{"title":"酵母生产甜菜素用植物糖苷转移酶的筛选。","authors":"Christiane Glitz, Jane Dannow Dyekjær, Dovydas Vaitkus, Mahsa Babaei, Ditte Hededam Welner, Irina Borodina","doi":"10.1007/s12010-024-05100-4","DOIUrl":null,"url":null,"abstract":"<p><p>To cover the rising demand for natural food dyes, new sources and production methods are needed. Microbial fermentation of nature-identical colours, such as the red pigment betanin, has the potential to be a cost-efficient alternative to plant extraction. The last step of betanin production is catalysed by a UDP-glycosyltransferase (UGT). To find a high-performing UGT, we screened 27 UGTs from different plant species and tested their ability to produce betanin in vivo in Saccharomyces cerevisiae. We identified two new UGTs likely involved in the betanin synthesis in the plant they derive from: CqGT2 (UGT73A37) from Chenopodium quinoa and BgGT2 (UGT92X1) from Bougainvillea glabra. The betanin-producing UGTs were also tested in Yarrowia lipolytica, where CqGT2 was the best-performing glycosyltransferase for betanin production. While it has previously been shown that the UGTs can glycosylate either betanidin or cyclo-DOPA to ultimately form betanin, the molecular mechanism behind the preference for the acceptor molecule has not been elucidated. Therefore, we performed in silico structural analysis to characterise the betanin-producing UGTs further, particularly by looking into their binding mechanism. The docking model suggested that a smaller binding site found in some UGTs only allows glycosylation of cDOPA, while a wider binding site allows glycosylation of both cyclo-DOPA and betanidin.</p>","PeriodicalId":465,"journal":{"name":"Applied Biochemistry and Biotechnology","volume":" ","pages":""},"PeriodicalIF":3.1000,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Screening of Plant UDP-Glycosyltransferases for Betanin Production in Yeast.\",\"authors\":\"Christiane Glitz, Jane Dannow Dyekjær, Dovydas Vaitkus, Mahsa Babaei, Ditte Hededam Welner, Irina Borodina\",\"doi\":\"10.1007/s12010-024-05100-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>To cover the rising demand for natural food dyes, new sources and production methods are needed. Microbial fermentation of nature-identical colours, such as the red pigment betanin, has the potential to be a cost-efficient alternative to plant extraction. The last step of betanin production is catalysed by a UDP-glycosyltransferase (UGT). To find a high-performing UGT, we screened 27 UGTs from different plant species and tested their ability to produce betanin in vivo in Saccharomyces cerevisiae. We identified two new UGTs likely involved in the betanin synthesis in the plant they derive from: CqGT2 (UGT73A37) from Chenopodium quinoa and BgGT2 (UGT92X1) from Bougainvillea glabra. The betanin-producing UGTs were also tested in Yarrowia lipolytica, where CqGT2 was the best-performing glycosyltransferase for betanin production. While it has previously been shown that the UGTs can glycosylate either betanidin or cyclo-DOPA to ultimately form betanin, the molecular mechanism behind the preference for the acceptor molecule has not been elucidated. Therefore, we performed in silico structural analysis to characterise the betanin-producing UGTs further, particularly by looking into their binding mechanism. The docking model suggested that a smaller binding site found in some UGTs only allows glycosylation of cDOPA, while a wider binding site allows glycosylation of both cyclo-DOPA and betanidin.</p>\",\"PeriodicalId\":465,\"journal\":{\"name\":\"Applied Biochemistry and Biotechnology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":3.1000,\"publicationDate\":\"2025-01-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Applied Biochemistry and Biotechnology\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1007/s12010-024-05100-4\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Biochemistry and Biotechnology","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1007/s12010-024-05100-4","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Screening of Plant UDP-Glycosyltransferases for Betanin Production in Yeast.
To cover the rising demand for natural food dyes, new sources and production methods are needed. Microbial fermentation of nature-identical colours, such as the red pigment betanin, has the potential to be a cost-efficient alternative to plant extraction. The last step of betanin production is catalysed by a UDP-glycosyltransferase (UGT). To find a high-performing UGT, we screened 27 UGTs from different plant species and tested their ability to produce betanin in vivo in Saccharomyces cerevisiae. We identified two new UGTs likely involved in the betanin synthesis in the plant they derive from: CqGT2 (UGT73A37) from Chenopodium quinoa and BgGT2 (UGT92X1) from Bougainvillea glabra. The betanin-producing UGTs were also tested in Yarrowia lipolytica, where CqGT2 was the best-performing glycosyltransferase for betanin production. While it has previously been shown that the UGTs can glycosylate either betanidin or cyclo-DOPA to ultimately form betanin, the molecular mechanism behind the preference for the acceptor molecule has not been elucidated. Therefore, we performed in silico structural analysis to characterise the betanin-producing UGTs further, particularly by looking into their binding mechanism. The docking model suggested that a smaller binding site found in some UGTs only allows glycosylation of cDOPA, while a wider binding site allows glycosylation of both cyclo-DOPA and betanidin.
期刊介绍:
This journal is devoted to publishing the highest quality innovative papers in the fields of biochemistry and biotechnology. The typical focus of the journal is to report applications of novel scientific and technological breakthroughs, as well as technological subjects that are still in the proof-of-concept stage. Applied Biochemistry and Biotechnology provides a forum for case studies and practical concepts of biotechnology, utilization, including controls, statistical data analysis, problem descriptions unique to a particular application, and bioprocess economic analyses. The journal publishes reviews deemed of interest to readers, as well as book reviews, meeting and symposia notices, and news items relating to biotechnology in both the industrial and academic communities.
In addition, Applied Biochemistry and Biotechnology often publishes lists of patents and publications of special interest to readers.