Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Guanhao BU"'
Publikováno v:
Grain & Oil Science and Technology, Vol 7, Iss 3, Pp 159-167 (2024)
Soybean protein has high nutritional value, but its functional properties are easily affected by external factors, which limits its application in food industry. In the study, soybean protein isolate (SPI) was modified by dry heat glycation of galact
Externí odkaz:
https://doaj.org/article/a158aa60c1d7473f89b8e8414b7ef338
Autor:
Zihui LI, Xiaojie DUAN, Kunlun LIU, Guanhao BU, Liang WANG, Shuntang ZHANG, Jinfeng JING, Wei REN
Publikováno v:
Shipin gongye ke-ji, Vol 44, Iss 15, Pp 184-192 (2023)
In order to enhance the flavor of hydrolysate from the mixture of chicken skeleton and chicken breast, the hydrolysis of chicken skeleton and chicken breast composite substrate was carried out by biological enzymatic hydrolysis technology. The enzyma
Externí odkaz:
https://doaj.org/article/c82c33b5b0c540659e35024e46a96bac
Publikováno v:
CyTA - Journal of Food, Vol 18, Iss 1, Pp 409-416 (2020)
Peanut protein isolate was hydrolyzed by trypsin. The resulting peanut peptide fractions (PPF) were then divided into three molecular weight components by ultrafiltration (PPF1, MW >5 kDa; PPF2, 3 kDa < MW
Externí odkaz:
https://doaj.org/article/f0727267f0034b3fa280ea89c34ff5bf
Publikováno v:
Food Chemistry. 422:136085
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::754a5041af60e6cdb131e00656c4b696
https://doi.org/10.1016/j.foodchem.2023.136085
https://doi.org/10.1016/j.foodchem.2023.136085
Autor:
Guanhao Bu, Tanghao Li
Publikováno v:
Journal of the Science of Food and Agriculture. 102:4025-4034
High hydrostatic pressure (HHP) treatment has been used to alleviate the allergenicity of soybeans, but there are little data about the potential antigenicity of β-conglycinin after HHP treatment.We examined the effects of HHP treatment on the antig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a6fbe105fbc93ed165c6fcdf44a75e9
https://doi.org/10.1002/jsfa.11751
https://doi.org/10.1002/jsfa.11751
Publikováno v:
Journal of Food Engineering. 345:111411
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3472b2e7af595dc1005471f47746d61
https://doi.org/10.1016/j.jfoodeng.2023.111411
https://doi.org/10.1016/j.jfoodeng.2023.111411
Autor:
Zhenya Du, Fusheng Chen, Kunlun Liu, Shaojuan Lai, Lifen Zhang, Guanhao Bu, Xueli Gao, Shaobo Liu
Publikováno v:
Journal of Chemistry, Vol 2016 (2016)
Five different extruded soy protein isolates (ESPIs) were obtained by extrusion and denoted by IVD1, IVD2, IVD3, IVD4, and IVD5. Then the SDS-PAGE results showed that the subunits of SPI decreased after extrusion, especially the subunits of 90.8, 32.
Externí odkaz:
https://doaj.org/article/ff1fc0d0353b47019f92da15e26954e0
Publikováno v:
European Food Research and Technology. 246:1065-1072
Soybean protein is considered as a main food allergen. This study illustrates the effects of a combination of high hydrostatic pressure (HHP) with heat treatment on soybean protein allergen. The main allergic protein β-conglycinin was isolated from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a595de2a2121b0f2a0d5cec400927acb
https://doi.org/10.1007/s00217-020-03472-5
https://doi.org/10.1007/s00217-020-03472-5
Publikováno v:
International journal of biological macromolecules. 154
β-conglycinin is one of the major allergens in soybean protein. The purpose of this study was to predict and to identify the major linear epitopes of the β subunit of β-conglycinin. Potential linear epitopes were predicted and confirmed by three i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::158afd1b54821c194bbf089cf9e68ceb
https://pubmed.ncbi.nlm.nih.gov/32198043
https://pubmed.ncbi.nlm.nih.gov/32198043
Publikováno v:
Food Chemistry. 346:128962
In this study, the effects of heat treatment on antigenicity, antigen epitopes, and structural changes in β-conglycinin were investigated. Results showed that the IgG (Immunoglobulin G) binding capacity of heated protein was inhibited with increased
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::100a2747af19caf6538eca1a6e2cb398
https://doi.org/10.1016/j.foodchem.2020.128962
https://doi.org/10.1016/j.foodchem.2020.128962