1999
DOI: 10.1111/j.1745-4514.1999.tb00036.x
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DIGESTION OF MYOFIBRILLAR AND SARCOPLASMIC FRACTIONS FROM MENHADEN MUSCLE BY THE ACTION OF MENHADEN (Brevoortia spp.) AND WHITE CROAKER (Micropogonias furnieri) TRYPSINS

Abstract: Trypsins from the pyloric caeca of menhaden (Brevoortia spp.) and croaker (Micropogonias furnieri) were used for hydrolysis of both myofibrillar and sarcoplasmic fractions from menhaden muscle. Digestion of muscle proteins was carried out at 37C for 20 min with the pH maintained at either 3, 4, 5, 6, 7, 8 or 9; or for 60 min at the pH's of 5, 7, 8 or 9 at 30C and 37C. The hydrolytic action was evaluated based on the concentration of peptides solubilized. Solubility after digestion of myofibrillar, sarcoplasmic… Show more

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Cited by 8 publications
(2 citation statements)
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“…High variability may be due to differences in protein, peptide, and amino acid profiles of the individual pieces of seafood muscle tissue, that were each purchased on separate days from a variety of Montreal markets. The proteins to which MeHg is bound within the muscle tissue, as well as the sub-cellular fraction in which MeHg ends up within the seafood protein matrix might explain these differences (Pavlisko and Coppes, 1999; He and Wang 2011). Methylmercury bound to soluble proteins may be more easily solubilized into digestive fluids since these proteins are more accessible to digestive proteases compared to myofibrillar proteins (Pavlisko and Coppes, 1999), thus seafood with a higher soluble protein content may release MeHg more readily into digestive fluids and result in higher bioaccessibility of MeHg.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…High variability may be due to differences in protein, peptide, and amino acid profiles of the individual pieces of seafood muscle tissue, that were each purchased on separate days from a variety of Montreal markets. The proteins to which MeHg is bound within the muscle tissue, as well as the sub-cellular fraction in which MeHg ends up within the seafood protein matrix might explain these differences (Pavlisko and Coppes, 1999; He and Wang 2011). Methylmercury bound to soluble proteins may be more easily solubilized into digestive fluids since these proteins are more accessible to digestive proteases compared to myofibrillar proteins (Pavlisko and Coppes, 1999), thus seafood with a higher soluble protein content may release MeHg more readily into digestive fluids and result in higher bioaccessibility of MeHg.…”
Section: Discussionmentioning
confidence: 99%
“…The proteins to which MeHg is bound within the muscle tissue, as well as the sub-cellular fraction in which MeHg ends up within the seafood protein matrix might explain these differences (Pavlisko and Coppes, 1999; He and Wang 2011). Methylmercury bound to soluble proteins may be more easily solubilized into digestive fluids since these proteins are more accessible to digestive proteases compared to myofibrillar proteins (Pavlisko and Coppes, 1999), thus seafood with a higher soluble protein content may release MeHg more readily into digestive fluids and result in higher bioaccessibility of MeHg. Here we documented enzymatic digestion of fresh tuna protein, and found that by the end of the three-hour in vitro gastrointestinal digestion, 100% of the initial protein from raw seafood muscle tissue was broken down.…”
Section: Discussionmentioning
confidence: 99%