title: Interaction of carbohydrates with alcohol dehydrogenase: Effect on enzyme activity.
abstract: Alcohol dehydrogenase was covalently conjugated with three different oxidized carbohydrates i.e., glucose, starch and pectin. All the carbohydrates inhibited the enzyme. The inhibition was studied with respect to the inhibition rate constant, involvement of thiol groups in the binding, and structural changes in the enzyme. The enzyme activity decreased to half of its original activity at the concentration of 2 mg/mL of pectin, 4 mg/mL of glucose and 10 mg/mL of starch within 10 min at pH 7. This study showed oxidized pectin to be a potent inhibitor of alcohol dehydrogenase followed by glucose and starch. Along with the aldehyde-amino group interaction, thiol groups were also involved in the binding between alcohol dehydrogenase and carbohydrates. The structural changes occurring on binding of alcohol dehydrogenase with oxidized carbohydrates was also confirmed by fluorescence spectrophotometry. Oxidized carbohydrates could thus be used as potential inhibitors of alcohol dehydrogenase.
authors: Department of Biotechnology and Chemical Technology, Aalto University, School of Chemical Technology, POB 16100, 00076 Aalto, Finland; Food Engineering and Technology Department, Institute of Chemical Technology, Matunga, Mumbai 400 019, India.
authors: Swati B
authors: SB
authors: Jadhav
authors: Department of Biotechnology and Chemical Technology, Aalto University, School of Chemical Technology, POB 16100, 00076 Aalto, Finland.
authors: Sandip B
authors: SB
authors: Bankar
authors: Department of Biotechnology and Chemical Technology, Aalto University, School of Chemical Technology, POB 16100, 00076 Aalto, Finland.
authors: Tom
authors: T
authors: Granström
authors: Department of Biotechnology and Chemical Technology, Aalto University, School of Chemical Technology, POB 16100, 00076 Aalto, Finland.
authors: Heikki
authors: H
authors: Ojamo
authors: Food Engineering and Technology Department, Institute of Chemical Technology, Matunga, Mumbai 400 019, India.
authors: Rekha S
authors: RS
authors: Singhal
authors: Department of Biotechnology and Chemical Technology, Aalto University, School of Chemical Technology, POB 16100, 00076 Aalto, Finland. Electronic address: shrikantraje1@gmail.com.
authors: Shrikant A
authors: SA
authors: Survase
mesh_terms: D000426:Alcohol Dehydrogenase / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D005947:Glucose / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010084:Oxidation-Reduction; D010368:Pectins / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013213:Starch / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D013438:Sulfhydryl Compounds / Q000378:metabolism
chemical_list: D004791:Enzyme Inhibitors; D013438:Sulfhydryl Compounds; D010368:Pectins; D013213:Starch; D000426:Alcohol Dehydrogenase; D005947:Glucose
keywords: Alcohol dehydrogenase; Carbohydrates; Covalent binding; Inhibition; Thiol groups