• Korean Journal of Food Science and Technology
• /
• v.30 no.4
• /
• pp.895-901
• /
• 1998

To extract insoluble proteins and improve functional properties of sesame meal proteins was treated with phytase and protease from Aspergillus sp. It was found that the optimum pH, optimum temperature, optimum treatment time and optimum unit of enzyme for extraction of protein were pH $10{\sim}12$ (alkaline), $60^{\circ}C$, 11 hr. and 900 units of phytase and 60 units of protease, respectively. The foaming capacity, foaming stability, oil absorption and water absorption of sesame meal protein after treatment with phytase and protease were increased as compared to the control.

• Applied Biological Chemistry
• /
• v.41 no.1
• /
• pp.13-17
• /
• 1998

To improve extraction of insoluble proteins and functional properties of abolished proteins by protease. It was found that the optimum pH, optimum temperature, optimum treatment time and optimum unit of enzyme far extraction of protein were pH 9.0, $60^{\circ}C$, 8 hrs, 40 units. The foaming capacity and foaming satbility of sesame meal protein after treatment of enzyme were especially higher than control. The emulsion capacity and emulsion satbility of sesame meal protein were higher than control. Coil absorption as well as water absorption capacities of sesame meal protein were higher than control.

• Korean journal of food and cookery science
• /
• v.3 no.2
• /
• pp.1-8
• /
• 1987

Eighty eight percent of succinylation at $\varepsilon$-amino group of lysine was obtained from silkworm larvae protein concentrate and it resulted in increased bulk density and fat absorption, improved flavor and color, increased solubility over fivefold. Both emulsifying activity and emulsion stability of the succinylated protein were improved by 30% and emulsifying capacity was enhanced by 4%. Foaming capacity of the succinylated Protein concentrate was improved by 30% and foaming stability improved fivefold. The viscosity of succinylated silkworm larvae protein concentrate was increased at all concentrations and reached the highest at 4~5% of concentations. Acetylation of silkworm larvae protein concentrate caused negligible change in the functional properties studied. Therefore, high emulsification properties of silkworm larvae protein concentrate would be a good protein source for the emulsified foods.

• Applied Biological Chemistry
• /
• v.49 no.4
• /
• pp.304-308
• /
• 2006

To extract insoluble proteins from silkworm pupa meal, the meal was treated with pretense produced by Bacillus sp. JH-209. The extraction of insoluble silkworm pupa protein was enhanced at alkaline pHs ranged from 7 to 11 by treatment with the protease. The optimum extraction temperature was $40^{\circ}C$ for in soluble protein treated with pretense. The optimum protease treatment time for extraction of protein was 11 hrs and optimum amount of enzyme treated for extraction of protein was 60 Unit, respectively. The treatment of enzyme extracted more protein than ordinary extraction method without pretense. The foaming capacity, foaming stability, emulsion capacity, and emulsion stability of silkworm pupa meal protein extracted by the treatment of the enzymes increased at all pH ranges. Further more oil absorption as well as water absorption capacities of the protein extracted by the treatment of the enzymes were also increased.

• Food Science of Animal Resources
• /
• v.22 no.3
• /
• pp.267-273
• /
• 2002

The functional properties of egg shell membrane hydrolysate by Bacillus licheniformis(EESMH) and NaOH-ethanol(AESMH) as a food material were investigated.. The yield of egg shell membrane hydrolysate was about 15% by Bacillus licheniformis, whereas that was 70% by NaOH-ethanol. Histidine content was higher in EESMH (18.69%) than in AESMH (2.56%). Both EESMH and AESMH showed high protein solubility (>95%). Emulsi-fying activity and stability of EESMH were higher than those of AESMH. foaming capacity and stability of AESMH were 2 times higher than those of EESMH in the pH ranges from 2 to 12. The AESMH had antioxidative activity whereas EESMH had not. Therefore, both AESMH and EESMH can be used for industrial food materials from the results of functional properties.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.29 no.1
• /
• pp.57-63
• /
• 2000

To extract insoluble proteins from abolished soybean meal, the meal was treatesd with phytase and protease produced by Aspergillus sp. SM-15 and Aspergillus sp. MS-18. The extraction of insoluble soybean protein was increased at alkaline range more than pH 5 in case of phytase, pH 7 to 11 in case of protease and pH 5 to 12 in case of the mixed enzyme of phytase and protease. The optimum extraction temperature of insoluble protein was 5$0^{\circ}C$ for phytase and the mixed enzyme of phytase and protease, and 6$0^{\circ}C$ for protease. The optimum treatment time for extraction of protein was 9 hrs for phytase, 11 hrs for protease and the mixed enzyme of phytase and protease and optimum unit of enzyme for extraction of protein was 600 unit, 40 unit and 900 unit＋60 unit in case of phytase, protease, phytase and protease, respectively. The treatment of mixed enzyme showed higher extracton rate of protein than single enzyme treatment. The foaming capacity, foaming stability, emulsion capacity, and emulsion stability of soybean meal protein by the treatment of the enzymes increased at all pH range. Further more oil absorption as well as water absorption capacities by the treatment of the enzymes were also increased. The functional properteis of the soybean meal protein treated by the mixed enzyme were higher than those of soybean meal protein treated by the single enzyme.

