Zeus, Aesculapius, Amalthea and the proteome of goat milk

Cunsolo, Vincenzo; Fasoli, Elisa; Saletti, Rosaria; Muccilli, Vera; Gallina, Serafina; Righetti, Pier Giorgio; Foti, Salvatore

doi:10.1016/j.jprot.2015.07.009

Cited by 32 publications

(30 citation statements)

References 39 publications

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“…Among the studied animals, several N‐glycosylated proteins were newly identified in milk, which have not been reported in previous studies . For example, tolloid‐like protein 1 was only identified in goat milk, endoplasmic reticulum aminopeptidase 2 in yak milk, WAP four‐disulfide core domain protein 2 in buffalo milk, and torsin A interacting protein 2 in camel milk.…”

Section: Discussionmentioning

confidence: 67%

“…A recent study of ours reported that most whey proteins from Holstein, buffalo, yak, goat, and camel milk were assigned to biological regulation, response to stress, and localization . More recently, the goat whey proteome was also mapped by nanocapillary LC‐ESI‐MS, and most of the whey proteins were principally involved in metabolic processes, regulation of biological processes, and response to stimulus . Several additional studies also investigated the milk whey proteome from Holstein cows, buffaloes, and goats .…”

Section: Discussionmentioning

confidence: 99%

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N‐glycosylation proteomic characterization and cross‐species comparison of milk whey proteins from dairy animals

et al. 2017

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Glycosylated proteins in milk have been implicated in multiple biological roles. However, the N-glycoprotein components and their complexity in milk whey from dairy animals are not well characterized. Here, a modified proteomics approach consisting of N-glycopeptide enrichment and identification was used to map the N-glycoproteome profile of milk whey from Holstein and Jersey cows, buffaloes, yaks, goats, camels, and horses. A total of 233 N-glycosylation sites, corresponding to 147 N-glycoproteins, were detected in the studied animals. Most of the identified N-glycosylation sites were not characterized in the database and were considered as unknown. Functional analysis of the identified glycoproteins demonstrated that response to stimulus was the most abundant GO category shared in the studied animals according to their annotation. Lysosome, glycosaminoglycan degradation, and extracellular matrix-receptor interaction pathways were shared between Holstein and Jersey cows, and yaks. N-glycoprotein components of milk whey from Holstein and Jersey cows, buffaloes, yaks, and goats were more similar to each other than to those of camels and horses. These results significantly extend the number of known N-glycosylation sites and reveal in-depth composition and potential functions of N-glycoproteins in milk whey, which in turn provides insights to further explore N-glycoprotein biosynthesis in the studied animals.

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Section: Discussionmentioning

confidence: 67%

Section: Discussionmentioning

confidence: 99%

N‐glycosylation proteomic characterization and cross‐species comparison of milk whey proteins from dairy animals

et al. 2017

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“…Proteomic investigation is challenging due to the wide dynamic range of protein expression where the presence of high abundance protein masks or prevents the detection of low abundance proteins. Recently, the most comprehensive proteomic dataset of goat milk has been reported by Cunsolo et al [6]. This group fractionated the total milk samples using combinatorial hexapeptide ligand libraries (CPLL; such as ProteoMiner) at different pH levels to reduce the dynamic range of protein concentrations.…”

Section: Comprehensive Analysismentioning

confidence: 99%

“…They identified 452 unique gene products including many low abundance proteins in goat milk. Their success was also related to the use of further fractionation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), high resolution, nLC-MS/MS, and an advanced bioinformatics platform [6]. New strategies employing multi-enzyme digestion coupled with CID and ETD for protein sequencing and characterization was also used to increase sequence coverage and localization of PTMs [50].…”

Section: Comprehensive Analysismentioning

confidence: 99%

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Proteomic Analysis of Goat Milk

Olumee-Shabon¹,

Boehmer²

2018

Goat Science

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The advancement of electrophoresis and chromatography, along with technological developments in mass spectrometry, has widened the potential application of proteomics to study milk from smaller ruminants. The aim of this chapter is to provide an in-depth overview of the development and progress of proteomics applications in goat milk. After examining various proteomic approaches that are currently applied to this field, we narrow our focus on proteomic investigations of mastitis in goat milk. A summary of protein modulation in goat milk during experimentally-induced endotoxin mastitis is discussed. Because the molecular function of proteins is disrupted during disease due to changes in post-translational modifications, we also review the phosphorylation of caseins, which are the predominant phosphoproteins in milk, and discuss the implications of casein modifications during mastitis. These results offer new insights into the changes of protein expression in goat milk during infection.

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Protein digestion properties of Xinong Saanen goat colostrum and mature milk usingin vitrodigestion model

et al. 2019

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BACKGROUND Xinong Saanen goat milk is a raw material for goat milk‐based infant formula production. This study aims to analyze digestion properties of Xinong Saanen goat colostrum and mature milk by simulating infant gastrointestinal digestion. Zeta potential, particles size, protein profile and peptides composition of these two kinds of milk during the digestion process were studied. RESULTS Zeta‐potential values of the digested colostrum were lower than those of mature milk through the whole digestion. Absolute zeta potential of colostrum duodenal digestion samples showed a decrease from 16.63 ± 2.08 to 11.80 ± 2.03 mV while that of mature milk decreased sharply and then increased (P < 0.05). Colostrum had a larger particle size than mature milk and both milks showed decreased particle size with increasing digestion time but an increase for the last 30 min. Colostrum showed more high molecular weight (MW) proteins which cannot be hydrolyzed completely compared with mature milk. Digested peptides (< 10 kDa) were characterized using liquid chromatography combined with tandem mass spectrometry (LC–MS/MS). The casein‐derived peptides identified in digested colostrum and mature milk accounted for 76.67% and 59.53%, respectively. β‐Casein was the most abundant in colostrum while that in mature milk was αs1‐casein. Enterotoxin‐binding glycoprotein PP20K, butyrophilin subfamily 1 member A1 (BTN1A1) and perilipin (PLIN) were only detected in digested mature milk. CONCLUSION Differences in digestion properties between goat colostrum and mature milk were mainly shown in duodenal digestion phase. Data may provide useful information about utilization of goat milk for infant formula formulation. © 2019 Society of Chemical Industry

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Zeus, Aesculapius, Amalthea and the proteome of goat milk

Cited by 32 publications

References 39 publications

N‐glycosylation proteomic characterization and cross‐species comparison of milk whey proteins from dairy animals

N‐glycosylation proteomic characterization and cross‐species comparison of milk whey proteins from dairy animals

Proteomic Analysis of Goat Milk

Protein digestion properties of Xinong Saanen goat colostrum and mature milk usingin vitrodigestion model

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