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Article(id=1153433636016742448, tenantId=1146029695717560320, journalId=1149652044408987649, issueId=1153433633999282214, articleNumber=null, orderNo=null, doi=10.19812/j.cnki.jfsq11-5956/ts.20250110008, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1736438400000, receivedDateStr=2025-01-10, revisedDate=null, revisedDateStr=null, acceptedDate=null, acceptedDateStr=null, onlineDate=1752929608587, onlineDateStr=2025-07-19, pubDate=1742832000000, pubDateStr=2025-03-25, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1752929608587, onlineIssueDateStr=2025-07-19, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1752929608587, creator=13701087609, updateTime=1752929608587, updator=13701087609, issue=Issue{id=1153433633999282214, tenantId=1146029695717560320, journalId=1149652044408987649, year='2025', volume='16', issue='6', pageStart='1', pageEnd='322', issueExtLink='null', onlineDate='null', pubDate='null', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=0, createTime=1752929608105, creator=13701087609, updateTime=1758086445549, updator=13701087609, preIssue=null, nextIssue=null, ext={EN=IssueExt(id=1175062977960096080, tenantId=1146029695717560320, journalId=1149652044408987649, issueId=1153433633999282214, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1175062977960096081, tenantId=1146029695717560320, journalId=1149652044408987649, issueId=1153433633999282214, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null}, startPage=232, endPage=238, ext={EN=ArticleExt(id=1153433636901740599, articleId=1153433636016742448, tenantId=1146029695717560320, journalId=1149652044408987649, language=EN, title=Induced expression and enzymatic properties of recombinant bacterial laccase degrading sulfadiazine, columnId=1153433636805271605, journalTitle=Journal of Food Safety & Quality, columnName=Special Topic: Application of Enzyme Technology in Food Engineering, runingTitle=null, highlight=null, articleAbstract=

Objective To investigate the induced expression level and enzymatic properties of recombinant bacterial laccase and to improve the degradation efficiency of sulfadiazine antibiotics by bacterial laccase. Methods In this study, the effects of induction temperature, induction time, and concentration of isopropyl β-D-thiogalactopyranoside (IPTG) on enzyme expression were investigated by one-way experiments. The enzymatic properties of recombinant bacterial laccase were also investigated by both pH and temperature. Results The degradation of sulfadiazine by recombinant bacterial laccase at 24 h was 50%. The optimal conditions for the expression of recombinant bacterial laccase in Escherichia coli BL21 (DE3) were as follows: Induction temperature of 16 ℃, induction time of 16 h, and IPTG concentration of 0.2 mmol/L. The optimal pH was 3, and the stability was best at pH 7, with the enzyme activity reaching 150% in 6 h. The optimal temperature was 80 ℃, and the thermal stability was best at 70 ℃, with the enzyme activity increasing to 120% in 1 h. The half-life was about 6 h. Conclusion This study provides an experimental basis for the application of bacterial laccase in the degradation of sulfadiazine antibiotics and lays down a theoretical basis for the future study of its potential application in the industry.

, correspAuthors=Bo XIA, Xia LIU, 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, authorCompany=null, fund=null, authors=null, authorsList=Jing-Han WANG, Li PANG, Hong TIAN, Yi-Ya ZHAN, Yong-Zhen YI, Bo XIA, Xia LIU), CN=ArticleExt(id=1153433673027281260, articleId=1153433636016742448, tenantId=1146029695717560320, journalId=1149652044408987649, language=CN, title=可降解磺胺嘧啶的重组细菌漆酶诱导表达和酶学性质研究, columnId=1153433636968849465, journalTitle=食品安全质量检测学报, columnName=本期专题：酶技术在食品工程中的应用, runingTitle=null, highlight=null, articleAbstract=

目的 探究重组细菌漆酶诱导表达水平及酶学特性, 提高细菌漆酶对磺胺嘧啶抗生素的降解效率。方法 本研究通过单因素实验探讨了诱导温度、诱导时间以及异丙基-β-D-硫代半乳糖苷(isopropyl β-D-thiogalactopyranoside, IPTG)浓度对酶表达量的影响。并通过pH和温度两方面对重组细菌漆酶的酶学性质进行探究。结果 24 h重组细菌漆酶对磺胺嘧啶的降解率达50%。重组细菌漆酶在大肠杆菌BL21 (DE3)中的最适表达条件为: 诱导温度16 ℃, 诱导时间16 h, IPTG浓度0.2 mmol/L。最适pH为3, 在pH为7时, 稳定性最好, 6 h酶活达到150%; 最适温度为80 ℃, 在温度为70 ℃时热稳定性最好, 1 h提高到120%, 半衰期约为6 h。结论 本研究为细菌漆酶在磺胺嘧啶抗生素降解中的应用提供了实验基础, 并为未来研究其在工业中的潜在应用奠定了理论依据。

, correspAuthors=夏菠, 刘霞, authorNote=null, correspAuthorsNote=
* 夏菠(1980—), 男, 副教授, 博士, 主要研究方向为生物转化与生物降解。E-mail:
刘霞(1976—), 女, 教授, 博士, 主要研究方向为食品质量与安全。E-mail:
, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=MJEf6pCwuKcJTM5ABgkBbA==, magXml=IwdhZxSuUsSiu8Xs0GsYZQ==, pdfUrl=null, pdf=S5+kpMhgAcn+WdQ008MStg==, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=LbsOTFJXsv1Khqn5VR+jRg==, mapNumber=null, authorCompany=null, fund=null, authors=

