• Asian-Australasian Journal of Animal Sciences
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• v.27 no.1
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• pp.115-122
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• 2014

This study investigated on the effects of adding mechanically deboned chicken meat (MDCM) hydrolysates on the quality properties of imitation fish paste (IFP) during storage. IFP was prepared from Alaska Pollack, spent laying hens surimi and protein hydrolysates which were enzymatically extracted from MDCM. The study was designed as a $3{\times}4$ factorial design with three MDCM hydrolysate content groups (0%, 0.4%, and 0.8%) and four storage times (0, 2, 4, and 6 weeks). Addition of MDCM hydrolysates increased crude fat content but lowered water content (p<0.05). The breaking force of IFP, an indicator of gel formation, increased in treated groups compared to control (p<0.05). Angiotensin I-converting enzyme (ACE) activity was inhibited and free radical scavenging activity increased with increasing MDCM hydrolysate content (p<0.05). In conclusion, the addition of MDCM to IFP improves gel characteristics. Additionally, protein hydrolysates from MDCM serve as a potential source of ACE inhibiting peptides.

• Food Science and Preservation
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• v.30 no.3
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• pp.434-445
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• 2023

Hemp (Cannabis sativa L.) seeds have recently been attracting attention as a new high-value-added food material owing to their excellent nutritional properties, and research on the development of functional food materials using hemp seeds is actively progressing. This study aimed to evaluate the antioxidant properties of hemp seed protein hydrolysates. Protein hydrolysates were prepared from defatted hemp seed powder (HS) by enzymatic hydrolysis using five different proteases (alcalase, bromelain, flavourzyme, neutrase, and papain). 2,4,6-trinitrobenzene sulfonic acid (TNBS) assay and SDS-PAGE analysis revealed that HS showed a high degree of hydrolysis after treatment with each enzyme except papain. The total polyphenol content of the protein hydrolysates (<3 kDa) and the RC50 values obtained from two different antioxidant tests showed that alcalase hydrolysate (HSA) had a relatively high level of antioxidant capacity. In addition, treatment with HSA (25-100 ㎍/mL) significantly inhibited linoleic acid peroxidation. These results suggest that hemp seed protein hydrolysates are potential sources of natural antioxidants. Future studies will focus on the identification of active peptides from HSA.

• Preventive Nutrition and Food Science
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• v.5 no.3
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• pp.148-152
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• 2000

Mussel adhesive protein (MAP) was extracted from Korean Mytilus edulis and then partially purified using Sephacryl S-300 gel permeation chromatography and reversed-phase high performance liquid chromatography. As an indicator of adhesiveness, is 3,4-dihydroxyphenylalanine (DOPA) content was determined. Its DOPA/protein ratio of 0.19 was higher than those of other reports, indicating a good adhesive. The partially purified MAP was confirmed by acid-urea polyacrylamide gel electrophoresis using cetylpiridinium bromide as a cationic detergent. Sea mussel hydrolysates were prepared using three commercial proteases to provide value-added functional materials and their angiotensin converting enzyme (ACE) inhibitory activities were determined. Among hydrolysates of sea mussel, Protamex was the best and further purification would improved ACE inhibitory activity.

• Food Science of Animal Resources
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• v.37 no.1
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• pp.62-70
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• 2017

The aim of this study was identifying a suitable food grade enzymes to hydrolyze whey protein concentrates (WPCs), to give the highest bioactivity. WPCs from ultrafiltration retentate were adjusted to 35% protein (WPC-35) and hydrolyzed by enzymes, alcalase, ${\alpha}-chymotrypsin$, pepsin, protease M, protease S, and trypsin at different hydrolysis times (0, 0.5, 1, 2, 3, 4, and 5 h). These 36 types of hydrolysates were analyzed for their prominent peptides ${\beta}-lactoglobulin$ (${\beta}-Lg$) and ${\alpha}-lactalbumin$ (${\alpha}-La$), to identify the proteolytic activity of each enzyme. Protease S showed the highest proteolytic activity and angiotensin converting enzyme inhibitory activity of IC50, 0.099 mg/mL (91.55%) while trypsin showed the weakest effect. Antihypertensive and antioxidative peptides associated with ${\beta}-Lg$ hydrolysates were identified in WPC-35 hydrolysates (WPH-35) that hydrolyzed by the enzymes, trypsin and protease S. WPH-35 treated with protease S in 0.5 h, responded positively to usage as a bioactive component in different applications of pharmaceutical or related industries.

• Journal of Animal Science and Technology
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• v.47 no.1
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• pp.83-90
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• 2005

ACE-inhibitory peptides derived from goat's whey hydrolyzed by various proteolytic enzymes were separated and purified for antihypertension materials. The highest ACE-inhibitory activity of goat's whey hydrolysates was 85.5 % by pepsin for 72 hrs. Also the highest ACE-inhibitory activity of goat's whey hydrolysates was F-4 by pepsin for 72 hrs by Sephadex G-25 gel chromatograms. F-4e and F-4ed from F-4 by RP-HPLC to first and second purification were the highest in ACE-inhibitory activity, respectively. The most abundant amino acid was leucine(I 8.54 %) in F-4ed of ACE-inhibitory peptides after second purification. Amino acid sequence of F-4ed of ACE-inhibitory peptides showed Leu-Lys-Asp-Tyr-Gly-GlyVal- Ser-Leu and Leu-Gly-Asp-Gly-Ala-Gly- Asp-Val-Ala-Phe. $IC_{50}$ calibrated in peptic hydrolysates(72 hrs), F-4, F-4e and F-4ed from goat's whey hydrolysates by pepsin for 72 hrs were 33.93, 28.75, 11.74 and 1.09 mg/ml, respectively. From the results of this experiment, goat's whey hydrolysate by pepsin was shown to have ACE-inhibitory activity.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2005.05a
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• pp.109-116
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• 2005

