• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.6
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• pp.956-963
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• 1997

To enhance application of FPC in food industry, salmon FPC hydrolysates were produced and their functional properties were investigated. Hydrolysates of salmon FPC showed high solubilities ranged from approximately $80\~95\%$. Emulsifying activity index (EAI) values of hydrolysates were higher than that of egg white, however sugar ester showed the highest EAI value of 32.5. Though sugar ester had the best emulsifying stability value $({\Delta}EAI)$ of 9.65, hydrolysates showed better ${\Delta}EAI$ value than that of egg white. Foam Activity of hydrolysates was predominantly better than those of controls and also foam stability value showed similiar trend. Osmolality of hydrolysates was increased with the increase of degree of hydrolysis (DH) and concentration of protein, but it showed very lower osmolality than that of NaCl. Flow property of hydrolysates showed different upward-downward curves, and hysteresis loop increased with the increase of DH. ACE inhibitory activity showed similiar value ranged from $21.1\~24\%$ at all DH values.

• Fisheries and Aquatic Sciences
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• v.18 no.1
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• pp.13-20
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• 2015

Calculated chemical scores (computed in relation to the FAO/WHO reference protein) for salmon liver protein hydrolysates indicated that all amino acids (other than methionine and threonine) were present in adequate or excess quantities; thus, the raw liver material is a good source of essential amino acids. The hydrophobic amino acids contents in hydrolysates prepared from Oncorhynchus keta and O. gorbuscha were 38.4 and 39.1%, respectively. The proportion of released peptides exceeding 500 kDa was reduced when hydrolysates were treated with the commercial enzyme Alcalase, although proportions in the following MW ranges were elevated: 100-500 kDa and <50 kDa. The optimal conditions for enzymatic hydrolysis were as follows: pH 7.0, $50^{\circ}C$, and a reaction time of 1 h. Of the different proteases tested, Alcalase was the most efficient for production of salmon liver hydrolysate with the highest 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity. The hydrolysates prepared from salmon liver had a balanced amino acid composition. The liver protein hydrolysates contained low molecular weight peptides, some of which may be bio-active; this bio-active potential should be investigated. Inhibition of the DPPH radical increased with increased degree of hydrolysis (DH), regardless of protease type. DPPH radical scavenging abilities, antithrombotic effects and ${\alpha}$-glucosidase enzyme inhibition effects of O. keta liver hydrolysate increased in a dose-dependent manner. Thus, salmon liver hydrolysate may be useful in functional food applications and as a source of novel products.

• Korean journal of food and cookery science
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• v.20 no.3
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• pp.271-278
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• 2004

As an attempt to develop new functional beverages for breakfast, sweet potato based beverages were prepared with hydrolyzed sweet potato, potato, and carrot products (sample : water = 1 : 1), and their chemical and sensory properties were evaluated. The content of reducing sugar and soluble solid of the sweet potato, potato, and carrot increased with enzyme treatment, while their viscosity decreased without significant change of color. The hunter color test showed that the beverages with 10％ carrot content were high in redness leading to a decrease in their acceptability for sensory evaluation. The sensory score of the mixture containing 5％ carrot was good, but beverage with 0％ carrot reduced the sensory properties. The results showed that the final ratio of sweet potato to potato to carrot for the new functional beverage was 5 : 4.5 : 0.5. The pH of the beverage was adjusted to 5.0, 4.5, and 4.0 using an organic acid mixture. In the sensory test of the new functional beverage, the best sensory score(color, taste, smell, and texture) was the mixture of sweet potato : potato : carrot equaling 5 : 4.5 : 0.5 with a pH of 4.5.

• Journal of Dairy Science and Biotechnology
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• v.32 no.1
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• pp.7-16
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• 2014

Angiotensin-I-converting enzyme (ACE) inhibitory peptides have functional and potential properties of casein hydrolysates that are used in the development of food ingredients and anti-hypertensive hydrolysates derived from sodium caseinate enzymatic hydrolysates. Sodium caseinate could be treated by various kinds of commercial proteases, and then could be treated with the enzyme combination. Ultrafiltration treatment can be used to generate hydrolysates that can be used to determine ACE inhibitory activity. In general, hydrolysate quality can be evaluated by changes in hydrolysis characteristics, ACE inhibitory activity, as well as functional properties such as solubility, foam capacity, cytotoxicity, free radical-scavenging effects, and sensory evaluation. In this review, we present an overview of the ACE inhibitory peptides obtained by performing enzymatic hydrolysis on various sources to identify food ingredients and functional foods that reduce hypertension.