王婧涵(1997—), 女, 硕士研究生, 主要研究方向为生物降解。E-mail:

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王婧涵(1997—), 女, 硕士研究生, 主要研究方向为生物降解。E-mail:

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王婧涵(1997—), 女, 硕士研究生, 主要研究方向为生物降解。E-mail:

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Bioresource Technology, 2010, 102(3): 3126-3137., articleTitle=Cloning and functional analysis of a new laccase gene from Trametes sp. 48424 which had the high yield of laccase and strong ability for decolorizing different dyes, refAbstract=null), Reference(id=1175086990786703370, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, doi=null, pmid=null, pmcid=null, year=2022, volume=null, issue=null, pageStart=null, pageEnd=null, url=null, language=null, rfNumber=[26], rfOrder=31, authorNames=牛亚春, journalName=甘油单酯脂肪酶GMGL的高效表达及固定化研究, refType=null, unstructuredReference=牛亚春. 甘油单酯脂肪酶GMGL的高效表达及固定化研究[D]. 广州: 华南理工大学, 2022., articleTitle=null, refAbstract=null), Reference(id=1175086990858006539, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, doi=null, pmid=null, pmcid=null, year=2022, volume=null, issue=null, pageStart=null, pageEnd=null, url=null, language=null, rfNumber=[26], rfOrder=32, authorNames=NIU YC, journalName=High-efficiency expression and immobilization of monoacylglycerol lipase GMGL, refType=null, unstructuredReference=NIU YC. High-efficiency expression and immobilization of monoacylglycerol lipase GMGL[D]. Guangzhou: South China University of Technology, 2022., articleTitle=null, refAbstract=null), Reference(id=1175086990920921100, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, doi=null, pmid=null, pmcid=null, year=2018, volume=24, issue=6, pageStart=718, pageEnd=725, url=null, language=null, rfNumber=[27], rfOrder=33, authorNames=HAYAT SMG, FARAHANI N, GOLICHENARI B, journalName=Current Pharmaceutical Design, refType=null, unstructuredReference=HAYAT SMG, FARAHANI N, GOLICHENARI B, et al. Recombinant protein expression in Escherichia coli (E. coli): What we need to know[J]. 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Dyes and Pigments, 2007, 74(1): 123-126., articleTitle=The effect of violuric acid on the decolourization of recalcitrant dyes by laccase from Trametes hirsute, refAbstract=null), Reference(id=1175086991109664783, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, doi=null, pmid=null, pmcid=null, year=2011, volume=115, issue=null, pageStart=35, pageEnd=40, url=null, language=null, rfNumber=[30], rfOrder=36, authorNames=LU L, ZHAO M, WANG TN, journalName=Bioresource Technology, refType=null, unstructuredReference=LU L, ZHAO M, WANG TN, et al. Characterization and dye decolorization ability of an alkaline resistant and organic solvents tolerant laccase from Bacillus licheniformis LS04[J]. Bioresource Technology, 2011, 115: 35-40., articleTitle=Characterization and dye decolorization ability of an alkaline resistant and organic solvents tolerant laccase from Bacillus licheniformis LS04, refAbstract=null), Reference(id=1175086991168385040, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, doi=null, pmid=null, pmcid=null, year=2007, volume=23, issue=null, pageStart=823, pageEnd=832, url=null, language=null, rfNumber=[31], rfOrder=37, authorNames=SHARMA P, GOEL R, CAPALASH N, journalName=World Journal of Microbiology and Biotechnology, refType=null, unstructuredReference=SHARMA P, GOEL R, CAPALASH N. Bacterial laccases[J]. World Journal of Microbiology and Biotechnology, 2007, 23: 823-832., articleTitle=Bacterial laccases, refAbstract=null)], funds=[Fund(id=1175086988366590954, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, awardId=2022JJ30299, language=CN, fundingSource=湖南省自然科学基金项目(2022JJ30299), fundOrder=null, country=null), Fund(id=1175086988542751723, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, awardId=2022JJ30290, language=CN, fundingSource=湖南省自然科学基金项目(2022JJ30290), fundOrder=null, country=null)], companyList=[AuthorCompany(id=1175086983807382429, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, xref=null, ext=[AuthorCompanyExt(id=1175086983815771038, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, companyId=1175086983807382429, language=EN, country=null, province=null, city=null, postcode=null, companyName=null, departmentName=null, remark=1. 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注: M. Maker; L1. 诱导后菌液; L2. 诱导破碎后上清液; L3. 诱导破碎后沉淀。

, figureFileSmall=+TFmDbxTcsV9iTJR01dn8Q==, figureFileBig=LTVxNsrVU2g6WFgQT4pQkA==, tableContent=null), ArticleFig(id=1175086986407850964, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Fig.2, caption=SDS-PAGE plots of recombinant laccase solution after His-tag purification, figureFileSmall=r+ImobzXWWM56efv4LcD2A==, figureFileBig=20fqfdcZvehC7D5mrRcn8g==, tableContent=null), ArticleFig(id=1175086986487542741, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=图2, caption=His标签纯化后的重组漆酶液的SDS-PAGE图

