• Korean Journal of Agricultural Science
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• v.39 no.4
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• pp.561-568
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• 2012

The aim of this study was to introduce a simple method for isolation of ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin from cow's milk, and peptides produced by enzymatic hydrolysis of ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin with alcalase. Whey protein were precipitated from whey by ammonium sulfate and, ${\alpha}$-lactalbumin and ${\beta}$-lactoglobulin were isolated using Hi Prep 26/60 Sephacryl S-100 column gel filtration chromatography. Bovine serum albumin and ${\beta}$-lactoglobulin were isolated by Mono-Q 5/50 GL column anion exchange chromatography of the 50% Ammonium Sulfate-supernatant. Isolated whey proteins were hydrolyzed by proteolytic alcalase. Tricine SDS-PAGE and reverse-phase HPLC analyses revealed that almost hydrolyzed all the ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin with alcalase. Molecular weight of various peptides derived from alcalase hydrolysate were small molecular weight than 3.5 kDa.

• Journal of Fisheries and Marine Sciences Education
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• v.26 no.6
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• pp.1209-1216
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• 2014

This feeding experiment was conducted to investigate the effects of slurry type diet on growth performance and survival rate of growing leptocephalus, eel larva. We need to find new materials of diets for rearing eel larvae. Test diets were formulated with the eggs of the shark, fish soluble concentrate, soybean peptide and fish protein hydrolysate. Fish (average length 6 mm) were fed 3 slurry type diet(A, B and C) based on shark egg for 5 times per day. During feeding experiment, survival rates were significantly different among 3 slurry type diets. Total protein, lipid, moisture, ash and free amino acids contents were analyzed for slurry type diets. Leptocephalus fed the C slurry type diet was grown up to $38.0{\pm}9mm$ at 150 days. But all leptocephalus fed B slurry type diet were died at 100 days, reaching $16.4{\pm}8mm$. This results suggest that basic information for diet development of eel leptocephalus.

• Journal of Life Science
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• v.22 no.2
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• pp.220-225
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• 2012

The peptides of enzymatic hydrolysates from oyster were determined by inhibitory activity against angiotensin-converting enzyme. The ACE inhibitory activity of enzymatic oyster hydrolysates increases with hydrolysis time. Among enzymatic oyster hydrolysates, oyster hydrolysates incubated with Protamex showed the best ACE inhibitory activity after 10 h. Hydrolysates were filtered through a HiSep ultrafiltration membrane (M.W. cut-off 30 kDa, 10 kDa) to obtain the peptide fractions with ACE inhibition activity. These fractions were applied to an HPLC column (watchers 120 ODS-AP $250{\times}4.6$ ($5{\mu}m$)). Six active fractions were collected and the range of ACE inhibition was from 29.56 to 85.85%. Peptide was purified from fraction B, showing the highest ACE inhibitory activity, and its sequence was Leu-Gln-Pro. These results suggest that PEH may be beneficial for developing antihypertensive food and drug.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.6
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• pp.713-717
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• 1999

In order to utilize protein hydrolysate produced from hoki (Johnius Belengeri) frame among many different fish processing wastes, hoki frame peptide (PHFP) and phosphorylated hoki frame peptide (PHFP) were prepared, and their calcium absorption accelerating effects were investigated in comparison to control and casein phosphopeptide (CPP). In in vitro experiment, HFP and PHFP inhibited calcium phosphate formation as high as 1.5-fold and 2.5-fold, respectively, comparing to control, In addition, the inhibition rate of calcium phosphate precipitation as increasing concentrations of HFP and PHFP was risen and was similar to that of CPP at 2.0 mg/ml of PHFP concentration, In in vivo experiment using the rats, the groups fed HFP and PHFP indicated significantly increased calcium content in the femur. In particular, the calcium content in the small intestine of the rat fed PHFP was higher than that of control group by approximately $60\%$.

• 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.

• Food Science of Animal Resources
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• v.33 no.4
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• pp.493-500
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• 2013

Gelatin is a collagen-containing thermohydrolytic substance commonly incorporated in cosmetic and pharmaceutical products. This study investigated the antioxidant activity of gelatin by using different reagents, such as 2,2-azinobis-(3-ethylbenzothiazoline- 6-sulfonic acid) (ABTS), 2,2-di (4-tert-octylphenyl)-1-picrylhydrazyl (DPPH), and oxygen radical absorbance capacity-fluorescein (ORAC-FL) in a porcine gelatin hydrolysate obtained using gastrointestinal enzymes. Electrophoretic analysis of the gelatin hydrolysis products showed extensive degradation by pepsin and pancreatin, resulting in an increase in the peptide concentration (12.1 mg/mL). Antioxidant activity, as measured by ABTS, exhibited the highest values after 48-h incubation with pancreatin treatment after pepsin digestion. Similar effects were observed at 48 h incubation, that is, 61.5% for the DPPH assay and 69.3% for the ABTS assay. However, the gallic acid equivalent (GE) at 48 h was $87.8{\mu}M$, whereas $14.5{\mu}M$ GE was obtained using the ABTS and DPPH assays, indicating about sixfold increase. In the ORACFL assay, antioxidant activity corresponding to $45.7{\mu}M$ of trolox equivalent was found in the gelatin hydrolysate after 24 h hydrolysis with pancreatin treatment after pepsin digestion, whereas this activity decreased at 48 h. These antioxidant assay results showed that digestion of gelatin by gastrointestinal enzymes prevents oxidative damage.

