• Journal of the Korea Academia-Industrial cooperation Society
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• v.17 no.7
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• pp.182-191
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• 2016

The purpose of this research was the optimization of protein hydrolysate production using a commercial enzyme bromelain 1200 derived from the leg of Yeonsan Ogae by response surface methodology. Yeonsan Ogae has long been known as supporting health and high efficacy treatment. In recent days, as the efficacy of functional peptides becomes more known, optimization of oligopeptide production and its characteristics from Ogae leg meat has been performed. Response surface methodology was performed for optimization of enzyme hydrolysis. The process was varied in pressure (30 to 100 MPa), time (1 to 3 h), and substrate concentration (10 to 30%). The degree of hydrolysis, amino acids, and molecular weight of products were analyzed. The optimum conditions were determined to be a pressure of 100 Mpa, time of 3 h, and substrate concentration of 20%. Under optimized conditions, degree of hydrolysis was 34.10%. The average molecular weight of protein hydrolysates was less than 1,000 Da. Major amino acids were leucine, lysine, alanine, glutamic acid, and phenylalanine.

• Journal of Dairy Science and Biotechnology
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• v.39 no.1
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• pp.36-50
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• 2021

This study aimed to evaluate the biological potential of functional food, i.e., specific peptides obtained from the hydrolysis of milk protein, by assessing their antioxidant and antibacterial properties. For the preparation of casein hydrolysates, commercial enzymes were added to 10% casein solution in a 1:200 (w/v) ratio, and samples were collected each hour. Based on the assessment of the degree of hydrolysis (DH) of casein hydrolysates, it was observed that the concentration of all enzymatic hydrolysates increased rapidly from 30 to 40 minutes. However, no change was observed in their concentrations after 150 minutes. Protamex® and Neutrase® exhibited the highest DH when compared to other enzymes. Furthermore, SDS-PAGE was performed for analyzing the proteolytic pattern of each enzyme, except for Flavourzyme®, and peptides in the size range of 20-25 kDa were identified. Subsequently, peptides produced by two enzymes were isolated using a preparative liquid chromatography system. Overall, NF3, NF4, PF5, and PF6 showed higher antioxidant potential than other peptide fractions. Moreover, NF7 and PF3 exhibited the highest antibacterial activity. In this study, we evaluated the biological potential of novel casein-derived peptides that may find application in the food and healthcare industry.

• Journal of Animal Science and Technology
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• v.62 no.5
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• pp.741-752
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• 2020

Herein, the in vitro protein digestibility of lyophilized Protaetia brevitarsis larvae flour with and without defatting using 70% ethanol was compared with beef loin. Proximate analysis showed that the defatted larvae contained the highest protein content (p < 0.05). The viable counts of total aerobic bacteria, Escherichia coli, and coliform bacteria decreased significantly after defatting the larval samples with 70% ethanol (p < 0.05). Measurement of α-amino group content and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed higher amounts of low molecular weight proteins in the larvae compared to beef loin (p < 0.05). After in vitro digestion, the degree of protein hydrolysis of the digesta was higher for both larvae samples compared to beef loin (p < 0.05). No change was observed in the in vitro larval protein digestibility after defatting. These results highlight the excellent protein digestibility of P. brevitarsis larvae with high protein content. Defatting insect flour with 70% ethanol could enhance microbial safety while maintaining excellent protein digestibility.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.5
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• pp.784-787
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• 1997

Enzymatically hydrolyzed soy sauce(eHSS) was prepared by the treatment of defatted soy flake using two types of proteases, followed by maillard reaction and formulation with some ingredients. The eHSS was mixed with fermented soy sauce(FSS) to make enzymatically hydrolyzed mixed soy sauce(eHMSS). The properties and sensory characteristics were evaluated and compared with commercially available soy sauces. The control of salt and total nitrogen contents in eHSS and eHMSS was easy, and the production of soy sauce of low salt and high protein was possible. However, the free amino acid content of eHSS was lower than FSS. due to lower degree of hydrolysis. In sensory evaluation, the eHSS have no loss taste and overall acceptance than FSS. Consequently, the eHSS and eHMSS have the potential for use with FSS to produce high quality soy sauce of low salt and high protein contents.