• Food Science and Preservation
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• v.15 no.3
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• pp.361-366
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• 2008

This study was investigated the functional characteristic change by the enzymatic hydrolysate to improve the functionality of soybean milk. The soymilk (SM), hydrolysates of soy milk (HSM), whole soy milk (WSM) and hydrolysates of whole soy milk (HWSM) revealed composition difference whether the bean-curd removal was included or not, but nearly no change was found by the low molecule enzyme treatment. The chromaticity revealed clear difference whether the bean-curd was removed or not, but did not show any difference by the hydrolyzation. Total free sugar and oligosaccharide content was found to be 1,389.88 mg% in SM, 1,013.51 mg% in HSM, 1,539.51 mg% in WSM, and 1,331.53 mg% in HWSM by showing the reduction after the enzyme hydrolyzation. DPPH free radical scavenging activity revealed to show high activity in HSM and in HWSM which were enzymatically hydrolyzed by 49.26% and 45.34%, respectively. And the ACE inhibition activity of HSM and HWSM was found to be approximately 1.6 times higher than the control SM and HSM The superoxide radical scavenging activity revealed to show high activity at HSM and HWSM, and no difference was found by the removal of bean-curd from raw soybean. Based upon these results, the functional characteristics of HSM, WSM and HWSM were found to be excellent compared to SM and it is expected to be used as various functional sources in a future.

• Food Science of Animal Resources
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• v.35 no.3
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• pp.350-359
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• 2015

This review focuses on the enhanced functional characteristics of enzymatic hydrolysates of whey proteins (WPHs) in food applications compared to intact whey proteins (WPs). WPs are applied in foods as whey protein concentrates (WPCs), whey protein isolates (WPIs), and WPHs. WPs are byproducts of cheese production, used in a wide range of food applications due to their nutritional validity, functional activities, and cost effectiveness. Enzymatic hydrolysis yields improved functional and nutritional benefits in contrast to heat denaturation or native applications. WPHs improve solubility over a wide range of pH, create viscosity through water binding, and promote cohesion, adhesion, and elasticity. WPHs form stronger but more flexible edible films than WPC or WPI. WPHs enhance emulsification, bind fat, and facilitate whipping, compared to intact WPs. Extensive hydrolyzed WPHs with proper heat applications are the best emulsifiers and addition of polysaccharides improves the emulsification ability of WPHs. Also, WPHs improve the sensorial properties like color, flavor, and texture but impart a bitter taste in case where extensive hydrolysis (degree of hydrolysis greater than 8%). It is important to consider the type of enzyme, hydrolysis conditions, and WPHs production method based on the nature of food application.

• Journal of Animal Science and Technology
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• v.52 no.5
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• pp.435-440
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• 2010

Whey protein concentrate (WPC) is widely used to increase the nutritional and functional properties of food. In this study, the physiochemical and functionality of WPC-30 hydrolysates were examined to evaluate the possibility of application in the food industry. The WPC-30 was manufactured using ultrafiltration and spray-drying, and then hydrolyzed with proteolytic enzyme including alcalase, flavourzyme, nuetrase and protamex. Enzymatic hydrolysis had a significant influence on the physicochemical properties as evident from the increased foaming capacity, solubility. Alcalase caused highest protein hydrolysis (3.26%) and the bitterness. Foaming capacity was largest in WPC-30 hydrolysate treated with flavourzyme. Protein solubility at various levels of pH was highest in protamex-treated WPC-30 hydrolysate. However, the solubility of WPC-30 hydrolysates was significantly improved in alkaline condition than in acidic and neutral conditions. The study revealed that spray dried enzyme modified WPC can be used in various functional food.