注: M. Marker; CL. 裂解液; FT. 穿流液; E1~E5. 洗脱次数1~5次。

, figureFileSmall=r+ImobzXWWM56efv4LcD2A==, figureFileBig=20fqfdcZvehC7D5mrRcn8g==, tableContent=null), ArticleFig(id=1175086986563040214, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Fig.3, caption=Degradation rate of sulfadiazine by recombinant bacterial laccase, figureFileSmall=lEMDISYGXuRErsYO8rnvjw==, figureFileBig=IsaRdZ9ZM4HtelClOu0WVg==, tableContent=null), ArticleFig(id=1175086986613371863, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=图3, caption=重组细菌漆酶对磺胺嘧啶的降解率

注: a. 磺胺嘧啶标准曲线; b. 重组细菌漆酶对磺胺嘧啶的降解率; ****代表P<0.0001。

, figureFileSmall=lEMDISYGXuRErsYO8rnvjw==, figureFileBig=IsaRdZ9ZM4HtelClOu0WVg==, tableContent=null), ArticleFig(id=1175086986684675032, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Fig.4, caption=Effects of different induction temperatures on enzyme expression quantity, figureFileSmall=m6UYLz2zdbkcXdZD+NltyQ==, figureFileBig=aGprrb6Z7Of31UVQs7ZWnA==, tableContent=null), ArticleFig(id=1175086986751783897, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=图4, caption=诱导温度对酶表达量的影响

注: M. Maker; L1. 12 ℃; L2. 28 ℃; L3. 37 ℃; L4. 42 ℃; L5. 16 ℃。

, figureFileSmall=m6UYLz2zdbkcXdZD+NltyQ==, figureFileBig=aGprrb6Z7Of31UVQs7ZWnA==, tableContent=null), ArticleFig(id=1175086986818892762, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Fig.5, caption=Effects of different induction times on enzyme expression quantity, figureFileSmall=SCBwHbLU9X4kw5j5IgE6EQ==, figureFileBig=5iF4pcNuuEmAJiVSubB9ew==, tableContent=null), ArticleFig(id=1175086986886001627, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=图5, caption=诱导时间对酶表达量的影响

注: M. Maker; L1. 4 h; L2. 8 h; L3. 12 h; L4. 16 h; L5. 20 h; L6. 24 h。

, figureFileSmall=SCBwHbLU9X4kw5j5IgE6EQ==, figureFileBig=5iF4pcNuuEmAJiVSubB9ew==, tableContent=null), ArticleFig(id=1175086986948916188, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Fig.6, caption=Effects of different IPTG concentration on enzyme expression quantity, figureFileSmall=I26d/ghGwislISEs7w5aSA==, figureFileBig=o1ZXYaBS9mp4COAgLQYQIw==, tableContent=null), ArticleFig(id=1175086987007636445, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=图6, caption=IPTG浓度对酶表达量的影响

注: M. Maker; L1. 诱导前; L2. 0.05 mmol/L; L3. 0.1 mmol/L; L4. 0.2 mmol/L; L5. 0.4 mmol/L; L6. 0.6 mmol/L; L7. 0.8 mmol/L; L8. 1.0 mmol/L。

, figureFileSmall=I26d/ghGwislISEs7w5aSA==, figureFileBig=o1ZXYaBS9mp4COAgLQYQIw==, tableContent=null), ArticleFig(id=1175086987108299742, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Fig.7, caption=Optimal pH (a) and pH stability (b), figureFileSmall=Ub0M3LZl0lmh3N/r3/vb8A==, figureFileBig=H3g70pgTU6oYZx9p2weKtA==, tableContent=null), ArticleFig(id=1175086987229934559, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=图7, caption=最适pH (a)和pH稳定性(b), figureFileSmall=Ub0M3LZl0lmh3N/r3/vb8A==, figureFileBig=H3g70pgTU6oYZx9p2weKtA==, tableContent=null), ArticleFig(id=1175086987309626336, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Fig.8, caption=Optimal temperature (a) and temperature stability (b), figureFileSmall=REa8BFlqjyB+XtthfutYTw==, figureFileBig=hzIm3VmxPxyn1EnAcdbz4A==, tableContent=null), ArticleFig(id=1175086987376735201, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=图8, caption=最适温度(a)和温度稳定性(b), figureFileSmall=REa8BFlqjyB+XtthfutYTw==, figureFileBig=hzIm3VmxPxyn1EnAcdbz4A==, tableContent=null), ArticleFig(id=1175086987469009890, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Table 1, caption=

ImageJ grey scale analysis of SDS-PAGE electrophoresis results at protein purification

, figureFileSmall=null, figureFileBig=null, tableContent=
洗脱
次数		 区域 区域内灰度平均值 最大
灰度		 校正后的像素总和
E1 1180 7.919 38 9435
E2 1180 52.058 119 61428
E3 1180 64.203 119 75759
E4 1180 60.386 119 71256
E5 1180 42.904 115 50627
), ArticleFig(id=1175086987586450403, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=表1, caption=