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.5
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• pp.787-795
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• 2001

For the developing natural fisheries flavoring substances using crustacea, the flavor constituents of enzyme hydrolysates from shore swimming crab (crab) and spotted shrimp (shrimp) were investigated. In taste-active compounds of both enzyme hydrolysates, total free amino acid contents of crab and shrimp enzyme hydrolysates were 5,226.7 mg% and 8,757.3 mg%, respectively. The major amino acids were taurine, glutamic acid, proline, asparagine, glycine, alanine, valine, leucine, lysine anserine and arginine. As for ATP related compounds, AMP was the principal component and small amounts of IMP was detected in both enzyme hydrolysates. In the quarternary ammonium bases, betaine was the principal component (593.8mg%), and contents of TMAO and betaine in both samples were 60.7 mg% and 850.0 mg%, 124.1 mg% and 755.9 mg%, respectively. The major components were Na, K, P and Cl in inorganic ions. The major fatty acids of both sample were 14 : 0, 16 : 0, 16 : 1n7, 18 : 1n9, 20 : 5n3 and 22 : 6n3, and composition ration of n3 polyunsaturated fatty acids of were 27.8% and 28.5%, respectively. Total 99~109 volatile compounds were detected as a cooked odor of crab and shrimp enzyme hydrolysates by SDE apparatus/gas chromatography/mass spectrometry. The volatile flavor compounds identified from cooked crab enzyme hydrolysate were composed of 6 acids, 10 alcohols, 7 aldehydes, 11 ketones, 1 ester, 5 phenols, 4 benzenes, 22 hydrocarbons, 1 furan, 21 nitrogen containing compounds and 11 micellaneous compounds. And the volatile flavor compounds indentified from cooked shrimp enzyme hydrolysate were composed of 13 acids, 10 alcohols, 6 aldehydes, 10 ketones, 3 esters, 2 phenols, 5 benzenes, 36 hydrocarbons, 1 furan, 14 nitrogen containing compounds and 8 micellaneous compounds.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.31 no.6
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• pp.875-881
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• 1998

To develop functional food material with angiotensin converting enzyme (ACE) inhibitory peptides, muscle protein of anchovy, Engraulis japonica was hydrolyzed during 48 hrs by digestive pretenses such as pepsin, trypsin, $\alpha$-chymotrypsin, and commercial proteases such as papain, bromelain, complex enzyme, Elavourzyme, Novozym, Neutrase, Protamex and Alcalase. The only $50\%$ ethanol soluble hydrolysates were tested for inhibitory activity against ACE and yield of $50\%$ ethanol soluble peptide-nitrogen ($ESPN_{50}$). ACE inhibition effects and yield of $ESPN_{50}$ occurred as hydrolysis time increased to 8 hrs, Among those pretenses tested, hydrolysates by Alcalase and $\alpha$-chymohypsin had greater ACE inhibitory activity (80 and $74\%$, reipectively) with eletated levels of $ESPN_{50}$ (48 and 58 mg/ml, respectively), while Protamex hydrolysates had greater ACE inhibitory activities ($73\%$) with reduced levels of $ESPN_{50}$ (7.2mg/ml) than others. Amino acid compositions of $50\%$ ethanol solubles obtained from those hydrolysates were rich in glutamic acid, aspartic acid, cysteine and leucine.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.3
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• pp.229-235
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• 1992

Fish protein hydrolysates(FPH) prepared from defatted mackerel meal by proteases such as complex enzymes, bromelain, alcalase, $\alpha-chymotrypsin,$ trypsin, papain and pepsin were tested for inhibitory activity against angiotensin-I converting enzyme(ACE). Among proteases tested, the hydrolysates obtained from the treatment of complex enzymes or bromelain showed relatively higher activity. ACE inhibitory activity of the hydrolysates increased until hydrolysis of 8 hrs, and was stable by heat treatment for 20min at $100^{\circ}C.$ From the profiles of fractionation of the hydrolysates with Bio-gel P-2, the most active fraction had about MW 1,450 and it's amino acid was abundant in Asp, Glu, Lys, Leu, Val and Ala. $IC_{50}\;(amounts\;of\;inhibitors\;needed\;for\;50\%\;inhibition)$ of the active fraction of the hydrolysates obtained from the treatment of complex enzyme and bromelain was 90 and $130 {\mu}g,$ respectively.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.4
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• pp.427-431
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• 1999

This study was conducted to investigate the inhibitory activity of water extracts and its enzymatic hydrolysates from algae against angiotensin-I converting enzyme (ACE). The 7 kinds of algae were extracted with water at $50^{\circ}C,\;70^{\circ}C$ and $98^{\circ}C$. ACE inhibitory activities of water extracts were the highest at $70^{\circ}C$, and those of ceylon moss, layer, green layer, sea mustard, seaweed fusiforme sea tangle and sea staghorn were $10.9\%,\;9.3\%,\;8.9\%,\;8.2\%,\;7.5\%,\;7.1\%$ and $7.0\%$, respectively. Layer, green laver sea mustard and ceylon moss of high ACE inhibitory activities among the 7 kinds of water extracts were hydrolyzed by maxazyme and papain during 24hrs. ACE inhibitory activity of enzymatic hydrolysates was higher than that of water extracts, and was the highest in enzymatic hydrolysates of laver among the tested samples. In laver hydrolysates by proteases, the highest ACE inhibitory activity and peptide-nitrogen contents were observed at 8 hours hydrolysis and the hydrolysates by maxazyme showed relatively higher activity than those by papain(31.3 and $27.9\%$, respectively). But peptide-nitrogen contents were greater in papain hydrolysates than in maxazyme.