In vitro protein digestion of pork cuts differ with muscle type

Zou, Xiaoyu; Zhou, Guanghong; Yu, Xiaobo; Bai, Yun; Wang, Chong; Xu, Xinglian; Dai, Chen; Li, Chunbao

doi:10.1016/j.foodres.2017.12.070

Cited by 29 publications

(16 citation statements)

References 28 publications

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“…Before digestion (untreated samples), a reduction in band intensity of several protein bands was observed in cooked pork as the storage time of raw meat increased, indicating fragmentation and breakdown of meat proteins. This result was in agreement with our previous study (15). The appearance of the 30 kDa component (Troponin-T fragment) has been considered In pepsin treated samples, a substantial decrease in band intensity was observed for some large-molecular-weight protein bands (Figure 3), which could be due to degradation of proteins into smaller peptides or free amino acids.…”

Section: Sds-page Of Proteins In Cooked Meat and Their Digested Productssupporting

confidence: 93%

“…Similar phenomena have been observed in different pork cuts and pork products (14,24). However, SDS-PAGE could not separate smaller peptides well that were characterized by nano LC-MS/MS (15).…”

Section: Sds-page Of Proteins In Cooked Meat and Their Digested Productssupporting

confidence: 80%

“…The protein digestibility of cooked meat from 0, 1, 2 to 3 d samples was assessed as described by Zou et al ( 15 ). Briefly, meat pieces were packed in plastic bags and cooked in a 72°C water bath until the core temperature reached 70°C.…”

Section: Methodsmentioning

confidence: 99%

“…All peptides matched to myofibrillar proteins were listed in Table 1. Previous studies have shown that actin, myosin-1, myosin-4, myosin-7, and many glycolytic enzymes are highly abundant proteins in pork muscle (15,25). These proteins are involved in muscle contraction and energy production.…”

Section: Digested Products From Myofibrillar Proteins In Pork Evolvedmentioning

confidence: 99%

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Structural Changes and Evolution of Peptides During Chill Storage of Pork

Zou

Zhao

et al. 2020

Front. Nutr.

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In this work, we investigated changes in protein structures in vacuum-packed pork during chill storage and its impact on the in vitro protein digestion. Longissimus dorsi muscles were vacuum packed and stored at 4 • C for 3 days. Samples were subjected to Raman spectroscopy, in vitro digestion and nano LC-MS/MS. The 3 d samples had lower α-helix content, but higher β-sheet, β-turn, and random coil contents than the 0 d samples (P < 0.05). SDS-PAGE revealed significant protein degradation in the 3 d samples and the differences in digested products across the storage time. Proteome analysis indicated that the 3 d samples had the higher susceptibility to digestion. Increasing protein digestibility was mainly attributed to the degradation of myofibrillar proteins. Thus, exposure of more enzymatic sites in loose protein structure during chill storage could increase protein degradation in meat.

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Section: Sds-page Of Proteins In Cooked Meat and Their Digested Productssupporting

confidence: 93%

Section: Sds-page Of Proteins In Cooked Meat and Their Digested Productssupporting

confidence: 80%

Section: Methodsmentioning

confidence: 99%

Section: Digested Products From Myofibrillar Proteins In Pork Evolvedmentioning

confidence: 99%

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Structural Changes and Evolution of Peptides During Chill Storage of Pork

Zou

Zhao

et al. 2020

Front. Nutr.

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“…Based on the PSMs, there were 39 proteins with an abundance of more than 0.5%, including the major proteins in myofibrillar and connective tissue, such as myosin, actin, actinin, troponin, nebulin, myomesin, filamin C, and plectin, as well as kinds of enzymes in the sarcoplasm, such as alpha‐1,4 glucan phosphorylase, alpha‐glucanotransferase, beta‐enolase, calcium‐transporting ATPase, carbonic anhydrase 3, creatine kinase M‐type, fructose‐bisphosphate aldolase, glyceraldehyde‐3‐phosphate dehydrogenase, enolase, phosphoglucomutase‐1, phosphoglycerate kinase 1, pyruvate kinase, and triosephosphate isomerase. These high‐abundance proteins were similar to those in previous pork proteomics studies (Di Luccia et al, ; Mi, Li, et al, ; Zou et al, ).…”

Section: Resultssupporting

confidence: 88%

In‐depth mapping of the proteome of Tibetan pig tenderloin ( longissimus dorsi ) using offline high‐pH reversed‐phase fractionation and LC‐MS/MS

Gao

Luo

et al. 2019

J Food Biochem

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In recent years, Tibetan pig breeding and meat processing have developed rapidly. However, the basic physiological and biochemical characteristics of Tibetan pork have not been systematically explored. The present study conducted a high‐throughput analysis of the tenderloin (longissimus dorsi) proteome of the Tibetan pigs and performed a functional annotation and bioinformatics analysis of the identified proteins. Based on offline two‐dimensional liquid chromatography fractionation and MS/MS identification, a total of 1,723 proteins were identified in the tenderloin of Tibetan pigs. Gene ontology analysis and pathway enrichment analysis revealed that the proteins involved in respiration (oxidative phosphorylation, glycolysis/gluconeogenesis, citric acid cycle, and pyruvate metabolism) and protein synthesis and metabolism (proteasome, amino acid biosynthesis, endoplasmic reticulum protein processing, and ribosomes) were significantly enriched, indicating that the energy production and protein metabolism are the most important physiological processes in Tibetan pig tenderloin. Practical applicationsThe in‐depth mapping of the tenderloin (longissimus dorsi) proteome of the Tibetan pigs gives a panoramic perspective at the protein molecular level and provides important information on the mechanisms of postmortem muscle physiology and meat quality formation. Furthermore, the development of Tibetan pork storage and processing technologies would also benefit from the characterization of the biochemical properties of Tibetan pork.

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