ImageJ灰度分析蛋白纯化SDS-PAGE电泳结果

, figureFileSmall=null, figureFileBig=null, tableContent=
洗脱
次数		 区域 区域内灰度平均值 最大
灰度		 校正后的像素总和
E1 1180 7.919 38 9435
E2 1180 52.058 119 61428
E3 1180 64.203 119 75759
E4 1180 60.386 119 71256
E5 1180 42.904 115 50627
), ArticleFig(id=1175086987653559268, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Table 2, caption=

ImageJ grey scale analysis of SDS-PAGE electrophoresis results at different induction temperatures

, figureFileSmall=null, figureFileBig=null, tableContent=
诱导温度/℃ 区域 区域内灰度平均值 最大灰度 校正后的像素总和
12 11016 41.949 168 462109
16 11016 92.118 194 1014776
28 11016 89.427 187 985152
37 11016 60.689 178 668552
42 11016 105.02 204 1156901
), ArticleFig(id=1175086987745833957, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=表2, caption=

ImageJ灰度分析不同诱导温度下SDS-PAGE电泳结果

, figureFileSmall=null, figureFileBig=null, tableContent=
诱导温度/℃ 区域 区域内灰度平均值 最大灰度 校正后的像素总和
12 11016 41.949 168 462109
16 11016 92.118 194 1014776
28 11016 89.427 187 985152
37 11016 60.689 178 668552
42 11016 105.02 204 1156901
), ArticleFig(id=1175086987955549158, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=EN, label=Table 3, caption=

ImageJ grey scale analysis of SDS-PAGE electrophoresis results at different induction times

, figureFileSmall=null, figureFileBig=null, tableContent=
诱导
时间/h		 区域 区域内灰度
平均值		 最大灰度 校正后的
像素总和
4 3760 10.635 86 39987
8 3760 21.008 112 78989
12 3760 55.031 152 206916
16 3760 78.727 165 296014
20 3760 47.529 152 178710
24 3760 53.319 154 200478
), ArticleFig(id=1175086988068795367, tenantId=1146029695717560320, journalId=1149652044408987649, articleId=1153433636016742448, language=CN, label=表3, caption=

ImageJ灰度分析不同诱导时间下SDS-PAGE电泳结果

, figureFileSmall=null, figureFileBig=null, tableContent=
诱导
时间/h		 区域 区域内灰度
平均值		 最大灰度 校正后的
像素总和
4 3760 10.635 86 39987
8 3760 21.008 112 78989
12 3760 55.031 152 206916
16 3760 78.727 165 296014
20 3760 47.529 152 178710
24 3760 53.319 154 200478
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ImageJ grey scale analysis of SDS-PAGE electrophoresis results at different IPTG-induced concentration

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IPTG浓度/(mmol/L) 区域 区域内灰度平均值 最大灰度 校正后的像素总和
0.05 1932 34.66 145 66964
0.1 1932 29.128 132 56275
0.2 1932 65.651 170 126837
0.4 1932 61.365 170 118557
0.6 1932 41.32 157 79830
0.8 1932 61.205 167 118279
1.0 1932 33.165 144 64074
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ImageJ灰度分析不同IPTG浓度下SDS-PAGE电泳结果

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IPTG浓度/(mmol/L) 区域 区域内灰度平均值 最大灰度 校正后的像素总和
0.05 1932 34.66 145 66964
0.1 1932 29.128 132 56275
0.2 1932 65.651 170 126837
0.4 1932 61.365 170 118557
0.6 1932 41.32 157 79830
0.8 1932 61.205 167 118279
1.0 1932 33.165 144 64074
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可降解磺胺嘧啶的重组细菌漆酶诱导表达和酶学性质研究
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王婧涵 1 , 庞立 2 , 田红 1 , 詹依雅 1 , 易永真 1 , 夏菠 1, * , 刘霞 1, *
食品安全质量检测学报 | 本期专题：酶技术在食品工程中的应用 2025,16(6): 232-238
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食品安全质量检测学报 | 本期专题：酶技术在食品工程中的应用 2025, 16(6): 232-238
可降解磺胺嘧啶的重组细菌漆酶诱导表达和酶学性质研究
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王婧涵1 , 庞立2, 田红1, 詹依雅1, 易永真1, 夏菠1, * , 刘霞1, *
作者信息
  • 1.湖南农业大学食品科学技术学院, 长沙 410128
  • 2.湖南农业大学园艺学院, 长沙 410128

    • 王婧涵(1997—), 女, 硕士研究生, 主要研究方向为生物降解。E-mail:

通讯作者:

* 夏菠(1980—), 男, 副教授, 博士, 主要研究方向为生物转化与生物降解。E-mail:
刘霞(1976—), 女, 教授, 博士, 主要研究方向为食品质量与安全。E-mail:
Induced expression and enzymatic properties of recombinant bacterial laccase degrading sulfadiazine
Jing-Han WANG1 , Li PANG2, Hong TIAN1, Yi-Ya ZHAN1, Yong-Zhen YI1, Bo XIA1, * , Xia LIU1, *
Affiliations
  • 1. College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China
  • 2. College of Horticulture, Hunan Agricultural University, Changsha 410128, China
出版时间: 2025-03-25 doi: 10.19812/j.cnki.jfsq11-5956/ts.20250110008
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摘要
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目的 探究重组细菌漆酶诱导表达水平及酶学特性, 提高细菌漆酶对磺胺嘧啶抗生素的降解效率。方法 本研究通过单因素实验探讨了诱导温度、诱导时间以及异丙基-β-D-硫代半乳糖苷(isopropyl β-D-thiogalactopyranoside, IPTG)浓度对酶表达量的影响。并通过pH和温度两方面对重组细菌漆酶的酶学性质进行探究。结果 24 h重组细菌漆酶对磺胺嘧啶的降解率达50%。重组细菌漆酶在大肠杆菌BL21 (DE3)中的最适表达条件为: 诱导温度16 ℃, 诱导时间16 h, IPTG浓度0.2 mmol/L。最适pH为3, 在pH为7时, 稳定性最好, 6 h酶活达到150%; 最适温度为80 ℃, 在温度为70 ℃时热稳定性最好, 1 h提高到120%, 半衰期约为6 h。结论 本研究为细菌漆酶在磺胺嘧啶抗生素降解中的应用提供了实验基础, 并为未来研究其在工业中的潜在应用奠定了理论依据。

细菌漆酶  /  磺胺嘧啶  /  抗生素降解  /  异源表达  /  酶学性质  /  蛋白浓度

Objective To investigate the induced expression level and enzymatic properties of recombinant bacterial laccase and to improve the degradation efficiency of sulfadiazine antibiotics by bacterial laccase. Methods In this study, the effects of induction temperature, induction time, and concentration of isopropyl β-D-thiogalactopyranoside (IPTG) on enzyme expression were investigated by one-way experiments. The enzymatic properties of recombinant bacterial laccase were also investigated by both pH and temperature. Results The degradation of sulfadiazine by recombinant bacterial laccase at 24 h was 50%. The optimal conditions for the expression of recombinant bacterial laccase in Escherichia coli BL21 (DE3) were as follows: Induction temperature of 16 ℃, induction time of 16 h, and IPTG concentration of 0.2 mmol/L. The optimal pH was 3, and the stability was best at pH 7, with the enzyme activity reaching 150% in 6 h. The optimal temperature was 80 ℃, and the thermal stability was best at 70 ℃, with the enzyme activity increasing to 120% in 1 h. The half-life was about 6 h. Conclusion This study provides an experimental basis for the application of bacterial laccase in the degradation of sulfadiazine antibiotics and lays down a theoretical basis for the future study of its potential application in the industry.

