• Food Science and Industry
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• v.51 no.4
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• pp.278-301
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• 2018

Although more than 80% of living organisms are found in marine ecosystems, only less than 10% of marine resources have been utilized for human food consumptions and other usages. It is well known that marine resources (fish, shellfish and algae) have exceptional nutritional properties; however, their functional characteristic has not been completely discovered. It is believed that metabolites (organic compounds, proteins, peptides, lipids, minerals, etc.) play an important role to show its biological properties. Marine proteins and peptides are considered to be future drugs due to their excellent biological activities with a fewer adverse side effect. Marine peptides show several biological activities, including antimicrobial, antioxidant, anti-inflammatory, anti-cancer, anti-viral, anti-tumor, anti-diabetic, anti-hypertensive, anti-coagulant, immunomodulatory, appetite suppressing and neuroprotective effects. Therefore, the pharmaceutical, nutraceutical, and cosmeceutical companies have been paid attention to the marine peptides to commercialize into products. This current review mainly focused on the above mentioned biological activities of marine peptides and protein hydrolysates as a functional food and pharmaceutical applications. To commercialize these materials in industrial level required large quantity in high-purity level, and it is complicated to produce huge quantity from the marine resources due to insufficient raw materials, unavailability of raw materials through a year, hinder the growth with geographical variations, and availability of compounds in extreme small quantities. The best solution for these issues is to introduce new modern technologies such as artificial intelligence robots, drones, submersibles and automated raw material harvesting vessels in farming industries instead of man power, which will lead to 4th industrial revolution.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2002.10a
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• pp.90-91
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• 2002

The angiotensin converting enzyme (ACE) generates the powerful vasoconstrictor angiotensin II by removing the C-terminal dipeptide from the precursor decapeptide angiotensin I (1). The enzyme also inactivates the vasodilator bradykinin (2). There have been many studies on ACE inhibitory substances as functional in food, and ACE inhibitory peptides were isolated (3-5). (omitted)

• Fisheries and Aquatic Sciences
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• v.8 no.2
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• pp.109-112
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• 2005

A peptide that inhibits angiotensin-converting enzyme (ACE) was isolated from a hydrolysate of Manila clam (Ruditapes philippinarum) proteins prepared with thermolysin. Amino acid sequence of the peptide was determined to be Leu-Leu-Pro. Chemically synthesized Leu-Leu-Pro had an $IC_{50}\;value\;of\;158\;\mu{M}$. Peptides related to the Manila clam-derived peptide were synthesized to study the structure-activity relationships. The tetrapeptide, Leu-Leu-Pro-Pro, had a very weak effect on the enzyme. However, Leu-Leu-Pro-Asn showed no inhibitory activity.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.35 no.5
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• pp.529-533
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• 2002

The peptides inhibiting angiotensin converting enzyme (ACE) were isolated from the hydrolysate of manila clam (Ruditapes philippinamm) proteins prepared with thermolysin. The thermolysin hydrolysate was pretreated with membrane filter (MW cut-off 10,000) to obtain the peptide fraction with ACE inhibition. The crude peptides were applied to a Sephadex LH-20 column and eluted with $30\%$ methanol. The three active fractions (A, B and C) were collected and concentrated, and then applied to a SP-Toyopearl 650S column equilibrated with distilled water and was eluted with a linear gradient of NaCl concentration (0 to 1 M). The four active fractions (A-1, A-2, B-1 and C-1) were collected and concentrated, and then applied to a SuperQ-Toyopearl 650S column equilibrated with distilled water and was eluted with a linear gradient of NaCl concentration (0 to 1 M). The maximum inhibitory activity was observed in the fraction B-1Q showed the IC_{50} values of 0.748 $\mu$g. The abundant amino acids obtained from active fraction B-1Q were leucine, isoleucine, alanine and threonine.

• Ocean and Polar Research
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• v.25 no.3
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• pp.249-256
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• 2003

An immunological method was developed in this study to quantify reproductive output of the female butter clam, Saxidomus purpuratus. A clam egg-specific polyclonal antibody was developed using the purified butter clam egg as an antigen. An indirect Enzyme-Linked Immunosorbent Assay (ELISA) was used in quantitative measurement of the eggs. Size of the butter clam eggs ranged from $70.81{\pm}7.52{\mu}m$ in histology or $88.56{\pm}11.31{\mu}m$ in intact eggs. The predominant egg constituent was protein (37.44%), followed by lipids (11.40%) and carbohydrates (9.68%). The SDS-PAGE showed that the egg proteins are composed of several peptides of molecular weights consisting of 247, 200, 99, 91, 54 and 47 kDa. ELISA indicated that the clams collected from Geoje Island in May 2002 produced 8.2 to 26.8% of their body weight as eggs or 9,307,309 to 31,156,333 with a mean of 16,931,893 eggs per individual clam. The results of this study thus suggest that indirect ELISA using rabbit anti-clam egg IgG as a primary antibody is a rapid, affordable and sensitive method to assess reproductive output of 5. purpuratus and possibly other bivalves using a small amount of eggs.

