Muscle Proteins

Boland, Michael J.; Kaur, Lovedeep; Chian, Feng Ming; Astruc, Thierry

doi:10.1016/b978-0-08-100596-5.21602-8

Cited by 21 publications

(18 citation statements)

References 161 publications

(173 reference statements)

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“…In contrast to terrestrial animals, fish have shorter muscle fibers and less connective tissue, and these muscles are segmented into myotomes by fine connective tissue layers called myocommata or myosepta, which lie primarily in thin sheets that separate muscle fibers into orderly layers [ 15 , 16 ]. In addition, muscle fiber in fish is categorized into three main types of muscle, namely a major white muscle, a superficial red muscle, and an intermediate pink muscle; the axial muscle consists mainly of fast white fibers, covered by a thin layer of slow-red muscle fibers at the periphery, with a layer of pink intermediate muscle fibers in between them ( Figure 1 , [ 17 ]).…”

Section: Characteristics Of Fish Muscle Proteinmentioning

confidence: 99%

Muscle Protein Hydrolysates and Amino Acid Composition in Fish

2021

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Fish muscle, which accounts for 15%–25% of the total protein in fish, is a desirable protein source. Their hydrolysate is in high demand nutritionally as a functional food and thus has high potential added value. The hydrolysate contains physiologically active amino acids and various essential nutrients, the contents of which depend on the source of protein, protease, hydrolysis method, hydrolysis conditions, and degree of hydrolysis. Therefore, it can be utilized for various industrial applications including use in nutraceuticals and pharmaceuticals to help improve the health of humans. This review discusses muscle protein hydrolysates generated from the muscles of various fish species, as well as their amino acid composition, and highlights their functional properties and bioactivity. In addition, the role of the amino acid profile in regulating the biological and physiological activities, nutrition, and bitter taste of hydrolysates is discussed.

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Section: Characteristics Of Fish Muscle Proteinmentioning

confidence: 99%

Muscle Protein Hydrolysates and Amino Acid Composition in Fish

2021

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“…During 62 min of in vitro oral–gastric digestion, some differences in the intensities of the protein bands were observed. After 32 min of simulated oral–gastric digestion, the band intensities of the myosin heavy chain (MHC, 220 kDa) and C-protein (140 kDa) of the digest of the PEF-treated SV-cooked muscles were lighter than the digest of the control SV-cooked muscles, indicating more breakdown of these proteins in the former [ 19 , 20 ]. In addition, the intensity of the band with molecular weight 36 kDa of the digest of PEF-treated SV-cooked muscles was higher than the control untreated SV-cooked meat digest.…”

Section: Resultsmentioning

confidence: 99%

“…L9 and L11 represent PEF-treated SV-cooked samples at 122 and 182 min of oral–gastric–small intestinal digestion, respectively. The protein bands were identified on the electrophoretogram as described by Kaur et al [ 19 , 24 ] and Boland et al [ 20 ]. MHC stands for myosin heavy chain.…”

Section: Figurementioning

confidence: 99%

Effects of Pulsed Electric Field Processing and Sous Vide Cooking on Muscle Structure and In Vitro Protein Digestibility of Beef Brisket

Chian

Kaur

Oey

et al. 2021

Foods

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Pulsed electric fields (PEF) in conjunction with sous vide (SV) cooking has been explored for meat tenderisation. The aim of this experiment was to study the effect of PEF–SV treatment on the muscle structure and in vitro protein digestibility of beef brisket. Pulsed electric field treatment (specific energy of 99 ± 5 kJ/kg) was applied to bovine Deep and Superficial pectoral muscles in combination with sous vide (SV) cooking (60 °C for 24 h). A similar micro- and ultrastructure was detected between the control SV-cooked and PEF-treated SV-cooked pectoral muscles. The combined PEF–SV treatment increased the in vitro protein digestibility of the pectoral muscles by approximately 29%, in terms of ninhydrin-reactive free amino nitrogen released at the end of simulated digestion. An increment in proteolysis of the PEF-treated SV-cooked meat proteins (e.g., myosin heavy chains and C-protein) during simulated digestion was also observed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. More damaged muscle micro- and ultrastructure was detected in PEF-treated SV-cooked muscles at the end of in vitro digestion, showing its enhanced digestive proteolysis compared to the control cooked meat.

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“…Calpastatin, the endogenous inhibitor for both μ-calpain and m-calpain, has been correlated with tenderisation both across and within species (Boland et al, 2019;Chéret et al, 2007).…”

Section: Calpainsmentioning

confidence: 99%

“…Cathepsins are acidic lysosomal proteins and they must be released from the lysosomes to participate in post-mortem proteolysis of myofibrils (Bowker et al, 2010;Kemp et al, 2010). Cathepsin B, D, H, and L are the most abundant in muscle fibres and they have been claimed to be involved in the degradation of proteins during post-mortem aging (Boland et al, 2019;Bowker et al, 2010). Chéret et al (2007) showed that, in meat, both calpains and cathepsins act synergistically while an earlier study by Hopkins and Thompson (2001) reported that the inhibition of cathepsins B and L was not found to have any effect on meat tenderness.…”

Section: Cathepsinsmentioning

confidence: 99%

Endogenous Proteolytic Systems and Meat Tenderness: Influence of Post-Mortem Storage and Processing

Kaur¹,

Hui²,

Morton³

et al. 2021

Food Sci Anim Resour

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Meat proteolytic systems play a crucial role in meat tenderisation. Understanding the effects of processing technologies and post-mortem storage conditions on these systems is important due to their crucial role in determining the quality characteristics of meat and meat products. It has recently been proposed that tenderisation occurs due to the synergistic action of numerous endogenous proteolytic systems. There is strong evidence suggesting the importance of μcalpain during the initial post-mortem aging phase, while m-calpain may have a role during long-term aging. The caspase proteolytic system is also a candidate for cell degradation in the initial stages of conversion of muscle to meat. The role of cathepsins, which are found in the lysosomes, in post-mortem aging is controversial. Lysosomes need to be ruptured, through aging, or other forms of processing to release cathepsins into the cytosol for participation in proteolysis. A combination of optimum storage conditions along with suitable processing may accelerate protease activity within meat, which can potentially lead to improved meat tenderness. Processing technologies such as high pressure, ultrasound, and shockwave processing have been reported to disrupt muscle structure, which can facilitate proteolysis and potentially enhance the aging process. This paper reviews the recent literature on the impacts of processing technologies along with post-mortem storage conditions on the activities of endogenous proteases in meat. The information provided in the review may be helpful in selecting optimum post-mortem meat storage and processing conditions to achieve improved muscle tenderness within shorter aging and cooking times.

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Muscle Proteins

Cited by 21 publications

References 161 publications

Muscle Protein Hydrolysates and Amino Acid Composition in Fish

Muscle Protein Hydrolysates and Amino Acid Composition in Fish

Effects of Pulsed Electric Field Processing and Sous Vide Cooking on Muscle Structure and In Vitro Protein Digestibility of Beef Brisket

Endogenous Proteolytic Systems and Meat Tenderness: Influence of Post-Mortem Storage and Processing

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