Article(id=1297161249922502910, tenantId=1146029695717560320, journalId=1296125381406982186, issueId=1297161216049308076, articleNumber=null, orderNo=null, doi=10.13550/j.jxhg.20250321, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=null, receivedDate=1746547200000, receivedDateStr=2025-05-07, revisedDate=null, revisedDateStr=null, acceptedDate=1749139200000, acceptedDateStr=2025-06-06, onlineDate=1787196942071, onlineDateStr=2026-08-20, pubDate=1778774400000, pubDateStr=2026-05-15, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1787196942071, onlineIssueDateStr=2026-08-20, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1787196942071, creator=13701087609, updateTime=1787196942071, updator=13701087609, issue=Issue{id=1297161216049308076, tenantId=1146029695717560320, journalId=1296125381406982186, year='2026', volume='43', issue='5', pageStart='929', pageEnd='1184', issueExtLink='null', onlineDate='null', pubDate='1778774400000', pubDateStr='2026-05-15', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=1, specialIssue=null, createTime=1787196933996, creator='13701087609', updateTime=1787202244949, updator='13701087609', preIssue=null, nextIssue=null, articleTotal=null, ext={EN=IssueExt(id=1297183491922354645, tenantId=1146029695717560320, journalId=1296125381406982186, issueId=1297161216049308076, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1297183491922354646, tenantId=1146029695717560320, journalId=1296125381406982186, issueId=1297161216049308076, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null, downloadFileDto=null}, startPage=1136, endPage=1145, ext={EN=ArticleExt(id=1297161251696693503, articleId=1297161249922502910, tenantId=1146029695717560320, journalId=1296125381406982186, language=EN, title=Physicochemical characteristics and functional properties of white, red and black quinoa protein isolates, columnId=null, journalTitle=Fine Chemicals, columnName=null, runingTitle=null, highlight=null, articleAbstract=

White quinoa protein isolates (WQPI), red quinoa protein isolates (RQPI) and black quinoa protein isolates (BQPI) were isolated and extracted from white, red and black quinoa, respectively, after degreasing with n-hexane, alkaline dissolution with NaOH and precipitation with hydrochloric acid. The effects of pH (2.0~10.0) and NaCl concentration (0~0.6 mol/L) on the physicochemical properties and functional characteristics of WQPI, RQPI and BQPI were evaluated through polyacrylamide gel electrophoresis, Zeta potential and particle size determination, as well as surface hydrophobicity, protein solubility, water-holding capacity, oil-holding capacity, emulsifying activity, foaming property and gelation property tests. The results showed that the main components of WQPI, RQPI and BQPI were all 11S globulin and 7S globulin cross-linked via acidic subunits and basic subunits through disulfide bonds, but with significant difference in their contents. The average particle size and surface charge of the three proteins were highly dependent on pH, and their surface hydrophobicity significantly decreased as pH increased. The pH far from the isoelectric point (about 5.0) could significantly improve the solubility, emulsification and foaming property of the protein, but reduce the stability of the foam. Under neutral conditions, WQPI and RQPI exhibited better gelation and interfacial properties than BQPI. The influence of NaCl on the solubility, emulsification and foaming properties of proteins was correlated to its concentration. The gelation properties of WQPI and RQPI were significantly better than those of BQPI. The gel structures formed by WQPI and RQPI with a mass concentration of 120 g/L were complete and had good standing properties, while only BQPI with a mass concentration of 180 g/L could form a gel with standing properties.

, authors=Xiaohan GUO¹, Ying XU², Fuzhen ZHOU³, Yaosong WANG^{1, *}, authorsList=Xiaohan GUO, Ying XU, Fuzhen ZHOU, Yaosong WANG, authorCompany=null, correspAuthors=Yaosong WANG, 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=1297161252250341632, articleId=1297161249922502910, tenantId=1146029695717560320, journalId=1296125381406982186, language=CN, title=白、红、黑三色藜麦分离蛋白的物化性质和功能特性, columnId=1297161238627242138, journalTitle=精细化工, columnName=食品与营养化学品, runingTitle=null, highlight=null, articleAbstract=

以白色藜麦、红色藜麦和黑色藜麦为原料，经正己烷脱脂、NaOH碱溶、盐酸酸析出，分别分离提取了白色藜麦分离蛋白（WQPI）、红色藜麦分离蛋白（RQPI）及黑色藜麦分离蛋白（BQPI）。通过聚丙烯酰胺凝胶电泳、Zeta电位和粒径测定以及表面疏水性、蛋白溶解性、持水性、持油性、乳化活性、起泡性和凝胶性测试，考察了pH（2.0~10.0）和NaCl浓度（0~0.6 mol/L）对WQPI、RQPI和BQPI 3种蛋白的物化性质和功能特性的影响。结果表明，WQPI、RQPI和BQPI 3种蛋白主要组分均为由酸性亚基及碱性亚基通过二硫键交联的11S球蛋白和7S球蛋白，但两者含量存在显著差异。3种蛋白平均粒径及带电性强烈依赖于pH，其表面疏水性随着pH的升高而显著降低；远离等电点（约5.0）时的pH均能显著提高蛋白的溶解性、乳化性及起泡性，但降低泡沫稳定性。在中性条件下，WQPI、RQPI比BQPI表现出更好的凝胶性和界面性；NaCl对蛋白的溶解性、乳化性及起泡性的影响依赖于其浓度；WQPI、RQPI的凝胶性明显优于BQPI，质量浓度为120 g/L的WQPI、RQPI所形成的凝胶结构完整且有较好的站立性，而质量浓度为180 g/L的BQPI才能形成具有站立性的凝胶。

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郭笑含（2000—），女，硕士生，E-mail: guoxiaohan@njfu.edu.cn。

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郭笑含（2000—），女，硕士生，E-mail: guoxiaohan@njfu.edu.cn。

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