• Food Science of Animal Resources
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• v.30 no.2
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• pp.286-290
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• 2010

Angiotensin-converting enzyme (ACE) inhibitory activity and production optimization of ovotransferrin hydrolysates were studied. Ovotransferrin was hydrolyzed by several enzymes (protamex, alcalase, trypsin, pepsin, neutrase, and flavorzyme) and acid (0.03 N HCl). Ovotransferrin hydrolysate reduced ACE activity by 60.2%, 55.8%, and 42.6% when treated with trypsin, acid, and pepsin, respectively. Trypsin was selected for production of peptide having maximum AC inhibitory effect, which was greatest with 7 h hydrolysis. Central composite design determined that optimum composition of ACE inhibitory substances using substrate concentration of 20-35%, temperature of $35-55^{\circ}C$, and pH of 6.0-8.0. The optimum composition was 1% trypsin, substrate concentration of 26.32%, $51.29^{\circ}C$, and pH 6.32. Under this conditions, a maximum ACE inhibitory effect of 69.1% was evident, similar to the predicted value.

• Korean Journal of Food Science and Technology
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• v.34 no.3
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• pp.529-532
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• 2002

The angiotensin converting enzyme (ACE) inhibitory activity in peptic hydrolysate of raw anchovy cooking discards was 51.3% at 1 mg of protein per $100\;{\mu}L$ sample solution. While, after the treatment of pepsin for 4 h, was 65.8%. The crude peptides fractionated through Bio-gel P-2 column chromatography consisted of five fractions $({P-1}{\sim}{P-5})$ and had maximum inhibitory activity in the fraction P-2 ($IC_{50}$=0.319 mg protein/mL). The fraction P-2 was rich in aspartic acid, glutamic acid, and glycine.

• Korean Journal of Food Science and Technology
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• v.51 no.5
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• pp.473-479
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• 2019

Gryllus bimaculatus (GB) has recently been registered as a food variety in Korea. In the present study, we prepared protein hydrolysates from GB and evaluated their antioxidant capacity. Protein hydrolysates were prepared from dried GB using enzymatic hydrolysis using five different proteases, and protein hydrolysates showing high hydrolysis value (alcalase, flavourzyme, and neutrase) were separated further into fractions ${\leq}3kDa$ and then lyophilized. Based on $RC_{50}$ values of hydrolysates (${\leq}3kDa$) obtained from four different antioxidant analyses, the flavourzyme hydrolysates showed relatively high levels of antioxidant capacity among the three hydrolysates, and in particular, it showed considerably strong antioxidant activity in 2,2-diphenyl-1-picrylhydrazyl (DPPH) assays. The flavourzyme hydrolysate also significantly inhibited peroxidation of linoleic acid. These results suggest that protein hydrolysates from GB represent potential sources of natural antioxidants. Our current studies are focused on identification of active peptides from the flavourzyme hydrolysate.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.54 no.6
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• pp.849-860
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• 2021

This study investigated the preparation of seasoned anchovy sauce (SAS) and its functional characteristics by using aminopeptidase active fractions (AAFs) derived from squid Todarodes pacificus hepatopancreas as a bitter taste improver. As the base of the SAS, a hydrolysate (AAAH) prepared by continuously treating raw anchovies with Alcalase-AAF was used. The high-performance liquid chromatography profile of the AAAH suggested that the action of AAFs decreased the hydrophobicity of the N-terminal peptide related to bitterness in the protein hydrolysates. SAS was prepared by blending with the AAAH and other ingredients. The crude protein (2.5%), carbohydrates (18.4%), amino acid-nitrogen (1,325.1 mg/100 mL), and total free and released amino acids (FRAAs, 700.2 mg/100 mL) of SAS were higher than those of commercial anchovy sauce (CAS). Sensory evaluation revealed that SAS was superior to CAS in flavor, color, and taste. The main FRAAs of SAS were glycine (16.8%), alanine (13.2%), glutamic acid (7.8%), and leucine (7.3%). The amino acids that had a major influence on the taste according to the SAS taste values were glutamic acid, aspartic acid, alanine, and histidine. The angiotensin-converting enzyme inhibitory (2.21 mg/mL) and antioxidant activities (3.58 mg/mL) of SAS were superior to those of CAS.