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Investigation into IgG/IgE binding capacity and gut microbiota of digestion products derived from glycated ovalbumin
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作者 Jihua Mao yanhong shao +2 位作者 Hui Wang Jun Liu Zongcai Tu 《Food Science and Human Wellness》 SCIE CAS CSCD 2024年第6期3633-3641,共9页
Gut microbiota plays an important role in food allergy.The immunoglobulin G(IgG)/immunoglobulin E(IgE)binding capacity and human gut microbiota changes of digestion products derived from glycated ovalbumin(OVA)were in... Gut microbiota plays an important role in food allergy.The immunoglobulin G(IgG)/immunoglobulin E(IgE)binding capacity and human gut microbiota changes of digestion products derived from glycated ovalbumin(OVA)were investigated.Gastrointestinal digestion effectively destroyed the primary structure of glycated OVA,resulting in a significantly higher digestibility than gastric digestion,and more abundant peptides<3 kDa.Moreover,gastric and gastrointestinal digestion products have different fluorescence quenching and red shift of fluorescence peaks,and possess different conformational structures.These changes resulted in a decrease in 28.7%of the IgE binding capacity of gastrointestinal digestion products beyond that of pepsin.Moreover,gastrointestinal digestion products of glycated OVA increased significantly the proportion of Subdoligranulum,Collinsella,and Bifidobacterium.Therefore,gastrointestinal digestion products of glycated OVA altered human intestinal microbiota,reducing the risk of potential allergy. 展开更多
关键词 OVALBUMIN Glycation DIGESTION IgG/IgE binding capacity Gut microbiota
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Structure and allergenicity of a-lactalbumin:effects of ultrasonic prior to glycation and subsequent phosphorylation 被引量:1
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作者 Wenmei Chen Qiongzhen Chen +4 位作者 Houze Zhou yanhong shao Yang Wang Jun Liu Zongcai Tu 《Food Science and Human Wellness》 SCIE CSCD 2023年第3期825-831,共7页
Bovineα-lactalbumin(BLA)induced severe cow's milk allergy.In this study,a novel strategy combining ultrasonication,performed before glycation,and phosphorylation was proposed to reduce BLA allergenicity.Result sh... Bovineα-lactalbumin(BLA)induced severe cow's milk allergy.In this study,a novel strategy combining ultrasonication,performed before glycation,and phosphorylation was proposed to reduce BLA allergenicity.Result showed that IgE-and IgG-binding capacities and the release rates of histamine and interleukin-6 from RBL-2 H3 were reduced.Moreover,intrinsic fluorescence intensity and surface hydrophobicity were decreased,whereas glycated sites(R10,N44,K79,K108,N102 and K114)and phosphorylated sites(Y36 and S112)of BLA were increased.Minimum allergenicity was detected during BLA treatment after ultrasonic prior to glycation and subsequent phosphorylation because of considerable increase in glycated and phosphorylated sites.Therefore,the decrease in allergenicity of BLA,the effect correlated well with the shielding effect of glycated sites combined with phosphorylated sites and the conformational changes.This study provides important theoretical foundations for improving and using the ultrasonic technology combined with protein modification in allergenic protein processing. 展开更多
关键词 Bovineα-lactalbumin ALLERGENICITY ULTRASONIC Protein modification
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