bacterial laccase  /  sulfadiazine  /  antibiotic degradation  /  heterologous expression  /  enzymatic properties  /  protein concentration
王婧涵, 庞立, 田红, 詹依雅, 易永真, 夏菠, 刘霞. 可降解磺胺嘧啶的重组细菌漆酶诱导表达和酶学性质研究. 食品安全质量检测学报, 2025 , 16 (6) : 232 -238 . DOI: 10.19812/j.cnki.jfsq11-5956/ts.20250110008
Jing-Han WANG, Li PANG, Hong TIAN, Yi-Ya ZHAN, Yong-Zhen YI, Bo XIA, Xia LIU. Induced expression and enzymatic properties of recombinant bacterial laccase degrading sulfadiazine[J]. Journal of Food Safety & Quality, 2025 , 16 (6) : 232 -238 . DOI: 10.19812/j.cnki.jfsq11-5956/ts.20250110008
正文
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0 引言
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磺胺类抗生素(sulfonamide antibiotics, SAs)是一种广谱抑菌剂, 可以阻断四氢叶酸的合成, 从而抑制细菌蛋白质生长而起到抗菌的作用。磺胺嘧啶在人体和动物医学中有广泛的应用, 因而在土壤和水生生态系统中普遍存在, 且半衰期较长。磺胺类抗生素可能增加病原菌的耐药性, 加速抗生素耐药性的传播, 导致更高的人类发病率感染与死亡率[1]。磺胺类抗生素的降解方法分为非生物降解和生物降解。非生物降解需要额外的装置和能量, 产生更高的费用。生物降解大多是微生物降解, 单独使用微生物降解, 在后期菌株对反应环境的影响和菌株的培养与鉴定都存在许多不确定因素。而使用特定的酶法降解磺胺类抗生素, 是一种清洁且高效的方法。并且酶相较于微生物更易控制和分离, 通过固定化酶等方法可以应用于食品中。
漆酶(EC 1.10.3.2), 是一种含铜的多酚氧化酶, 能够氧化多种酚类和非酚类化合物, 同时伴随4个氢质子转移, 将氧分子转化为水[2]。是一种对环境友好的“绿色酶”, 广泛存在于真菌[3]、细菌[4]和植物[5]中, 漆酶在很多方面都有应用, 如染料的脱色[6]、生物传感器[7]、废水处理[8-9]、纺织品[10]、食品工业[11]、造纸和纸浆生产[12]、化妆品[13]和油漆[14]。漆酶分为真菌漆酶和细菌漆酶, 真菌漆酶生产时间较长、成本较高, 并且在高温、高碱和高盐条件下不稳定[15]。而细菌漆酶可以在很大程度上弥补真菌漆酶的各种缺点。近年来对细菌漆酶的研究和应用迅速增长[16]。部分细菌漆酶可以在高温条件下保留较高的酶活性。细菌漆酶在中性和碱性条件下稳定, 对抑制剂的敏感性较低, 对金属离子的依赖性较低, 并易于异源表达。异源表达可以提供更高的酶产率, 并且可以允许产生具有用于工业应用的期望性质的漆酶[17]。不同的宿主包括大肠杆菌、巴斯德毕赤酵母、酿酒酵母等已被普遍用作重组漆酶表达的宿主生物[18]。基于细菌漆酶容易进行异源表达, 能通过异源表达提高细菌漆酶的产量和纯度, 进行成本更为有效的生产、提高工业价值。因此选择合适的诱导方法尤为关键。
本研究使用来自死谷芽孢杆菌Bacillus vallismortis fmb-103的细菌漆酶, 通过之前的研究得出该细菌漆酶可以在大肠杆菌中异源表达, 并且有较好的耐热性, 具有降解孔雀蓝、磺胺嘧啶的能力, 有很好的研究前景。故对酶学特性进一步挖掘。将可降解磺胺嘧啶的重组细菌漆酶质粒转入大肠杆菌BL21(DE3)中进行诱导表达, 并系统优化诱导条件, 包括诱导温度、诱导时间及异丙基-β-D-硫代半乳糖苷(isopropyl β-D-thiogalactopyranoside, IPTG)浓度, 以期提高重组细菌漆酶蛋白的表达水平。与此同时, 研究还通过探讨pH和温度对重组细菌漆酶酶学性质的影响, 分析其最适反应条件及稳定性。以期为细菌漆酶降解磺胺嘧啶在工业生产中的应用奠定重要的理论基础。
1 材料与方法
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1.1 材料与试剂
选择Bacillus vallismortis fmb-103的漆酶进行后续研究, GeneBank: KC859464.1, 并用SDla代表; pGBTNH2- SDla质粒(深圳市博奥康生物科技公司); 感受态大肠杆菌(BL21)、IPTG(质量浓度50 mg/mL)、氨苄青霉素(质量浓度50 μg/mL)、琼脂糖凝胶DNA回收试剂盒[天根生化科技(北京)有限公司]; His标签纯化试剂盒(上海碧云天生物技术有限公司); 2,2-联氮-二(3-乙基-苯并噻唑-6-磺酸)二铵盐[ABTS](分析纯, 上海麦克林生化科技股份有限公司); 磺胺嘧啶[分析纯, 梯希爱(上海)化成工业发展有限公司]。
1.2 仪器与设备
Bio-Photometer紫外可见光分光光度计(上海艾本德国际贸易有限公司); JY96-IIN超声破碎仪(宁波新芝生物科技股份有限公司); ZNCL-B智能磁力搅拌器(河南佰年仪器有限公司); 赛默飞Vanquish Core液相色谱仪[赛默飞世尔科技(中国)有限公司)]。
1.3 实验方法
1.3.1 细菌漆酶重组质粒的转化和诱导表达
