{"title":"Study of Reduction Properties of Enzyme Alcohol Dehydrogenase from Saccharomyces cerevisiae Meyen ex. Hansen on Some Selected Compounds","authors":"Saif Khan","doi":"10.21276/ijlssr.2017.3.4.19","DOIUrl":null,"url":null,"abstract":"Saccharomyces cerevisiae (Family: Saccharomycetaceae) is a Basidiomycetes fungus that is used in day to day life for human welfare ranging from food to medicines depending upon the type of strains and uses. Alcohol Dehydrogenase (ADH) is an important enzyme produced by the Saccharomyces fungus that catalyzes the many oxidation-reduction reaction in nature. The present study focuses on the reduction properties of the enzyme ADH on compounds like Nicotinamide Adenine Dinucleotide (NAD), Dicholorophenol Indophenol (DCPIP), and Acetophenone using Spectrophotometric assays. The aim and hypothesis of the present study was to extract the enzyme in Crude and Immobilized form and to check the best reduction of compounds in either form. The activity of enzyme in Crude and Immobilized was mathematically calculated and was expressed in Units of enzyme activity per ml of the ADH enzyme on respective compounds used for study. Successfully the ADH was extracted in both forms, but reduction of compounds at best was observed in Immobilized Enzyme form. Key-wordsSaccharomyces cerevisiae, Alcohol Dehydrogenase, Nicotinamide Adenine Dinucleotide, Dicholorophenol Indophenol, Acetophenone INTRODUCTION Alcohol Dehydrogenase (ADH), part of the oxidoreductase family, catalyzes the oxidation of alcohols, using NAD or NADP as an electron acceptor. It is constitutive enzyme that reduces the acetaldehyde to ethanol during the fermentation of glucose. The reaction is reversible and substrates can be variety of primary or secondary alcohols and hemiacetals. Alcohol Dehydrogenase is present in most organisms, with that of yeast being the most active form of the enzyme . The alcohol dehydrogenases comprise a group of several isozymes that catalyze the oxidation of primary and secondary alcohols to aldehydes and ketones respectively and also can catalyze the reverse reaction . Generally Baker’s Yeast (Sacchromyces cerevisiae) is a good source of enzyme . Access this article online Quick Response Code Website:","PeriodicalId":22509,"journal":{"name":"The International Journal of Life-Sciences Scientific Research","volume":"14 1","pages":"1218-1222"},"PeriodicalIF":0.0000,"publicationDate":"2017-07-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The International Journal of Life-Sciences Scientific Research","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.21276/ijlssr.2017.3.4.19","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Saccharomyces cerevisiae (Family: Saccharomycetaceae) is a Basidiomycetes fungus that is used in day to day life for human welfare ranging from food to medicines depending upon the type of strains and uses. Alcohol Dehydrogenase (ADH) is an important enzyme produced by the Saccharomyces fungus that catalyzes the many oxidation-reduction reaction in nature. The present study focuses on the reduction properties of the enzyme ADH on compounds like Nicotinamide Adenine Dinucleotide (NAD), Dicholorophenol Indophenol (DCPIP), and Acetophenone using Spectrophotometric assays. The aim and hypothesis of the present study was to extract the enzyme in Crude and Immobilized form and to check the best reduction of compounds in either form. The activity of enzyme in Crude and Immobilized was mathematically calculated and was expressed in Units of enzyme activity per ml of the ADH enzyme on respective compounds used for study. Successfully the ADH was extracted in both forms, but reduction of compounds at best was observed in Immobilized Enzyme form. Key-wordsSaccharomyces cerevisiae, Alcohol Dehydrogenase, Nicotinamide Adenine Dinucleotide, Dicholorophenol Indophenol, Acetophenone INTRODUCTION Alcohol Dehydrogenase (ADH), part of the oxidoreductase family, catalyzes the oxidation of alcohols, using NAD or NADP as an electron acceptor. It is constitutive enzyme that reduces the acetaldehyde to ethanol during the fermentation of glucose. The reaction is reversible and substrates can be variety of primary or secondary alcohols and hemiacetals. Alcohol Dehydrogenase is present in most organisms, with that of yeast being the most active form of the enzyme . The alcohol dehydrogenases comprise a group of several isozymes that catalyze the oxidation of primary and secondary alcohols to aldehydes and ketones respectively and also can catalyze the reverse reaction . Generally Baker’s Yeast (Sacchromyces cerevisiae) is a good source of enzyme . Access this article online Quick Response Code Website: