{"title":"黑曲霉固态发酵咖啡渣渣中a - l -鼠李糖苷酶活性的研究","authors":"Kahar Muzakhar, Rudju Winarsa","doi":"10.15575/BIODJATI.V4I1.4411","DOIUrl":null,"url":null,"abstract":" An α-L-Rhamnosidase released by Aspergillus niger during solid-state fermentation (SSF) using coffee pulp (CP) wastes media has been investigated. The activity of α-L-Rhamnosidase based on reducing sugar production against 2% CP alkali extract substrate in 50 mM acetate buffer pH 5. The maximum activity of α-L-Rham-nosidase was obtained in sixth-day SSF with reducing sugar pro-duction of 13 μg/mL. The enzyme is actively hydrolyzed 0.1% p-ni-trophenyl-α-L-rhamnopyranoside (PNP-Rha) to 95% from initial concentration. Purification using DEAE-Toyopearl 650M increased hydrolysis activity ten times against the substrate, reaching 134 μg/mL of reducing sugar. Optimum enzyme activity at pH 4.5 and 50°C, while stable at pH and temperature in a pH range of 3.5-7 and below 50°C. ","PeriodicalId":17683,"journal":{"name":"Jurnal Biodjati","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2019-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":"{\"title\":\"Activity of an A-L-Rhamnosidase Produced by Aspergillus niger During Solid State Fermentation of Coffee Pulp Wastes\",\"authors\":\"Kahar Muzakhar, Rudju Winarsa\",\"doi\":\"10.15575/BIODJATI.V4I1.4411\",\"DOIUrl\":null,\"url\":null,\"abstract\":\" An α-L-Rhamnosidase released by Aspergillus niger during solid-state fermentation (SSF) using coffee pulp (CP) wastes media has been investigated. The activity of α-L-Rhamnosidase based on reducing sugar production against 2% CP alkali extract substrate in 50 mM acetate buffer pH 5. The maximum activity of α-L-Rham-nosidase was obtained in sixth-day SSF with reducing sugar pro-duction of 13 μg/mL. The enzyme is actively hydrolyzed 0.1% p-ni-trophenyl-α-L-rhamnopyranoside (PNP-Rha) to 95% from initial concentration. Purification using DEAE-Toyopearl 650M increased hydrolysis activity ten times against the substrate, reaching 134 μg/mL of reducing sugar. Optimum enzyme activity at pH 4.5 and 50°C, while stable at pH and temperature in a pH range of 3.5-7 and below 50°C. \",\"PeriodicalId\":17683,\"journal\":{\"name\":\"Jurnal Biodjati\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-05-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Jurnal Biodjati\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15575/BIODJATI.V4I1.4411\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Jurnal Biodjati","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15575/BIODJATI.V4I1.4411","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
摘要
研究了黑曲霉(Aspergillus niger)利用咖啡渣(CP)固体发酵(SSF)过程中释放的α- l -鼠李糖苷酶。α- l -鼠李糖苷酶对2% CP碱提物在50 mM醋酸缓冲液pH 5条件下的活性研究。α- l -鼠李糖苷酶活性在SSF第6天达到最高值,还原糖产量为13 μg/mL。该酶能将0.1%的p-ni-trophenyl-α-L-rhamnopyranoside (PNP-Rha)活性水解至95%。采用DEAE-Toyopearl 650M进行纯化,对底物的水解活性提高了10倍,达到134 μg/mL的还原糖。在pH为4.5和50℃时酶活性最佳,在pH为3.5-7和低于50℃时酶活性稳定。
Activity of an A-L-Rhamnosidase Produced by Aspergillus niger During Solid State Fermentation of Coffee Pulp Wastes
An α-L-Rhamnosidase released by Aspergillus niger during solid-state fermentation (SSF) using coffee pulp (CP) wastes media has been investigated. The activity of α-L-Rhamnosidase based on reducing sugar production against 2% CP alkali extract substrate in 50 mM acetate buffer pH 5. The maximum activity of α-L-Rham-nosidase was obtained in sixth-day SSF with reducing sugar pro-duction of 13 μg/mL. The enzyme is actively hydrolyzed 0.1% p-ni-trophenyl-α-L-rhamnopyranoside (PNP-Rha) to 95% from initial concentration. Purification using DEAE-Toyopearl 650M increased hydrolysis activity ten times against the substrate, reaching 134 μg/mL of reducing sugar. Optimum enzyme activity at pH 4.5 and 50°C, while stable at pH and temperature in a pH range of 3.5-7 and below 50°C.