{"title":"Identification and recombinant production of a flavonoid glucosyltransferase with broad substrate specificity from Vaccinium corymbosum","authors":"","doi":"10.1007/s13562-024-00876-2","DOIUrl":null,"url":null,"abstract":"<h3>Abstract</h3> <p>Glucosyltransferases (GTs) are enzymes that use UDP-glucose to glucosylate wide variety of substrates, including the aglycones of anthocyanins. Anthocyanins are glycosylated polyphenolic plant pigments possessing potential health benefits to humans. The berries of <em>Vaccinium</em> species plants are rich in anthocyanins. Although the flavonoid content of bilberries is well characterized, the enzymes responsible for carrying out anthocyanin modifications are not thoroughly studied. In this study, a predicted sequence of an anthocyanin glucosyltransferase was identified from the genomic data of <em>Vaccinium corymbosum</em>. The codon-optimized gene sequence of the protein was integrated into the genome of <em>P. pastoris.</em> Constitutive expression in yeast extract-peptone-dextrose based media gave satisfactory amount of recombinant protein. The enzyme activity assays revealed that the <em>V. corymbosum</em> GT transferred glucosyl moieties to up to three positions of diverse flavonoids, such as naringenin, kaempferol, eriodictyol and cyanidin 3-<em>O</em>-glucoside, being therefore a rather unique enzyme among GTs described so far. The enzyme preferred cyanidin 3-<em>O</em>-glucoside, peonidin 3-<em>O</em>-glucoside and eriodictyol as substrates. This enzyme could find application in biotechnological production of glucosylated flavonoids.</p>","PeriodicalId":16835,"journal":{"name":"Journal of Plant Biochemistry and Biotechnology","volume":"51 1","pages":""},"PeriodicalIF":1.6000,"publicationDate":"2024-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Plant Biochemistry and Biotechnology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s13562-024-00876-2","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Glucosyltransferases (GTs) are enzymes that use UDP-glucose to glucosylate wide variety of substrates, including the aglycones of anthocyanins. Anthocyanins are glycosylated polyphenolic plant pigments possessing potential health benefits to humans. The berries of Vaccinium species plants are rich in anthocyanins. Although the flavonoid content of bilberries is well characterized, the enzymes responsible for carrying out anthocyanin modifications are not thoroughly studied. In this study, a predicted sequence of an anthocyanin glucosyltransferase was identified from the genomic data of Vaccinium corymbosum. The codon-optimized gene sequence of the protein was integrated into the genome of P. pastoris. Constitutive expression in yeast extract-peptone-dextrose based media gave satisfactory amount of recombinant protein. The enzyme activity assays revealed that the V. corymbosum GT transferred glucosyl moieties to up to three positions of diverse flavonoids, such as naringenin, kaempferol, eriodictyol and cyanidin 3-O-glucoside, being therefore a rather unique enzyme among GTs described so far. The enzyme preferred cyanidin 3-O-glucoside, peonidin 3-O-glucoside and eriodictyol as substrates. This enzyme could find application in biotechnological production of glucosylated flavonoids.
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The Journal publishes review articles, research papers, short communications and commentaries in the areas of plant biochemistry, plant molecular biology, microbial and molecular genetics, DNA finger printing, micropropagation, and plant biotechnology including plant genetic engineering, new molecular tools and techniques, genomics & bioinformatics.
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