• Fisheries and Aquatic Sciences
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• v.14 no.3
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• pp.174-178
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• 2011

This study aimed to determine the degree of hydrolysis and angiotensin-I-converting enzyme (ACE)-inhibitory activity of Giant Jellyfish Nemopilema nomurai (jellyfish) hydrolysates. The degree of hydrolysis using six proteolytic enzymes (Alcalase, Flavozyme, Neutrase, papain, Protamex, and trypsin) ranged from 13.1-36.8% and the inhibitory activities from 20.46-79.58%. Using papain hydrolysate, we newly isolated and characterized ACE-inhibitory peptides with a molecular weight of 3,000-5,000 Da that originated from jellyfish collagen. The purified peptide (FII-b) was predicted to be produced from an alpha-2 fragment of the type IV collagen of jellyfish. The N-terminal sequence of FII-b was Asp-Pro-Gly-Leu-Glu-Gly-Ala-His-Gly- and showed 87% identity to the collagen type IV alpha-2 fragment of Rattus norvegicus and a predicted protein from Nematostella vectensis, indicating that the ACE-inhibitory peptide originated from the collagen hydrolysate and had an $IC_{50}$ value of 3.8 ${\mu}g$/mL. The primary structure of the fragment is now being studied; this peptide represents an interesting new type of ACE inhibitor and will provide knowledge of the potential applications of jellyfish components as therapies for hypertension.

• Food Science of Animal Resources
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• v.38 no.4
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• pp.780-793
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• 2018

This study was conducted to compare the anti-allergic effects of a whey protein concentrate (WPC) and WPC hydrolysate. WPC hydrolysate was prepared using enzymatic digestion for 8 h with trypsin and ${\alpha}$-chymotrypsin, after which it was freeze-dried. The allergic parameters assessed in rat basophilic leukemia (RBL)-2H3 cells were degranulation and release of ${\beta}$-hexosaminidase, release of tumor necrosis factor $(TNF)-{\alpha}$, and changes in the expression of $IL-1{\beta}$, IL-4, and IL-10 by real time polymerase chain reaction (PCR). During preparation of the WPC hydrolysate, hydrolysis increased rapidly from 0 to 10 min and then gradually increased slowly from 1 h onwards, achieving a final degree of hydrolysis of 78.50%. The SDS-PAGE analysis revealed a reduction in the intensity of several protein bands in the WPC hydrolysate compared to the WPC. IgE-induced ${\beta}$-hexosaminidase release from RBL-2H3 cells was decreased to a higher degree following treatment with the hydrolysate compared to WPC treatment. W500 ($500{\mu}g/mL$ WPC) showed the least inhibition of ${\beta}$-hexosaminidase release, but there was no significant difference between W500 and W1000 ($1,000{\mu}g/mL$) (p<0.05). H1000 ($1,000{\mu}g/mL$ WPC hydrolysate) inhibited ${\beta}$-hexosaminidase release by 39%. Compared to the control, treatment with H1000 decreased $TNF-{\alpha}$ secretion to 11.87 pg/mL. The gene expression levels of IL-1${\beta}$, IL-4, and IL-13 were all significantly decreased in hydrolysate (p<0.05). In the case of $IL-1{\beta}$ and IL-4, the expression levels in W1000 treated cells were decreased by 73.67% and 65%, respectively, and that of IL-13 was decreased by 66.43% compared to the control.

• Korean Journal of Food Science and Technology
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• v.24 no.6
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• pp.519-523
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• 1992

The patterns on the proteolysis of mussel protein using a commercial enzyme preparation were investigated. The best one among six commercial enzyme preparations for the manufacture of mussel extract was Corolase PP, based on the degree of hydrolysis (DH). When the raw mussel paste, without water addition, was adjusted to pH 6.5, added 0.1% (w/w dry basis) of Corolase PP. and reacted at $50^{\circ}C$ for four hours, it reached the maximum value of DH (79%). The precooking of raw mussel decreased the efficiency of extraction and hydrolysis of the protein, due to the inactivation of the autolytic enzymes contained in the mussel. During the course of proteolysis, major free amino acids such as glycine, alanine, glutamic acid and lysine, representing a characteristic brothy taste of mussel were replaced with free hydrophobic amino acids including valine, methionine, isoleucine, and leucine. The electrophoretic pattern and HPLC-GPC pattern of mussel protein hydrolysates during the hydrolysis were observed and also discussed.

