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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1177/1082013218779239
|2 doi
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|a pubmed25n0951.xml
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|a (DE-627)NLM285556045
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|a (NLM)29911412
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|a DE-627
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|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Wang, Lei
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Protein structural development of threadfin bream ( Nemipterus spp.) surimi gels induced by glucose oxidase
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| 264 |
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 07.01.2019
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|a Date Revised 07.01.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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
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|a Journal Article
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|a Glucose oxidase
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|a Raman spectroscopy
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|a chemical interactions
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|a gel properties
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|a Cross-Linking Reagents
|2 NLM
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|a Disulfides
|2 NLM
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|a Fish Proteins
|2 NLM
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|a Gels
|2 NLM
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|a Sulfhydryl Compounds
|2 NLM
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|a Actomyosin
|2 NLM
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| 650 |
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|a 9013-26-7
|2 NLM
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|a Glucose Oxidase
|2 NLM
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| 650 |
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|a EC 1.1.3.4
|2 NLM
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| 650 |
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|a Glucose
|2 NLM
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| 650 |
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|a IY9XDZ35W2
|2 NLM
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| 700 |
1 |
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|a Fan, Daming
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Fu, Lulu
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Jiao, Xidong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Huang, Jianlian
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhao, Jianxin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Yan, Bowen
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhou, Wenguo
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Wenhai
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ye, Weijian
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Hao
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Food science and technology international = Ciencia y tecnologia de los alimentos internacional
|d 1998
|g 24(2018), 7 vom: 08. Okt., Seite 598-606
|w (DE-627)NLM098247832
|x 1532-1738
|7 nnns
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| 773 |
1 |
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|g volume:24
|g year:2018
|g number:7
|g day:08
|g month:10
|g pages:598-606
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| 856 |
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|u http://dx.doi.org/10.1177/1082013218779239
|3 Volltext
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