• Korean Chemical Engineering Research
• /
• v.53 no.3
• /
• pp.382-390
• /
• 2015

Poly(methyl methacrylate) (PMMA) supports and amine additives were investigated to adsorb $CO_2$. PMMA supports were fabricated by using different ratio of pore forming agents (porogen) to control the BET specific surface area, pore volume and distribution. Toluene and xylene are used for porogens. Supported amine sorbents were prepared by wet impregnation of tetraethylenepentamine (TEPA) on PMMA supports. So we could identify the effect of the pore structure of supports and the quantity of impregnated TEPA on the adsorption capacity. The increased amount of toluene as pore foaming agent resulted in the decreased average pore diameter and the increased BET surface area. Polymer supports with huge different pore distribution could be fabricated by controlling the ratio of porogen. After impregnation, the support with micropore structure is supposed the pore blocking and filling effect so that it has low $CO_2$ capacity and kinetics due to the difficulty of diffusing. Macropore structure indicates fast adsorption capacity and low influence of amine loading. In case of support with mesopore, it has high performance of adsorption capacity and kinetics. So high surface area and meso-/macro- pore structure is suitable for $CO_2$ capture.

• Applied Biological Chemistry
• /
• v.33 no.1
• /
• pp.52-61
• /
• 1990

Fish protein was acylated with acetic anhydride(AA), succinic anhydride(SA) and maleic anhydride(MA) in order to improve the functional properties of the protein. The surface hydrophobicity and functional properties of protein were measured to study the relationship between them. It was found that the extented acylation of nucleophilic groups such as amino and sulfhydryl groups of the amino acid residues of fish protein was higher than other groups when acylated with AA, and the degree of acylation was 89.5 % for amino groups and 72.2 % for sulfhydryl groups. The surface hydrophobicity of fish protein was decreased by succinylation and maleylation, whereas acetylation caused tittle change. The acylated fish protein concentrate(FPC) showed higher surface hydrophobicity than the acylated fish myofibrilla protein(FMP). Acylation with AA, SA and MA of fish protein resulted in a significant increase in protein solubility, emulsifier properties, foaming properties, water adsorption capacity and oil adsorption capacity. These properties of acylated FMP were more improved than those of acylated FPC. Decrease in protein hydrophobicity was highly correlated with increase in protein solubility, and emulsifier properties and foaming properties were largely dependent on the solubility as well as surface hydrophobicity. The water adsorption capacity of the protein was significantly affected by solubility. Surface hydrophobicity had greater influence on oil adsorption capacity, whereas it had tittle effect on water adsorption capacity.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.57 no.1
• /
• pp.1-14
• /
• 2024

We investigated the functional properties and in vitro bioactivity of protein isolates (RPIs) recovered from olive flounder Paralichthys olivaceus roes by isoelectric solubilization/precipitation process, according to pH-shift treatments. The buffer capacity of RPIs was shown to be stronger in alkaline pH than in acidic pH. Water holding capacity of RPIs was in range of 4.5-5.2 g/g protein with no significant differences (P>0.05). The foaming capacity and emulsifying activity index of RPIs did not show any significant differences between RPI-1 (pH 11/4.5) and 3 (pH 12/4.5), however they were superior to RPI-2 (pH 11/5.5) and 4 (pH 12/5.5). The 2,2'-azino-bis-3-ethylbenzo-thiazoline-6-sulfonic acid radical scavenging activity of RPI-3 (2.5 mg protein/mL) was 102.4 ㎍/mL, and the angiotensin I converting enzyme inhibitory activity was 30.8%. Among the RPIs, RPI-3 was relatively superior in protein functional properties such as buffer capacity, foaming capacity, emulsification, and anti-oxidative activity. Therefore, we suggest that RPI prepared from olive flounder roes could serve as a potential food resource.

• Asian-Australasian Journal of Animal Sciences
• /
• v.4 no.4
• /
• pp.407-410
• /
• 1991

The relationship between the possible structural change due to chemical modifications and functionality changes was studied in pigskin collagen. Amino groups in collagen were modified by succinylation and reductive alkylation. Carboxyl groups were modified using carbodiimide. Thermal denaturation temperature of collagen increased remarkably by carboxyl groups modification whereas decreased by succinylation and reductive alkylation. Emulsifying capacity was improved by reductive alkylation and carboxyl groups modification while emulsion stability was improved by succinylation. Chemical modifications increased solubility whereas decreased the foaming capacity of collagen. Viscosity of collagen at various pH varied with methods of modification.