2020
DOI: 10.1007/s12562-020-01444-y
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Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish

Abstract: Fish and marine invertebrates constitute an important part of the human diet worldwide, and their muscles are the major edible parts. The muscles are a rich source of proteins, which in other terms determines the nutritional value and the quality of seafood products. Though the fish skeletal muscle proteins share many similarities with their mammalian counterparts, there exist great differences in their biological activity and structural stability. While the muscles of shellfish or aquatic invertebrates share … Show more

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Cited by 42 publications
(14 citation statements)
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“…It is a sarcoplasmic monomeric globular heme protein, which is varied in the muscle, depending on the fiber type, muscle activity, and age of the animal (Chaijan et al., 2008; Zhao et al., 2021). Generally, fish Mb comprises 143 amino acids, which is lower than the mammalian Mb, and the molecular weight is around 17 kDa (Ochiai & Ozawa, 2020). Mb contains a heme prosthetic group and a large‐coiled polypeptide globin moiety (Figure 1).…”
Section: Color and Pigments Of Fishmentioning
confidence: 99%
“…It is a sarcoplasmic monomeric globular heme protein, which is varied in the muscle, depending on the fiber type, muscle activity, and age of the animal (Chaijan et al., 2008; Zhao et al., 2021). Generally, fish Mb comprises 143 amino acids, which is lower than the mammalian Mb, and the molecular weight is around 17 kDa (Ochiai & Ozawa, 2020). Mb contains a heme prosthetic group and a large‐coiled polypeptide globin moiety (Figure 1).…”
Section: Color and Pigments Of Fishmentioning
confidence: 99%
“…The α–helix decreased from 30.70% to 12.20%, the β–turn increased from 17.70% to 22.40%, and the random coil increased from 32.80% to 54.00%, with an overall trend of a decreasing α–helix and an increasing β–turn and random coil. Because of their bulge structures, the β–turn and random coil easily bind to antibodies to form epitopes, whereas the α–helix is not easily deformed and does not easily bind to antibodies to form epitopes, such as tropomyosin, a coiled–coil protein with an α–helix structure that becomes a major allergen from shellfish [ 36 ]. Furthermore, a high frequency of β–turn and random coil occurrence was found in the entire amino acid sequence of Ana o 2 and Ana o 3, indicating a high possibility of epitope formation in this region.…”
Section: Resultsmentioning
confidence: 99%
“…In fish meat, major proteins are those such as myosin, actin, troponin, tropomyosin and collagen [ 37 ]. It is speculated that the peptide derived by digestion of these proteins of APP may promote muscle fiber hypertrophy in a coordinated manner with the development of intramuscular connective tissue.…”
Section: Discussionmentioning
confidence: 99%