Chemically Modified Lignin Peroxidase ofPhanerochaete chrysosporiumin Water-miscible Organic Solvents

Efficient Repeated Use of Alcohol Dehydrogenase with NAD + Regeneration in an Aqueous-organic Two-phase System

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