Results 201 to 210 of about 102,497 (280)
Some of the next articles are maybe not open access.
Food Chemistry, 2021
The mechanism by which sodium tripolyphosphate affected the aggregation behavior of ovalbumin-lysozyme complexes was investigated in this work. The highest stability coefficients were detected for natural ovalbumin and lysozyme at pH 9.0 and pH 5.0, with
Haobo Jin, Yongguo Jin, Long Sheng
exaly +2 more sources
The mechanism by which sodium tripolyphosphate affected the aggregation behavior of ovalbumin-lysozyme complexes was investigated in this work. The highest stability coefficients were detected for natural ovalbumin and lysozyme at pH 9.0 and pH 5.0, with
Haobo Jin, Yongguo Jin, Long Sheng
exaly +2 more sources
Food Hydrocolloids, 2020
The aim of this research was to synthesize ovalbumin-pullulan conjugates through the Maillard reaction and compare the molecular characteristics of native ovalbumin (N-OVA), heated ovalbumin (H-OVA) and glycosylated ovalbumin (G-OVA).
Long Sheng, Meihu Ma, Xi Huang
exaly +2 more sources
The aim of this research was to synthesize ovalbumin-pullulan conjugates through the Maillard reaction and compare the molecular characteristics of native ovalbumin (N-OVA), heated ovalbumin (H-OVA) and glycosylated ovalbumin (G-OVA).
Long Sheng, Meihu Ma, Xi Huang
exaly +2 more sources
Food Chemistry, 2023
The mechanism of epigallocatechin gallate (EGCG)-modified ovalbumin gel (EMOG) was investigated. Results indicated that, with the increase of EGCG concentration from 0% to 0.05%, the opacity, hardness, and cohesiveness of EMOG increased significantly ...
Hui Xue +4 more
semanticscholar +1 more source
The mechanism of epigallocatechin gallate (EGCG)-modified ovalbumin gel (EMOG) was investigated. Results indicated that, with the increase of EGCG concentration from 0% to 0.05%, the opacity, hardness, and cohesiveness of EMOG increased significantly ...
Hui Xue +4 more
semanticscholar +1 more source
Food Chemistry, 2021
In this paper, the effects of ultrasonic assisted glycosylation on the gel properties of ovalbumin (OVA) were studied. The molecular characteristics of native ovalbumin, heated ovalbumin, traditional glycosylated ovalbumin, ultrasonic ovalbumin and ...
Long Sheng, Qiao Liu, Wanyi Dong, Z. Cai
semanticscholar +1 more source
In this paper, the effects of ultrasonic assisted glycosylation on the gel properties of ovalbumin (OVA) were studied. The molecular characteristics of native ovalbumin, heated ovalbumin, traditional glycosylated ovalbumin, ultrasonic ovalbumin and ...
Long Sheng, Qiao Liu, Wanyi Dong, Z. Cai
semanticscholar +1 more source
Flavonoids enhance gel strength of ovalbumin: Properties, structures, and interactions.
Food Chemistry, 2022The effect of ovalbumin-flavonoids (naringenin, genistein, naringin, puerarin, and daidzein) interactions on the formation and properties of ovalbumin hydrogels was investigated.
Yejun Zhong +6 more
semanticscholar +1 more source
Food Chemistry, 2021
In this study, the interaction of ovalbumin with lutein dipalmitate and the effect of ovalbumin on marigold lutein esters extracts were investigated. Lutein dipalmitate quenched the fluorescence of ovalbumin by static quenching. Binding and thermodynamic
Xin Qi +6 more
semanticscholar +1 more source
In this study, the interaction of ovalbumin with lutein dipalmitate and the effect of ovalbumin on marigold lutein esters extracts were investigated. Lutein dipalmitate quenched the fluorescence of ovalbumin by static quenching. Binding and thermodynamic
Xin Qi +6 more
semanticscholar +1 more source
Food Hydrocolloids, 2020
Ovalbumin (OVA) is the most abundant protein component present in egg white which has a well-balanced amino acid composition and can be used as an excellent protein source for many food products.
Zheng Zhou
exaly +2 more sources
Ovalbumin (OVA) is the most abundant protein component present in egg white which has a well-balanced amino acid composition and can be used as an excellent protein source for many food products.
Zheng Zhou
exaly +2 more sources
Archives of Biochemistry and Biophysics, 1961
Abstract A study of the carbohydrate component of ovalbumin points to the presence of three moles of d -glucosamine and six moles of d -mannose per 45,000 g. of the protein. Ovalbumin is extensively oxidized by sodium periodate, the primary reaction with the carbohydrate moiety cleaving three residues of d -mannose and one residue of d ...
Y C, LEE, R, MONTGOMERY
openaire +2 more sources
Abstract A study of the carbohydrate component of ovalbumin points to the presence of three moles of d -glucosamine and six moles of d -mannose per 45,000 g. of the protein. Ovalbumin is extensively oxidized by sodium periodate, the primary reaction with the carbohydrate moiety cleaving three residues of d -mannose and one residue of d ...
Y C, LEE, R, MONTGOMERY
openaire +2 more sources