• 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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.54 no.4
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• pp.543-551
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• 2021

Changes in gluten surface hydrophobicity, which play an important role in the functional characteristics of protein, were measured according to various protein concentrations, pH levels, electrolytes concentrations, and alginate molecular weights using 8-anilino-1-naphthalene sulfonic acid (ANS) as a fluorescent probe. Gluten surface hydrophobicity decreased as gluten concentration increased, reaching a maximum pH of 7.0. The effects of alginate molecular weights and alginate concentration on the surface hydrophobicity, emulsifying activity index (EAI), and emulsion stability index (ESI) of gluten-sodium alginate dispersion (GAD) were measured. Gluten surface hydrophobicity rapidly increased the asl NaCl concentration of gluten solution up to 300 mM and showed no significant increase above 300 mM. However, gluten surface hydrophobicity notably decreased until the concentration of CaCl₂ and MgCl₂ reached 30 mM, indicating no significant variations above 30 mM. GAD surface hydrophobicity increased as the concentration and molecular weight of sodium alginate increased, however, gluten concentration increased as the GAD surface hydrophobicity decreased. The EAI and ESI of GAD increased as both molecular weight and concentration of sodium alginate increased.

• Food Science of Animal Resources
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• v.31 no.5
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• pp.727-730
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• 2011

The effects of various NaCl levels (0, 0.3, and 0.6 M) and pH values (pH 5.0, 5.5, 6.0, and 6.5) on the emulsifying and gelling properties of pork myofibrillar protein (MP) were assessed. The emulsion stability index (ESI), emulsifying activity index (EAI), and creaming index were measured at a 1:20 ratio of MP to corn oil. The EAI and ESI of pork MP showed maximum values at pHs 6.0 and 6.5 and at 0.3 M NaCl, resulting in better emulsion properties. Additionally, the cooking yield (CY) and gel strength (GS) of emulsified MP gel were measured at an MP: corn oil ratio of 1: 2; GS increased with increasing levels of salt. At 0.6 M NaCl, GS decreased with decreasing pH from 5.5 to 6.5. GS and gelling properties were optimal at pH 5.5 in 0.6 M salt. The highest CY was observed at 0.6 M NaCl, regardless of the pH value. However, increasing pH increased CY at salt levels of 0 and 0.3 M. These results indicate that NaCl and pH profoundly affected the emulsified MP system. Future work will be conducted on the rheological properties of the pork emulsified system as affected by adding non-meat protein.

• Korean Journal of Food Science and Technology
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• v.32 no.5
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• pp.1093-1101
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• 2000

The effects of concentration and pH on the emulsifying and rheological properties of the pine nut's protein extract(PNPE) and carbohydrate extract(PNCE) were investigated. Emulsifying activity index(EAI) of sample containing PNPE was minimal at pH 4.0 and the alteration of pH from 4 to 3 or 8 increased EAI regardless of concentration. The most EAI(about 6.44 $m^2/g$ solid) significantly(p<0.05) observed in solution containing 1% PNPE at pH 8.0, but that of 3% PNPE(0.10 $m^2/g$ solid) was minimal at pH 4.0. The emulsion stability exhibited maximum value(about 20) in 3% PNPE emulsion at pH 8.0. However, EAI of samples containing PNCE increased gradually with the increase of pH, but it had lower value than that of samples containing PNPE. At pH 7.0 and 8.0, the rheological behavior of emulsion solutions showed Newtonian fluid(n=1, $r^2>0.99$) regardless of concentration in all samples containing PNPE, but the samples containing PNCE showed pseudoplastic behavior(n<1) in all conditions. The sample with the better emulsion stability index(ESI) significantly(p<0.05) exhibited the higher L, b, and ${\delta}E$, however, lower a value.