将含有细胞漆酶基因的克隆质粒物热激至大肠杆菌BL21(DE3)表达菌株中, 涂布于含100 μg/mL氨苄青霉素抗性的LB平板上。挑取阳性菌落送往上海生工生物工程股份有限公司进行测序。测序正确的菌液, 按3% (V/V)加入含100 μg/mL氨苄青霉素抗性的LB液体培养基, 将混合物在37 °C下旋转振荡孵育。当细胞达到指数生长期(OD600=0.6~0.8), 加入0.1 mmol/L IPTG 100 μg/mL诱导产酶, 16 ℃孵育16 h。
1.3.2 重组细菌漆酶粗酶液的获取与蛋白纯化
吸取10 mL的大肠杆菌BL21(DE3)菌液于6000 r/min离心10 min, 收集菌体。加入等体积细菌蛋白制备裂解液, 冰浴条件下超声波破碎20 min。将裂解液于12000 r/min离心10 min, 收集上清液即为可溶性蛋白并用于蛋白纯化。粗酶液采用His标签纯化试剂盒进行, 在重组漆酶破碎粗酶液中加入已平衡的50% BeyoGold™ His-tag纯化树脂, 混匀后在冰浴环境下缓慢摇动60 min, 使His标签重组蛋白与镍柱充分结合。用非变性洗脱液洗柱5次, 并收集洗脱液至离心管中。对得到的各组分收集液进行十二烷基硫酸钠-聚丙烯酰胺凝胶(sodium dodecyl sulfate - polyacrylamide gel electrophoresis, SDS-PAGE)电泳检测[19-20]。
1.3.3 重组细菌漆酶对磺胺嘧啶抗生素的降解效果
将1.5 mg/L的重组细菌漆酶酶液添加至终质量浓度为1 mg/L的磺胺嘧啶体系中, 在30 ℃反应24 h, 取1 mL反应产物过膜装样, 进行液相色谱检测。
1.3.4 SDS-PAGE电泳分析
将蛋白质样品和上样缓冲液按4:1 (V:V)混合, 置于100 ℃水浴加热10 min。按配方制备10%分离胶、4%浓缩胶, 观察洗脱蛋白的分子质量大小和纯度。
1.3.5 重组漆酶SDla诱导表达的条件优化
(1)诱导温度对重组细菌漆酶表达量的影响
在20 mL含氨苄青霉素的LB液体培养基中培养重组菌株, 同1.3.1, 加入终浓度为0.1 mmol/L的IPTG于12、16、28、37、42 ℃以100 r/min分别诱导16 h, 取10 μL菌液进行SDS-PAGE电泳检测。
(2)诱导时间对重组细菌漆酶表达量的影响
在20 mL含氨苄青霉素的LB液体培养基中培养重组菌株, 同1.3.1, 加入终浓度为0.1 mmol/L的IPTG于16 ℃以100 r/min分别诱导4、8、12、16、20、24 h, 取10 μL菌液进行SDS-PAGE电泳检测。
(3) IPTG浓度对重组细菌漆酶表达量的影响
在20 mL含氨苄青霉素的LB液体培养基中培养重组菌株, 同1.3.1, 加入终浓度为0.05、0.1、0.2、0.4、0.6、0.8、1.0 mmol/L的IPTG于16 ℃以100 r/min分别诱导16 h, 取10 μL菌液进行SDS-PAGE电泳检测。
1.3.6 重组漆酶SDla的酶学性质
(1)酶活活力测定
以ABTS为底物, 反应体系总体积3 mL, 包括2.45 mL 0.1 mol/L pH 5醋酸钠缓冲液、0.5 mL 6 mmol/L ABTS及50 μL酶液, 45 ℃反应3 min, 在420 nm吸光值OD的增量[20], 以水替换酶液做为对照。以每分钟内生成1 μmol反应物所需的酶量为一个酶活力单位。实验重复3次, 取平均值。漆酶酶活计算公式见(1)。
$\text { 漆酶酶活力 }(\mathrm{U})=\frac{V_{\text {总 }} \times \Delta \mathrm{OD} \times \text { 酶液稀释倍数 }}{V_{\text {酶 }} \times \varepsilon \times \Delta t \times 10^{-6}}$
式中: V总为反应总体系的体积, mL; V酶为反应体系中酶的体积, mL; ΔOD为反应时间OD值的变化; Δt为反应时间, min; ε=36000 M/cm。
(2)最适pH及pH稳定性
分别加入pH为2~8的醋酸钠缓冲液, 再加入50 μL重组漆酶酶液, 在45 ℃反应3 min, 在420 nm下测定吸光值, 根据上述方法计算酶活。在4 ℃下将漆酶在pH (2、3、7)下孵育6 h, 每隔1 h取样, 迅速冰浴, 以初始时酶活定为100%, 以残余酶活百分比表示测定结果, 使用ABTS作为底物测量残余活性。以pH为横坐标, 相对酶活力为纵坐标作图, 得到重组漆酶的最适pH和pH稳定性。
(3)最适温度及温度稳定性
将加入ABTS底物的缓冲液(pH 3)分别在30~90 ℃水浴中孵育10 min, 准确加入50 μL重组漆酶酶液, 分别在以上各个温度条件下反应3 min, 在420 nm下测定吸光值, 根据上述方法计算酶活。将酶溶液放置在70、80、90 ℃水浴中保温6 h, 每隔1 h取样, 迅速冰浴, 在所有实验组保温结束后使用ABTS作为底物测量残余活性, 以初始时酶活定为100%, 以残余酶活百分比表示测定结果。以温度为横坐标, 相对酶活力为纵坐标作图, 得到重组漆酶的最适温度和温度稳定性。
1.3.7 液相色谱仪器条件
色谱柱为Kromasil 100-5-C18 (250 mm×4.6 mm), 流动相为0.1%甲酸水:乙腈(70:30, V:V), 流速为1.0 mL/min, 波长为265 nm, 柱温30 ℃, 进样量为10 μL。
1.4 数据处理
所有实验均重复进行3次, 以确保结果的可靠性和可重复性。实验数据通过使用GraphPad Prism 9.0软件进行详细的统计学分析, 并可视化数据结果。
2 结果与分析
收起
2.1 重组细菌漆酶的诱导表达及分离纯化
如图1 SDS-PAGE分析的粗酶液结果所示, 在65 kDa处出现了特征条带。而且在诱导表达前无SDla相对应的条带, 并在诱导后的上清液中观察到目标蛋白的条带, 表明重组工程菌成功可溶性表达了细菌漆酶。