• Applied Biological Chemistry
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• v.42 no.1
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• pp.49-57
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• 1999

Enzymatic hydrolysis with tuna pyloric caeca crude enzyme(TPCCE) was performed to recover a protein hydrolysate from hoki frame, fish processing by-product. Optimum hydrolytic conditions were pH 10.0, temperature $50^{\circ}C$, and incubation time 12 hrs, and then the degree of hydrolysis was about 60%. The yield of the hydrolysate from hoki frame by enzymatic hydrolysis was approximately 77% on a dry weight basis. The prepared protein hydrolysates were also fractionated through a series of 30, 10, 5 and 1 kDa molecular weight cut-off (MWCO) membranes in order to investigate the effect of their functionalities according to the difference of their molecular size. As the result of studying functionalities of the hydrolysates, 1 K hydrolysate showed the highest solubility over all pHs, and 30 and 10 K hydrolysate showed more excellent emulsifying property and whippability than the other hydrolysates.

• Journal of Applied Biological Chemistry
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• v.55 no.4
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• pp.263-266
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• 2012

Isolation of iron and calcium-binding peptides derived from cottonseed meal protein (CMP) hydrolysates was investigated. The degree of hydrolysis of CMP by Flavourzyme was monitored using trinitrobenzenesulfonic acid method and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Enzymatic hydrolysis of CMP for 12 h was sufficient for the preparation of CMP hydrolysates, and the hydrolysates were membrane-filtered under 3 kDa as a molecular weight. The filtered solution was fractionated using Q-Sepharose fast flow, Sephadex G-15, and reversed phase-high performance liquid chromatography for iron and calcium-binding peptides. As a result, F51 fraction was obtained as the best candidate for calcium and iron chelation, and the isolated iron and calcium-binding peptides can be used as functional food additives, similar to iron and calcium supplements.

• Food Science and Preservation
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• v.10 no.1
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• pp.80-88
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• 2003

In order to establish the enzymatic hydrolysis system improving of taste and flavor in the preparation of soy protein hydrolysates using the enzymes with excellent hydrolytic ability and different hydrolysis pattern of soy protein, Degree of hydrolysis(DH) and surface hydrophobicity under the optimal conditions of enzyme reaction, hydrolysis patterns by the SDS electrophoresis and sensory evaluation of soy protein hydrolysates by enzyme reactions were investigated. Four enzyme reactions were highly activated at pH 7.0, 45$^{\circ}C$ under the optimal conditions. As result of changes on the pattern of soy-protein hydrolysates by SDS-electrophoresis, high molecular peptides of hydrolysates by No. 5(Mucor circinelloides M5) and No. 16(Bacillus megaterium B16) enzymes were slowly decrease and 66KD band of these were remained after 3hours reaction. Production of low molecular peptides of hydrolysates by No. 4(Aspergillus oryzae M4) and No. 95(Bacillus subtilis YG 95) enzymes were remarkably detected during the proceeding reactions. As results of HPLC analysis, low molecular peptides of 15∼70KD were mainly appeared during the proceeding enzyme reactions. And, the more DH was increased, the more SDS-surface hydrophobicity was decreased. Hydrolysates by No. 4 enzyme was not only the highest DH of all hydrolysates, but the strongest bitter taste in a sensory evaluation. Sweat taste among the hydrolysates showed little difference. But, when combinative enzymes were treated, combinative enzyme of No. 4(Aspergillus oryzae M4)and No. 16(Bacillus megaterium B16) showed the strongest sweat taste. In conclusion, we assumed that it will be possible to prepare the hydrolysates having functionality when soy-protein were hydrolyzed by these specific enzymes.