General composition and protein surface hydrophobicity of goat, sheep and cow milk in the region of Mount Ida

Yüksel, Zerrin; Avcı, Elif; Uymaz, B.; Erdem, Yaşar Kemal

doi:10.1016/j.smallrumres.2012.03.022

Cited by 20 publications

(17 citation statements)

References 7 publications

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“…The slope of cow milk samples was found to be highest whereas sheep milk samples had the lowest value. The differences in the ANS titration curve slopes within different origins were in accordance with Yuksel et al (2012). The differences between kinetic parameters that were calculated for cow, goat, sheep, and buffalo milks based upon ANS titration curves are shown in Fig.…”

Section: General Compositionsupporting

confidence: 74%

A tool for explaining the differences on renneting characteristics of milks from different origins: the surface hydrophobicity approach

Yıldırım

Erdem

2015

Dairy Sci. & Technol.

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International audienceAbstractThe differences between renneting characteristics of raw milk samples from different origins (bovine, ovine, caprine, buffalo) were investigated by protein surface hydrophobicity approach. 8-Anilinonaphthalene-1-sulfonic acid (ANS) binding method was used to evaluate surface hydrophobicity of raw milk samples and rennet precipitates. The following surface hydrophobicity parameters were calculated: number of surface hydrophobic sites (Fmax), dissociation constant of the fluorescent ANS–protein complex (Kd), binding affinity of ANS to protein surface (1/Kd), the average tightness of binding of ANS to the protein (Fmax/Kd), turnover number (kcat), and protein surface hydrophobicity index (PSHI). The number of hydrophobic sites on the protein surface was found to be highest in cow milk, whereas ovine milk samples had the lowest number of hydrophobic sites and binding affinity to ANS. Protein content was not found directly related to the number of surface hydrophobic sites. The binding affinity of the proteins to ANS was greater in buffalo milk. PSHI was found to be the highest for bovine milk and the lowest for ovine milk. Renneting period was interpreted in two phases (enzymatic phase and flocculation phase) for each origin via ANS partition curves of rennet precipitates. Same trends between bovine–ovine and caprine–buffalo milks were observed during renneting. Buffalo milk completed both of two phases and total renneting period significantly earlier than the milks from the other origins. The hydrophobic parameters of proteins were found to play a key role on coagulation properties

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Section: General Compositionsupporting

confidence: 74%

A tool for explaining the differences on renneting characteristics of milks from different origins: the surface hydrophobicity approach

Yıldırım

Erdem

2015

Dairy Sci. & Technol.

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“…Hydrophobic amino acid residues, always hiding inside protein, only exposure to the surface when protein unfolds. Therefore, surface hydrophobicity is widely used to observe the structure changes of protein (Yuksel, Avcı, Uymaz, & Erdem, 2012). As shown in Figure 1c, the S 0 ‐ANS value decreased significantly ( p < .05) with the increasing concentration of EGCG, which indicated that EGCG was beneficial for the increase of hydrophilicity of myofibril protein from yak meat.…”

Section: Resultsmentioning

confidence: 99%

Effect of tea polyphenols on the tenderness of yak meat

Gao

Zeng

2020

J Food Process Preserv

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The effect and action mechanism of tea polyphenols (TP) on the tenderness of yak meat were investigated. With the treatment of TP at the low concentrations, the myofibril fragmentation index (MFI) value of yak meat was increased and its microstructure was obviously changed. By using fluorescence spectroscopy and the determination of surface hydrophobicity, the tertiary structure of myofibrillar protein (MP) showed the obvious changes with the treatment of epigallocatechin gallate (EGCG). In addition, the secondary structure of MP was also obviously changed according to the measurement of circular dichroism (CD) spectrum, while the α‐helix structure of MP decreased and the β‐sheet increased. Furthermore, according to the analysis of molecular docking, EGCG could interact tightly with myofibril protein by hydrogen bonds, and changed its spatial configuration and molecular force. All results suggested that TPs showed the potentially value to improve the tenderness of yak meat in food industry. Practical applications Yak meat is more and more popular by its high nutrition value. But due to its special myofibril protein, the tenderness of yak meat is unfavorably and affects its sensory properties, which may limit its processing and consumption in food industry. In present study, TPs was used to improve the tenderness of yak meat by changing the spatial configuration and molecular force of myofibril protein, which suggested that TPs showed the potential value to enhance the quality of yak meat during its processing in food industry.

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“…The surface hydrophobicity was determined by a spectrofluorometer (Shimadzu RF-5301, Kyoto, Japan) according to the method of Yuksel, Avci, Uymaz, and Erdem (2012), with a little modification. This allowed us to know the extent of exposed surface hydrophobic sites on the micelles.…”

Section: Determining the Surface Hydrophobicity Micellar Calcium Andmentioning

confidence: 99%

The pressure-induced, lactose-dependent changes in the composition and size of casein micelles

et al. 2015

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General composition and protein surface hydrophobicity of goat, sheep and cow milk in the region of Mount Ida

Cited by 20 publications

References 7 publications

A tool for explaining the differences on renneting characteristics of milks from different origins: the surface hydrophobicity approach

A tool for explaining the differences on renneting characteristics of milks from different origins: the surface hydrophobicity approach

Effect of tea polyphenols on the tenderness of yak meat

The pressure-induced, lactose-dependent changes in the composition and size of casein micelles

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