为了进一步纯化重组表达带有His标签SDla漆酶蛋白, 采用了镍柱亲和层析的方法。该方法基于His标签与镍离子之间的强亲和力, 通过镍柱可以特异性纯化目标蛋白[19]。收集的各组分洗涤液和洗脱液通过SDS-PAGE电泳分析, 以检测His标签重组蛋白的纯化效果。通过ImageJ软件对灰度值进行分析, 灰度值越高意味着诱导表达的蛋白量增加。根据电泳结果, 选择含有目标蛋白的洗脱液进行储存, 图2结果所示, 第3次洗脱(E3)的蛋白的表达量最高且灰度值也最高(表1)。
2.2 重组细菌漆酶对磺胺嘧啶的降解效果
如图3结果所示, 诱导表达成功的重组细菌漆酶可以降解磺胺嘧啶抗生素, 并且24 h降解效果可达50.00%±0.69%。在24 h, 重组细菌漆酶SDla对磺胺嘧啶的降解效果高于来自枯草芽孢杆菌WD23、X1的细菌漆酶[21]。
2.3 重组细菌漆酶诱导表达的条件优化
2.3.1 诱导温度对重组细菌漆酶SDla表达量的影响
从图4可以看出, 重组蛋白在大肠杆菌的表达会受到诱导温度的影响[22-23], 低温会防止包涵体的形成, 减少质粒丢失的可能性[24]。16 ℃蛋白表达量最高, 随着温度升高蛋白量逐渐下降, 并且灰度值最高(表2)。因此在后续实验中选用16 ℃作为诱导温度。
2.3.2 诱导时间对重组漆酶SDla表达量的影响
如图5所示, 诱导时间的合理选择对重组蛋白表达至关重要[25]。蛋白表达量随诱导时间的延长而增加, 在16 h达到最大, 延长诱导时间, 不会增加蛋白表达量, 且16 h的灰度值最高(表3), 故选择16 h为诱导时间。
2.3.3 IPTG浓度对重组漆酶SDla表达量的影响
诱导剂浓度至关重要, 根据研究已经证明IPTG浓度在0~1 mmol/L之间的样品对大肠杆菌的生长不会有毒性作用[26-27]。如图6所示, IPTG在0.2 mmol/L时, 蛋白质表达量均高于其他组, 灰度值(表4)也高于其他组, 因此选择IPTG浓度为0.2 mmol/L进行后续实验。
2.4 重组细菌漆酶的酶学性质
2.4.1 最适pH和pH稳定性
图7显示pH对重组漆酶SDla的影响。以ABTS为底物, 在pH为3的时候酶活达到最高, 比枯草芽孢杆菌漆酶(pH 4.2)和真菌漆酶更耐酸[28-29]。重组漆酶更耐酸可能是由于在之前的基础上更换了缓冲液类型, 不使用柠檬酸-磷酸盐溶液, 而是采用醋酸-醋酸钠溶液。不同缓冲液的最适pH是不同的。图7b所示, 1 h时, 3个pH条件下重组漆酶SDla的酶活稳定不变。在pH 7条件下, 酶活随反应时间的延长而增加, 3 h到达顶峰后缓慢下降, 6 h时酶活仍有150%。而pH 2和pH 3反应条件的酶活变化趋势接近, 反应时间越长, 酶活越低。6 h时, pH 3的酶活高于pH 2, 酶活仅有50%。
2.4.2 最适温度和温度稳定性
图8显示温度对重组漆酶SDla的影响。以ABTS为底物, 80 ℃时为最适温度, 高于Bacillus licheniformis LS04的最适温度[30]和大多数真菌漆酶[31]。重组漆酶SDla的热稳定性也优于其他芽孢杆菌漆酶[21]。重组漆酶SDla在70 ℃加热1 h后酶活有所提高, 提高至120%以上, 随后逐渐下降, 在6 h达到半衰期。在80 ℃和90 ℃, 酶活变化趋势类似, 随着加热时间的延长, 酶活逐渐降低, 在3 h内达到半衰期。重组漆酶SDla在高温中加热1 h并不会失活, 但不能在高温下长时间存在。
3 结论
收起
本研究成功构建了重组细菌漆酶表达系统, 并初步证明了该酶对磺胺嘧啶的降解能力。实验结果表明, 细菌漆酶在优化的表达条件下表现出较强的酶活性和稳定性, 特别是在高温和酸性环境中, 具备良好的耐热性能, 降解磺胺嘧啶能力更优。这些发现为细菌漆酶在环境污染治理, 尤其是抗生素降解领域的潜在应用提供了理论支持。尽管研究已取得初步进展, 但为了推动其在工业化应用中的可行性, 未来的工作应聚焦于酶的进一步优化和适应性研究, 如探讨金属离子、化学试剂对酶活性及稳定性的影响, 以及反应动力学的深入分析。这些研究将为细菌漆酶在工业环境中的大规模应用奠定坚实基础。
基金
收起
  • 湖南省自然科学基金项目(2022JJ30299)
  • 湖南省自然科学基金项目(2022JJ30290)
文献
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doi: 10.19812/j.cnki.jfsq11-5956/ts.20250110008
  • 接收时间：2025-01-10
  • 首发时间：2025-07-19
  • 出版时间：2025-03-25
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  • 收稿日期：2025-01-10
基金
湖南省自然科学基金项目(2022JJ30299)
湖南省自然科学基金项目(2022JJ30290)
作者信息
    1.湖南农业大学食品科学技术学院, 长沙 410128
    2.湖南农业大学园艺学院, 长沙 410128

通讯作者:

* 夏菠(1980—), 男, 副教授, 博士, 主要研究方向为生物转化与生物降解。E-mail:
刘霞(1976—), 女, 教授, 博士, 主要研究方向为食品质量与安全。E-mail:
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genus		 种数
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species		 占总种数比例
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Genus		 种数
Number of
species		 占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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