• Korean Journal of Food Science and Technology
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• v.30 no.4
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• pp.988-991
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• 1998

Plasma proteins were obtained from bloods of slaughtered bovine and porcine and analyzed by Fast Protein Liquid Chromatography (FPLC). Serum albumin content decreased in the following order: Porcine Plasma Protein (PPP)> Bovine Plasma Protein (BPP)> Whey Protein Concentrate (WPC). Protein contents of BPP, PPP, and WPC determined by Kjeldahl method were 85.79%, 82.30%, and 84.38%, respectively. Compared to WPC, plasma proteins had higher emulsifying activity index (EAI) below 2% protein concentration and slightly lower EAI above 4% protein concentration. Plasma proteins had higher EAI in the acidic pH range and more dependence on NaCl than WPC. Also, EAI of plasma proteins with NaCl was higher in the acidic range than that of WPC. These results indicated that plasma protein can be utilized as a raw material for emulsifier.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.4
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• pp.320-326
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• 2001

To obtain the basic data for preparing edible or biodegradable film, fish meal protein isolates (FMPI) were prepared through alkaline extraction. And FMPI's properties and the ester compounds permeability of FMPI film were measured. FMPI were extracted under various extracting time with 0.2 N NaOH solution at $60^{\circ}C$, Recovery ratios of FMPI extracted from fish meal were increased with extracting time increasing. Surface hydrophobicity of FMPI extracted for 1 hr showed highest value. Emulsifying activity index (EAI) was increased with the increasement of extracting time but its emulsifying stability index (ESI) showed an inverse results. Viscosity of FMPI solution showed the highest value at pH 2 but showed the lowest value at pH 4, The higher concentration of sorbitol as plasticizer showed the higher ethyl acetate permeability of FMPI film, Ethyl acetate permeability of FMPI films according to kind of plasticizers showed different degree and increased in order as follow: polyethylene glycol, glycerol and sorbitol. Ester compounds having the lower molecular weight showed the higher permeability. Increment of temperature increased the ethyl acetate permeability of FMPI film. FMPI haying higher surface hydrophobicity made FMPI film be higher tensile strength. On elongation of FMPI films, kinds of plasticizer were more effective than surface hydrophobicity of FMPI.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.51 no.4
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• pp.351-361
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• 2018

This study investigated the potential of collagenous protein fractions (CPFs) as functional foods. The specific CPFs studied were recovered from the roe of bastard halibut (BH), Paralichthys olivaceus; skipjack tuna (ST), Katsuwonus pelamis; and yellowfin tuna (YT), Thunnus albacares through the alkaline solubilization process at pH 11 and 12. The buffer capacity, water-holding capacity and solubility of CPFs with pH-shift treatment were significantly better at alkaline pH (10-12) than at acidic pH (2.0). At pH-shift treatment (pH 2 and 12), the foaming capacities of CPFs from ST and YT were improved compared to those of controls, but they were unstable compared to BH CPFs. The emulsifying activity index (EAI, $m^2/g$ protein) of CPFs (controls) was 16.0-21.1 for BH, 20.1-23.9 for ST and 9.3-13.7 for YT (P<0.05). CPFs adjusted to pH 12 showed improved EAI and YT CPFs showed significantly greater emulsifying ability than those from BH and ST. CPFs recovered from fish roe are not only protein sources but also have a wide range of food functionalities, confirming the high availability of fish sausage and surimi-based products as protein or reinforcing materials for functional foods and alternative raw materials.

• Food Science of Animal Resources
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• v.34 no.6
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• pp.808-814
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• 2014

This study investigated the effect of gum arabic (GA) combined with microbial transglutaminase (TG) on the functional properties of porcine myofibrillar protein (MP). As an indicator of functional property, heat-set gel and emulsion characteristics of MP treated with GA and/or TG were explored under varying NaCl concentrations (0.1-0.6 M). The GA improved thermal gelling ability of MP during thermal processing and after cooling, and concomitantly added TG assisted the formation of viscoelastic MP gel formation. Meanwhile, the addition of GA decreased cooking yield of MP gel at 0.6 M NaCl concentration, and the yield was further decreased by TG addition, mainly attributed by enhancement of protein-protein interactions. Emulsion characteristics indicated that GA had emulsifying ability and the addition of GA increased the emulsification activity index (EAI) of MP-stabilized emulsion. However, GA showed a negative effect on emulsion stability, particularly great drop in the emulsion stability index (ESI) was found in GA treatment at 0.6 M NaCl. Consequently, the results indicated that GA had a potential advantage to form a viscoelastic MP gel. For the practical aspect, the application of GA in meat processing had to be limited to the purposes of texture enhancer such as restructured products, but not low-salt products and emulsion-type meat products.

• 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.