Yanjiao Feng, Lifen Huang, Yue Zeng, Yiyuan Zhang, Wei Liu, Gang He
{"title":"Cloning, Expression and Enzymatic Characterization of Pectin Methyl Esterase from Populus trichocarpa and Its Application","authors":"Yanjiao Feng, Lifen Huang, Yue Zeng, Yiyuan Zhang, Wei Liu, Gang He","doi":"10.3390/pr12071511","DOIUrl":null,"url":null,"abstract":"The pectin methyl esterase gene from Populus trichocarpa (PtPME) was successfully cloned through PCR amplification and subsequently inserted into the expressing vector pMAL-c5e for successful expression in Escherichia coli BL21 (DE3). Initially, we determined the primary enzymatic properties of PtPME, a pectin methyl esterase derived from Populus trichocarpa. Notably, this enzyme exhibits a higher affinity towards citrus pectin, with an esterification degree exceeding 60%. Furthermore, this enzyme’s optimal reaction temperature and pH were found to be 30 °C and 8, respectively. Importantly, its exceptional stability under neutral conditions highlights its potential application in the industrial production of low-ester pectin.","PeriodicalId":506892,"journal":{"name":"Processes","volume":" 4","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-07-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Processes","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3390/pr12071511","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
The pectin methyl esterase gene from Populus trichocarpa (PtPME) was successfully cloned through PCR amplification and subsequently inserted into the expressing vector pMAL-c5e for successful expression in Escherichia coli BL21 (DE3). Initially, we determined the primary enzymatic properties of PtPME, a pectin methyl esterase derived from Populus trichocarpa. Notably, this enzyme exhibits a higher affinity towards citrus pectin, with an esterification degree exceeding 60%. Furthermore, this enzyme’s optimal reaction temperature and pH were found to be 30 °C and 8, respectively. Importantly, its exceptional stability under neutral conditions highlights its potential application in the industrial production of low-ester pectin.