Protein structural development of threadfin bream ( Nemipterus spp.) surimi gels induced by glucose oxidase

This study investigated the effect of glucose oxidase on the gel properties of threadfin bream surimi. The gel strength of surimi increased with the addition of 0.5‰ glucose oxidase after two-step heating. Based on the results of the chemical interactions, the hydrophobic interaction and disulfide b...

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Détails bibliographiques
Publié dans:Food science and technology international = Ciencia y tecnologia de los alimentos internacional. - 1998. - 24(2018), 7 vom: 08. Okt., Seite 598-606
Auteur principal: Wang, Lei (Auteur)
Autres auteurs: Fan, Daming, Fu, Lulu, Jiao, Xidong, Huang, Jianlian, Zhao, Jianxin, Yan, Bowen, Zhou, Wenguo, Zhang, Wenhai, Ye, Weijian, Zhang, Hao
Format: Article en ligne
Langue:English
Publié: 2018
Accès à la collection:Food science and technology international = Ciencia y tecnologia de los alimentos internacional
Sujets:Journal Article Glucose oxidase Raman spectroscopy chemical interactions gel properties Cross-Linking Reagents Disulfides Fish Proteins Gels Sulfhydryl Compounds plus... Actomyosin 9013-26-7 Glucose Oxidase EC 1.1.3.4 Glucose IY9XDZ35W2
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Résumé:This study investigated the effect of glucose oxidase on the gel properties of threadfin bream surimi. The gel strength of surimi increased with the addition of 0.5‰ glucose oxidase after two-step heating. Based on the results of the chemical interactions, the hydrophobic interaction and disulfide bond of glucose oxidase-treated surimi samples increased compared with the control samples at the gelation temperature and gel modori temperature. The surface hydrophobicity of samples with glucose oxidase and glucose increased significantly ( p < 0.05) and total sulfhydryl groups decreased significantly ( p < 0.05). The analysis of Raman spectroscopy shows that the addition of glucose oxidase induced more α-helixes to turn into a more elongated random and flocculent structure. Glucose oxidase changes the secondary structure of the surimi protein, making more proteins depolarize and stretch and causing actomyosin to accumulate to each other, resulting in the formation of surimi gel
Description:Date Completed 07.01.2019
Date Revised 07.01.2019
published: Print-Electronic
Citation Status MEDLINE
ISSN:1532-1738
DOI:10.1177/1082013218779239