Comparative proteomics of goat milk during heated processing

Chen, Di; Li, Xiangying; Zhao, Xuan; Qin, Yusi; Jian‐min, Wang; Wang, Cunfang

doi:10.1016/j.foodchem.2018.09.129

Cited by 51 publications

(34 citation statements)

References 32 publications

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“…All milk samples were centrifuged at 4°C and 1,365 × g for 20 min to remove fat, then were adjusted to pH levels of 6.5, 6.9, 7.3, and 7.7 with 10% acetic acid or l mol/L sodium hydroxide solution as necessary. These milk samples were heated at 65, 85, 105, and 125°C for 15 s, respectively, and served as the treated groups, referring to the study of Chen et al (2019a). As Figure 1 shows, the fresh goat milk samples were used as the control group (CG).…”

Section: Sample Collection and Preparationmentioning

confidence: 99%

“…Goat milk is widely used in dairy products because it is highly digestible, is hypoallergenic, and has high nutritional value (Lou et al, 2018;Chen et al, 2019a). The lower content of α S1 -casein and lactose in goat milk might allow β-LG and lactose to have better digestion and be less allergenic than cow milk (Bevilacqua et al, 2001;Lara-Villoslada et al, 2004;Chen et al, 2018a).…”

Section: Introductionmentioning

confidence: 99%

“…Milk protein is the most important nutritional component in goat milk, and is a good standard for evaluating and testing the nutritional quality of dairy products (García et al, 2014;Chen et al, 2018a;Zhu et al, 2018). The protein in goat milk is composed of 70% water-insoluble casein, 25% water-soluble whey protein, and 5% fat-soluble milk fat globule membrane protein (Chen et al, 2019a). In the processing and production of dairy products, the proteins in milk are prone to flocculation and precipitation, which has a serious effect on the quality of goat milk products.…”

Section: Introductionmentioning

confidence: 99%

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Change in the structural and functional properties of goat milk protein due to pH and heat

Cheng

et al. 2020

Journal of Dairy Science

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This study was carried out to investigate the effects of pH and heat on the structure and function of milk proteins by comparing goat milk treated under different pH and temperature conditions. The results showed that pH had a significant effect on the thermal stability of goat milk proteins, and the proteins were least thermally stable at pH 7.7. Except for the pH 6.9 goat milk, the surface hydrophobicities of the milk proteins at various pH values reached their maxima at 85°C. The particle size, zeta potential, and content of regular secondary structure also decreased significantly at 85°C, and the turbidity of milk proteins under alkaline pH conditions was lower than that under acidic conditions. It was concluded that alkaline conditions resulted in better emulsion stability and oil-holding capacity, and acidic conditions offered better foaming ability, foam stability, and water-holding capacity for goat milk protein during heat processing. It can also be seen that 85°C was the key temperature for milk proteins after changing the pH of the milk. This paper provides a theoretical basis for optimizing the processing conditions for goat milk and the applications of goat milk proteins.

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Section: Sample Collection and Preparationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Change in the structural and functional properties of goat milk protein due to pH and heat

Cheng

et al. 2020

Journal of Dairy Science

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“…Rich nutrients are presented in goat milk, including protein, fat, lactose, vitamins, and minerals, of which protein is a key component. Goat milk proteins consist of 70% casein, 25% whey protein, and 5% milk fat globule membrane protein (Chen et al, 2019). Although the proportion of whey protein is not the highest, it is known to have a wide range of biological activities.…”

Section: Introductionmentioning

confidence: 99%

Proteomic analysis of whey proteins in the colostrum and mature milk of Xinong Saanen goats

Sun

Wang

Sun

et al. 2020

Journal of Dairy Science

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Xinong Saanen goats are among the major dairy goats in China, and their milk is one of the major milk supplies for the Chinese dairy industry. To explore the whey proteome of Xinong Saanen goat milk, we analyzed the whey proteins of goat colostrum and mature milk using proteomic techniques. We identified a total of 314 and 524 proteins in goat colostrum and mature milk, respectively. Our data showed the first 3 functional categories of signal, disulfide bond, and secreted in both milk types. The most abundant Gene Ontology annotations in both milks were the biological process of positive regulation of extracellular regulated protein kinases (ERK)1 and ERK2 cascade; the cellular component of extracellular exosome; and the molecular function of calcium ion binding. Goat colostrum whey proteins showed more disease-related pathways, and mature milk showed more pathways associated with metabolism. Moreover, we observed several pathways involved in intestinal mucosal immunity only in colostrum. Protein-protein interaction network and module analysis revealed that complement and coagulation cascades and Staphylococcus aureus infection were significant in the whey proteins of both milks, and carbon metabolism was more common for mature milk than for colostrum. These findings could provide useful information for the use of goat milk whey proteins in the Chinese dairy industry.

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“…Although several goat's milk proteome studies have been performed for different purposes [15,26,27], our study is the first that attempts to establish an optimized extraction method suited for the 2DE-based proteomic analysis of whole goat's milk proteins. The protein structures of goat's milk are known to be similar to cow's milk, where its solid phase is composed of caseins that are bound together into micelles by calcium phosphate and traces of citrate, potassium, sodium, and magnesium, as well as a soluble phase that is made up of whey proteins [28].…”

Section: Introductionmentioning

confidence: 99%

Optimization of Protein Extraction Method for 2DE Proteomics of Goat’s Milk

et al. 2020

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Two-dimensional electrophoretic (2DE)-based proteomics remains a powerful tool for allergenomic analysis of goat’s milk but requires effective extraction of proteins to accurately profile the overall causative allergens. However, there are several current issues with goat’s milk allergenomic analysis, and among these are the absence of established standardized extraction method for goat’s milk proteomes and the complexity of goat’s milk matrix that may hamper the efficacy of protein extraction. This study aimed to evaluate the efficacies of three different protein extraction methods, qualitatively and quantitatively, for the 2DE-proteomics, using milk from two commercial dairy goats in Malaysia, Saanen, and Jamnapari. Goat’s milk samples from both breeds were extracted by using three different methods: a milk dilution in urea/thiourea based buffer (Method A), a triphasic separation protocol in methanol/chloroform solution (Method B), and a dilution in sulfite-based buffer (Method C). The efficacies of the extraction methods were assessed further by performing the protein concentration assay and 1D and 2D SDS-PAGE profiling, as well as identifying proteins by MALDI-TOF/TOF MS/MS. The results showed that method A recovered the highest amount of proteins (72.68% for Saanen and 71.25% for Jamnapari) and produced the highest number of protein spots (199 ± 16.1 and 267 ± 10.6 total spots for Saanen and Jamnapari, respectively) with superior gel resolution and minimal streaking. Six milk protein spots from both breeds were identified based on the positive peptide mass fingerprinting matches with ruminant milk proteins from public databases, using the Mascot software. These results attest to the fitness of the optimized protein extraction protocol, method A, for 2DE proteomic and future allergenomic analysis of the goat’s milk.

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Comparative proteomics of goat milk during heated processing

Cited by 51 publications

References 32 publications

Change in the structural and functional properties of goat milk protein due to pH and heat

Change in the structural and functional properties of goat milk protein due to pH and heat

Proteomic analysis of whey proteins in the colostrum and mature milk of Xinong Saanen goats

Optimization of Protein Extraction Method for 2DE Proteomics of Goat’s Milk

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