Article(id=1315696632910430648, tenantId=1146029695717560320, journalId=1315121759093096577, issueId=1315696624781869390, articleNumber=null, orderNo=null, doi=10.3969/j.issn.1005-7021.2026.02.004, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1751817600000, receivedDateStr=2025-07-07, revisedDate=null, revisedDateStr=null, acceptedDate=null, acceptedDateStr=null, onlineDate=1791616121747, onlineDateStr=2026-10-10, pubDate=1776614400000, pubDateStr=2026-04-20, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1791616121747, onlineIssueDateStr=2026-10-10, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1791616121747, creator=13701087609, updateTime=1791616121747, updator=13701087609, issue=Issue{id=1315696624781869390, tenantId=1146029695717560320, journalId=1315121759093096577, year='2026', volume='46', issue='2', pageStart='1', pageEnd='136', issueExtLink='null', onlineDate='null', pubDate='1776614400000', pubDateStr='2026-04-20', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=null, createTime=1791616119809, creator='13701087609', updateTime=1791616211073, updator='13701087609', preIssue=null, nextIssue=null, articleTotal=null, ext={EN=IssueExt(id=1315697007629550369, tenantId=1146029695717560320, journalId=1315121759093096577, issueId=1315696624781869390, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1315697007629550370, tenantId=1146029695717560320, journalId=1315121759093096577, issueId=1315696624781869390, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null, downloadFileDto=null}, startPage=36, endPage=43, ext={EN=ArticleExt(id=1315696633082397113, articleId=1315696632910430648, tenantId=1146029695717560320, journalId=1315121759093096577, language=EN, title=Study on the Synthesis of Floridoside Through Trans-Glycosylation by
α-Galactosidase rAgaAJB07, columnId=null, journalTitle=Journal of Microbiology, columnName=null, runingTitle=null, highlight=null, articleAbstract=
Floridoside, a glycosyl alcohol exhibiting diverse biological activities including antioxidant effects, immune regulation, and protein stabilization, demonstrates significant potential for applications in the food and cosmetic industries. In our previous study, we successfully achieved the heterologous expression of the recombinant α-galactosidase rAgaAJB07 from Mesorhizobium, which catalyzes floridoside biosynthesis via trans-glycosylation was obtained. In order to improve floridoside production, the reaction conditions were systematically optimized for the recombinant enzyme using glycerol as the acceptor substrate and p-nitrophenyl α-D-galactopyranoside (pNPG) as the donor substrate. The optimal parameters were determined as follows: 500 mmol/L glycerol, 40 mmol/L pNPG, 1.5 U/mL enzyme concentration, 2 h reaction duration, pH 8.5, and 30 ℃. Under these conditions, recombinant rAgaAJB07 achieved a maximum floridoside yield with a 66.2% enhancement compared to baseline parameters, while simultaneously reducing the reaction time by 22 hours. This optimization strategy provides a robust methodological framework for scalable enzymatic synthesis of floridoside.
, authors=Xi SHEN
1, 4, Meng TIAN
1, Yue-lu ZHU
1, Xin-yue LI
1, Ling-xi QI
1, Rui ZHANG
1, 2, 3, 4, Jun-pei ZHOU
1, 2, 3, 4, *, authorsList=Xi SHEN, Meng TIAN, Yue-lu ZHU, Xin-yue LI, Ling-xi QI, Rui ZHANG, Jun-pei ZHOU, authorCompany=null, correspAuthors=Jun-pei ZHOU, authorNote=null, correspAuthorsNote=null, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=null, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, fund=null), CN=ArticleExt(id=1315696633745097146, articleId=1315696632910430648, tenantId=1146029695717560320, journalId=1315121759093096577, language=CN, title=
α-半乳糖苷酶rAgaAJB07转糖基合成红藻糖苷的研究, columnId=1315696197449405326, journalTitle=微生物学杂志, columnName=研究报告, runingTitle=null, highlight=null, articleAbstract=
红藻糖苷是一种具有抗氧化性、调节免疫系统、保护蛋白等生物活性的糖基醇,在食品和化妆品等领域具有广阔的应用前景。本实验室前期已成功实现了中慢生根瘤菌(Mesorhizobium)来源的α-半乳糖苷酶rAgaAJB07的异源表达,该酶可通过转糖基作用合成红藻糖苷。为提高红藻糖苷的产量,以甘油作为反应受体,对硝基苯基α-D-吡喃半乳糖苷(pNPG)作为反应供体,对rAgaAJB07合成红藻糖苷的条件进行优化。当甘油浓度为500 mmol/L,pNPG浓度40 mmol/L,酶浓度1.5 U/mL,反应时间2 h,反应pH 8.5,反应温度30 ℃时,rAgaAJB07合成红藻糖苷的产量达到最大,比优化前提高66.2%,反应时间缩短22 h,为红藻糖苷的酶法合成研究提供参考。
, authors=申熙
1, 4, 田萌
1, 朱悦露
1, 李新月
1, 祁玲曦
1, 张蕊
1, 2, 3, 4, 周峻沛
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2.Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Yunnan Normal University, Kunming 650500
3.Key Laboratory of Yunnan Provincial Education Department for Plateau Characteristic Food Enzymes, Yunnan Normal University, Kunming 650500
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3.云南师范大学云南省高校高原特色食品酶重点实验室,云南 昆明 650500
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