• Asian Pacific Journal of Cancer Prevention
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• v.17 no.12
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• pp.5139-5145
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• 2016

There has been an increment in the number of studies focused on marine bioactive materials. Many peptides and other biomaterials with anticancer potential have been extracted from various marine animals. Artemia extracts have found uses in sun-light protection cosmetics and anti-aging products. However, contents of biochemical compounds in Artemia spp. and molecular mechanisms of have not been clearly studied in leukemic cells in vitro. In this work, we isolated and purified proteins of Artemia Urmiana. Six clear fractions (A-F) observed on DEAE-cellulose chromatography were assayed for effects on cell growth, differentiation and apoptosis using the human leukemic HL-60 cell line. Cell proliferation analysis by MTT and BrdU assays indicated that did not affect cells, growth. Cells treated with crude extract and fractions A, B and C, but not E and F (up to $100{\mu}g/mL$), exhibited increase of cell growth in a dose dependent manner. Stimulatory effects of fraction D were observed at concentrations of $10{\mu}g/mL$ and above. In nitro blue tetrazolium (NBT) reduction assays, treatment with $100{\mu}g/mL$ of fraction E or F for 96 hr increased the fraction of differentiated cells up to $14.8{\pm}3.56%$ and $16.5{\pm}2.08%$ respectively. Combination of those fractions with retinoic acid had significant synergistic effects on the differentiation of cells ($56.8{\pm}3.7%$ and $67.4{\pm}4.2%$, $p{\leq}0.01$). Annexin-V FITC staining for apoptosis and flow cytometric assays indicated induction of apoptosis by fractions E and F up to 23.8 and 31.8% of cells.

• 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.

• Microbiology and Biotechnology Letters
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• v.34 no.1
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• pp.1-6
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• 2006

Harmful algal blooms (HABs or red tides), caused by uncontrolled proliferation of marine phytoplankton, impose a severe environmental problem and occasionally threaten even public health. We sequenced the genome of an EPS-producing marine bacterium Hahella chejuensis that produces a red pigment with the lytic activity against red-tide dinoflagellates at parts per billion level. H. chejuensis is the first sequenced species among algicidal bacteria as well as in the order Oceanospirillales. Sequence analysis indicated a distant relationship to the Pseudomonas group. Its 7.2-megabase genome encodes basic metabolic functions and a large number of proteins involved in regulation or transport. One of the prominent features of the H. chejuensis genome is a multitude of genes of functional equivalence or of possible foreign origin. A significant proportion (${\sim}23%$) of the genome appears to be of foreign origin, i.e. genomic islands, which encode genes for biosynthesis of exopolysaccharides, toxins, polyketides or non-ribosomal peptides, iron utilization, motility, type III protein secretion and pigment production. Molecular structure of the algicidal pigment was determined to be prodigiosin by LC-ESI-MS/MS and NMR analyses. The genomics-based research on H. chejuensis opens a new possibility for controlling algal blooms by exploiting biotic interactions in the natural environment and provides a model in marine bioprospecting through genome research.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.19 no.3
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• pp.219-226
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• 1986

To confirm the application of a newer in vitro assays to determining the nutritional value of marine crustaceans (mainly shrimps and crabs), which have been considered to be highly nutritive depending on their levels of the essential amino acids and digestibility, their C-PERs and DC-PERs were determined and studied the factors influencing their in vitro results. Four species of seawater shrimps and 2 species of seawater crabs were used in this experiment. The in vitro digestibilities showed $83{\sim}86\%$ for raw shrimps and the trypsin indigestibile substrate content (TIS) was ranged from 1.32 to 3.33 mg/g solid expressed quantitatively as mg of purified soybean trypsin inhibitor. The smaller size of shrimps revealed a greater in vitro digestibility and a lower contents of TIS. It was noted that the in vitro digestibility of raw blue crab meat was around $85\%$ while boiled tenner crab meat showed $86\%$ or above, and the leg meat had the greatest in vitro digestibility in the various parts of crab meats. The poor in vitro digestibilities for shrimp's and crab's meat, compared with that of the other seafoods as noted in previous reports, suggest that the drop in pH, due to the change in their freshness during harvesting and frozen storage, resulted in underestimating their digestibilities using four-enzyme digestion technique. The lysine contents in all samples were higher than that of ANRC casein but they contained a slightly lower sulfur-containing amino acids than those in ANRC casein. But the other EAA, such as valine, tyrosine and phenylalanine, were found to be a half as little as that in casein and played a key-factor in calculation of C-PER or DC-PER. It was observed that the value of C-PER and DC-PER for all samples ranged from 2.1 to 2.4, and the predicted digestibilities showed $90\%$ or above in all samples. It was a different results from the fact that the animal proteins bear a higher values and predicted digestibilities than those of C-PER values. The lack of correlation between C-PER and DC-PER values is attributable to the fact that the lower content of valine, tyrosine and phenylalanine, and drop in pH owing to the changes of freshness in marine crustacea proteins. Therefore, if a newer in vitro digestion technique-which are taken into account the pH drop before digestion, TIS content and released free amino acids and/or peptides-developed, C-PER assays can provide more advantages in assessing the protein nutritional value of marine crustacea than any other in vitro assays.

• Korean Journal of Food Science and Technology
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• v.38 no.4
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• pp.567-570
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• 2006

This study was carried out to investigate the effect of antihypertensive peptides originating from marine proteins on ACE inhibitory activity and systolic blood pressure in spontaneously hypertensive rats (SHR). Sixteen male SHR (SHR/NCrj) weighing approximately 270 g were randomly divided into few experimental groups based on diet: C (control), A (anchovy), P (pollack) and M (mackerel). The final body weights of P and M groups were higher, than those of C and A groups, but difference was not significant. Average reference blood pressure (RBP) was 224 mmHg at 12 weeks old. Compared with RBP, final systolic blood pressure of the marine peptide oops after 28 days of feeding with anchovy, pollack and mackerel fractions by gavage was decreased by 9.0% (A), 10.2% (P) and 14.3% (M), respectively, but was not different in C. Especially, final blood pressure of M was lower by 32 mmHg than RBP. These results suggested that peptide originated from mackerel hydrolysate was considered to have an antihypertensive fraction as effective lowering of blood pressure in SHR.