Variation of Inhibition Modes by n-Alcohols in Arbutin (Hydroquinone-O-β-D-glucopyranoside) Hydrolysis by β-Glucosidase

スポンサーリンク

概要

• 論文の詳細を見る

• When n-alcohols were added to the β-glucosidase-catalyzed hydrolysis of arbutin, the rate was decreased almost linearly with their elevating concentrations. The inhibition was shown in two modes, competitive for higher n-alcohols and noncompetitive for lower n-alcohols than n-butanol. The inhibition constants (K_i) obtained, moreover, clearly demonstrated classifying the modes in two groups according to physicochemical parameters, logP, Hildebrand solubility parameter (δ), and dielectric constant (ε), of n-alcohols. n-Butanol being between two modes of inhibition showed a mixed-type inhibition. The data suggested that the inhibition of n-alcohols for β-glucosidase may be related with their chain length. An imaging model in this case of inhibition is presented.

• 社団法人日本農芸化学会の論文
• 1995-07-23

著者

• Tadasa Koji

  Department Of Bioscience And Biotechnology Shinshu University

• Tadasa Koji

  Department Of Bioscience And Biotechnology Faculty Of Agriculture Shinshu University

• Sakama Noriko

  Department of Bioscience and Biotechnology, Shinshu University

• Sakama Noriko

  Department Of Bioscience And Biotechnology Shinshu University

関連論文

• Effects of Normal and Their Branched Alcohols with Structurally Minimal Variation on Kinetic Parameters in Thermolysin-catalyzed Peptide Hydrolysis and Synthesis of N-(Benzyloxycarbonyl)-L-phenylalanyl-L-phenylalanine and Its Methyl Ester
• Modification Effects of Organic Solvents on Microenvironment of the Enzyme in Thermolysin-catalyzed Peptide Synthesis of N-(Benzyloxycarbonyl)-L-phenylalanyl-L-phenylalanine Methyl Ester
• A Trial of Peptide Synthesis Using Angiotensin-I Converting Enzyme (ACE)
• Variation of Inhibition Modes by n-Alcohols in Arbutin (Hydroquinone-O-β-D-glucopyranoside) Hydrolysis by β-Glucosidase
• Synthesis of Amino Acid Derivatives of Kojic Acid and Their Tyrosinase Inhibitory Activity

スポンサーリンク