• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.126-126
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• 2003

• Korean Journal of Fisheries and Aquatic Sciences
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• v.46 no.6
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• pp.717-724
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• 2013

To characterize the food components of two mussels (wild hard-shelled mussel (HM) Mytilus coruscus, and cultured sea mussel (SM) Mytilus edulis) in Korea, we examined the proximate composition, fatty composition, amino acid/mineral content, texture, collagen content and chemical and taste compounds. Regarding the proximate composition, HM had lower moisture levels and higher crude protein and carbohydrate contents than SM. The amino nitrogen, volatile basic nitrogen and total amino acid contents of HM and SM were 250.6 and 227.3 mg/100 g, 11.2 and 12.0 mg/100 g, and 17,451.1 and 15,334.8 mg/100 g, respectively. The major amino acids were glutamic acid, aspartic acid, glycine, alanine, lysine and arginine. The major fatty acids of HM and SM were 14:0, 16:0, 16:1n-7, 20:5n-3, and 22:6n-3, which did not differ significantly between the two mussels. HM had a higher n-3 polyene ratio, and a lower saturate and monoene ratio than SM. Regarding the taste-active compounds, the free amino acid contents of HM and SM were 1,116.5 and 961.8 mg/100 g, respectively, and the major free amino acids were taurine, glutamic acid, glutamine, glycine, citrulline, lysine and arginine. The primary minerals in both HM and SM were Na, Cl, K and P which did not differ significantly between the two mussels. The soluble and insolube collagen contents of HM and SM were 265.8 and 228.4 mg/100 g, and 119.5 and 121.8 mg/100 g, respectively.

• Korean Journal of Food Science and Technology
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• v.22 no.3
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• pp.234-240
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• 1990

Attempts have been made to optimize the hydrolysis conditions of the oyster and the mussel by the commercial proteolytic enzymes. Raw materials were digested with seven different commercial enzymes, and their quality parameters measured in terms of degree of hydrolysis and content of free amino nitrogen, nucleic acid-related substances. and free amino acids as well as sensory evaluation of optimization of their hydrolysis conditions. As a result, following enzymes have been disclosed as effective for enzymatic digestion: MKC-HT proteolytic, alcalase 0.6L and thermease for the oyster whereas MKC-acid fungal protease and thermoase for the mussel, respectively.

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.419-419
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• 2005

• Proceedings of the KSLP Conference
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• 2015.03a
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• pp.18-18
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• 2015

• Journal of Life Science
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• v.9 no.3
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• pp.276-281
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• 1999

This study was designed as a part of efforts to investigate the biochemical pollutant markers for diagnosis of marine pollutions by changes in oxygen radicals and their scavenger enzymes of the mussel (Mytilus coruscus) in South Sea of Korea. Protein contents in muscle of cultured mussel in South Sea were remarkably lower (4-14%, respectively) than those of wild mussel in Pohang of East Sea. Superoxide radical activities in muscle of cultured in South Sea were significantly higher 82∼138% than those of wild mussel in Pohang. Hydroxyl radical formations in muscle of cultured mussels in South Sea were significantly 9∼25% higher than those of wild mussels in Pohang. Superoxide dismutase (SOD) activities in muscle of cultured mussels in South Sea were significantly 16∼28% lower than those of wild mussels in Pohang. It is believed that significantly decrease of protein contents in muscle, remarkable increases of superoxide radical and hydroxyl radical in muscle of cultured mussels of South Sea may be used as a biochemical pollutant markers for diagnosis of marine pollutions. These results suggest that near-coastal water as well as neritic water of the south sea might be affected by pollutant.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.50 no.6
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• pp.656-661
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• 2017

To develop a highly value-added product from extract from small and damaged sea mussels Mytilus edulis, we prepared two types of sea mussel sauce (MS): bottled (BMS) and retort pouched (RMS). We investigated the processing conditions, quality metrics and flavor compounds in each type of sauce. We found that the most appropriate base formulation for both BMS and RMS consisted of 40.0% SME (Brix $30^{\circ}$), 15.0% sugar, 6.0% salt, 4.0% monosodium glutamate, 4.0% soy sauce, 3.5% starch, 3.0% yeast extract, 3.5% wheat flour and 21.0% water. The crude protein, salinity, volatile basic nitrogen and amino-nitrogen content of the BMS and RMS were 8.7% and 8.8%, 9.3% and 9.2%, 24.9 and 31.4 mg/100 g, and 468.5 and 455.1 mg/100 g, respectively. For comparison, the ranges of these values in commercial oyster sauces (COS) are 4.7-7.5%, 10.7-12.0%, 8.2-12.5 mg/100 g, and 225.7-448.2 mg/100 g, respectively. The total free amino acid content of RMS and Premium COS was 7,215.7 and 6,160.7 mg/100 g, respectively, and the main free amino acids were glutamic acid, taurine, glycine, alanine, arginine, proline and lysine. These results demonstrate that BMS and RMS have favorable organoleptic qualities and good storage stability compared to COS, and are suitable for commercialization as high-flavor seasoning sauces.