• Journal of Marine Bioscience and Biotechnology
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• v.11 no.2
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• pp.71-80
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• 2019

Previously, agar obtained from Gelidum sp. has a small molecular weight and has the disadvantage of inherent viscosity properties and poor functionality as a dietary fiber. In order to improve aforementioned disadvantages, agar having a fluidity that can be added to food at a higher concentration that a powder agar having a gelling property at low concertation was manufactured. In addition, the anti-inflammatory activity of agar hydrolysates was evaluated to confirm their potential as a functional material. As a result, agar hydrolysates significantly reduced NO levels secreted by LPS-activated macrophages and inhibited the expression of iNOS and COX-2, which are inflammatory mediators that regulates NO secretion in macrophages. Furthermore, in in vivo zebrafish embryos model results demonstrated significant reduction of LPS induced NO production after the treatment of agar hydrolysate hydrolyzed for 360 min. In addition, ROS production and cell death by stresses were also reduced in LPS-exposed embryos after the treatment of agar hydrolysis product hydrolyzed for 360 min. Taken together, agar hydrolysate hydrolyzed for 360 min can be easily added into food due to their fluidity and used as a food ingredient that inhibits inflammation due to their anti-inflammatory property.

• Food Science of Animal Resources
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• v.34 no.3
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• pp.362-371
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• 2014

This study utilized commercially available proteolytic enzymes to prepare egg-white protein hydrolysates (EPHs) with different degrees of hydrolysis. The antioxidant effect and functionalities of the resultant products were then investigated. Treatment with Neutrase yielded the most ${\alpha}$-amino groups (6.52 mg/mL). Alcalase, Flavourzyme, Protamex, and Ficin showed similar degrees of ${\alpha}$-amino group liberation (3.19-3.62 mg/mL). Neutrase treatment also resulted in the highest degree of hydrolysis (23.4%). Alcalase and Ficin treatment resulted in similar degrees of hydrolysis. All hydrolysates, except for the Flavourzyme hydrolysate, had greater radical scavenging activity than the control. The Neutrase hydrolysate showed the highest 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity ($IC_{50}=3.6mg/mL$). Therefore, Neutrase was identified as the optimal enzyme for hydrolyzing egg-white protein to yield antioxidant peptides. During Neutrase hydrolysis, the reaction rate was rapid over the first 4 h, and then subsequently declined. The $IC_{50}$ value was lowest after the first hour (2.99 mg/mL). The emulsifying activity index (EAI) of EPH treated with Neutrase decreased, as the pH decreased. The EPH foaming capacity was maximal at pH 3.6, and decreased at an alkaline pH. Digestion resulted in significantly higher 1,1-diphenyl-2-picrylhydrazyl (DPPH) and ABTS radical scavenging activity. The active peptides released from egg-white protein showed antioxidative activities on ABTS and DHHP radical. Thus, this approach may be useful for the preparation of potent antioxidant products.

• Fisheries and Aquatic Sciences
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• v.25 no.6
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• pp.335-349
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• 2022

To optimize the hydrolysis conditions in the production of antioxidant hydrolysates from tuna cooking juice concentrate (TC) to maximize the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, TC containing 48.91% protein was hydrolyzed with Alcalase 2.4 L, and response surface methodology (RSM) was applied. The optimum hydrolysis conditions included a 2.2% (w/v) Alcalase concentration and 281 min hydrolysis time, resulting in the highest DPPH radical scavenging activity of 66.49% (0.98 µmol Trolox/mg protein). The analysis of variance for RSM showed that hydrolysis time was an important factor that significantly affected the process (p < 0.05). The effects of different drying methods (freeze drying, hot air drying, and vacuum drying) on the DPPH radical scavenging activity and amino acid (AA) profiles of TC hydrolysate (TCH) were evaluated. Vacuum-dried TCH (VD) exhibited an increase in DPPH radical scavenging activity of 81.28% (1.20 µmol Trolox/mg protein). The VD samples were further fractionated by ultrafiltration. The AA profiles and antioxidant activities in terms of the DPPH radical scavenging activity, 2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid (ABTS) radical scavenging activity, ferric reducing antioxidant power, and ferrous ion chelating activity were investigated. Glutamic acid, glycine, arginine, and cysteine were the major AAs found in the TCH fractions. The highest DPPH radical scavenging activity was found in the VD-1 fraction (< 5 kDa). The VD-3 fraction (> 10 kDa) exhibited the highest ABTS radical scavenging activity and ferric reducing antioxidant power. The ferrous ion chelating activity was the highest in VD-1 and VD-2 (5 to 10 kDa). In conclusion, this study provided the optimal conditions to obtain high antioxidant activities through TCH production, and these conditions could provide a basis for the future application of TCH as a functional food ingredient.