• Journal of Adhesion and Interface
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• v.24 no.4
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• pp.113-119
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• 2023

Since it was reported that the unusual amino acid DOPA in synergy with lysine and histidine residues found in mussel adhesive proteins plays a pivotal role in mussel adhesion in underwater environments, there has been a burgeoning development of various catecholamines-based adhesives for biomedical applications. Among these, catechol-conjugated chitosan, containing catecholamine, featuring multiple catechol groups within its aminerich chitosan backbone, has found versatile utility in fields, such as tissue adhesion, wound dressing, tissue healing, hemostats, drug delivery systems, and tissue engineering scaffolds. Significantly, chitosan-catechol is a mussel-inspired material approved by both US Food and Drug Administration (FDA) and KR Ministry of Food and Drug Safety (MFDS) for its effectiveness in hemostasis. This review focuses on 1) general aspects of catechol-conjugated chitosan, highlighting catechol group integration into chitosan backbones, 2) examination of proposed mechanisms of hemostasis, and 3) exploration of diverse physical forms, including solution, hydrogels, patches, and thin films with practical applications inapplicable to hemostasis.

• Ocean Science Journal
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• v.41 no.1
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• pp.43-51
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• 2006

Concentration and distribution of Fe, Zn, Cu, Cd, Mn, Pb, Ni among subcellular fractions (cellular membrane structures and cytosol) and Zn, Cu, Cd among cytoplasmic proteins in the kidney and digestive gland of mussel Modiolus modiolus living along a polymetallic concentration gradient were studied. It was found in the kidney of M. modiolus from contaminated sites that the Fe percent increased in the "membrane" fraction, whereas Zn, Pb, Ni and Mn percent increased in the cytosol compared to the kidney of the control mussel. Note kidney cytosol of M. modiolus from clean and contaminated sites sequestered major parts of Cu and Cd. In the digestive gland of M. modiolus from contaminated sites Fe, Zn, Cd, Mn, Ni percent increased in the "membrane" fraction, whereas Cu, Pb percent increased in the cytosol compared to digestive gland of control mussel. Gel-filtration chromatography shows kidney of M. modiolus contains increased metallothionein-like protein levels irrespective of ambient dissolved metal concentrations. It was shown that the metal detoxification system in the kidney and digestive gland of M. modiolus was efficient under extremely high ambient metal levels. However, under complex environmental contamination in the kidney of M. modiolus, the metal detoxification capacity of metallothionein-like proteins was damaged.

• Molecules and Cells
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• v.26 no.1
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• pp.34-40
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• 2008

To express an increased level of recombinant Mefp1 (marine mussel adhesive protein) in soluble form, we constructed expression vectors encoding truncated OmpA signal peptide-Mefp1 fusion proteins. OmpA signal peptide (OmpASP) is the 21 residue peptide fragment of the 23 residue OmpA signal sequence cleavable by signal peptidase I. We successfully produced increased levels of soluble recombinant Mefp1 (rMefp1) with various deletions of OmpASP, and found that the increased expression was caused by the increased pI of the N-terminus of the fusion proteins (${\geq}10.55$). All the OmpA signal peptide segments of 3-21 amino acids in length had the same pI value (10.55). Our results suggest that the pI value of the truncated OmpASP ($OmpASP_{tr}$) play an important role in directional signaling for the fusion protein, but we found no evidence for the presence of a secretion enhancer in OmpASP. For practical applications, we increased the expression of soluble rMefp1 with $OmpASP_{tr}$ peptides as directional signals, and obtained rMefp1 with the native amino terminus (nN-rMefp1) using an $OmpASP_{tr}$ Xa leader sequence that contains the recognition site for Xa protease.