• Journal of Applied Biological Chemistry
• /
• v.42 no.4
• /
• pp.180-185
• /
• 1999

Protein concentrate was produced and succinylated from rice bran to assess and improve its functional properties for the purpose of expanding the uses of rice bran proteins. The most effective solvent for the extraction of rice bran proteins was 20% aqueous ethanol at pH 9. The protein content of rice bran protein concentrate produced was 70.0% and the total protein yield was 64.3%. The extent of succinylation of free amino groups in the modified products was 72.8%. Though the modified protein products showed good functional properties including solubility, emulsion properties, and oil absorption capacity, it did not form gel. Succinylation improved solubility and emulsion and gelling properties. These improvements in functionality will enhance the value of rice bran proteins, thus enabling them to be more competitive with other food proteins.

• Food Science of Animal Resources
• /
• v.39 no.2
• /
• pp.296-308
• /
• 2019

Although the yellow mealworm (Tenebrio molitor L.) is a promising alternative protein source, the effects of processing conditions on functional properties are unclear. In this study, a protein extract of yellow mealworm larvae (PEYM) was subjected to different heat temperature ($55^{\circ}C$, $75^{\circ}C$, and $95^{\circ}C$) with different time (20, 40, and 60 min) to evaluate the functional properties and protein oxidation. Different heat temperature treatment significantly affected the exposure of surface hydrophobicity of the proteins and protein molecule aggregation, which reached maximum levels at $95^{\circ}C$ for 60 min. Protein oxidation was inversely proportional to the temperature. Both the highest carbonyl value (1.49 nmol/mg protein) and lowest thiol value (22.94 nmol/mg protein) were observed at $95^{\circ}C$ for 60 min. The heating time-temperature interaction affected several functional properties, including solubility, emulsifying potential, and gel strength (GS). Solubility decreased near the isoelectric point (pH 5 to 6). As the temperature and heating time increased, emulsifying properties decreased and GS increased. The oil absorption capacity and foaming properties decreased and the water absorption capacity increased. These results confirmed that PEYM is a suitable source of proteins for processing and applications in the food industry.

• Journal of the Korean Magnetic Resonance Society
• /
• v.21 no.1
• /
• pp.26-30
• /
• 2017

Dynamic properties of proteins can present key information on protein-ligand and protein-protein interaction. Despite their usefulness, the properties of protein dynamics have not been obtained easily due to protein stability and short-term measurement. Here, it is shown that combined method for analysis of dynamical properties. It utilizes predicted order parameter and NMR relaxation data such as $T_1$, $T_2$, and heteronuclear NOE. The suggested method could be used to know the flexibility of protein roughly without precise dynamical parameters such as order parameters through model-free analysis.

• Journal of Dairy Science and Biotechnology
• /
• v.40 no.3
• /
• pp.134-142
• /
• 2022

Protein-enriched dairy powder is widely consumed to promote muscle synthesis. Recently, in Korea, elderly people have also begun consuming protein powder products to prevent muscle loss. However, these protein-enriched powders have poor flowability and hydration properties because of the fine particles of spray-dried milk protein powder. Therefore, in this study, the fluidized bed agglomeration process was used to solve these problems. The rheological and physical properties of milk protein isolate (MPI)/skim milk powder (SMP) mixtures were effectively improved via fluidized bed agglomeration. The particle size of the MPI/SMP mixtures significantly increased from 35.7-58 ㎛ to 118-136 ㎛, the flowability level improved from fair (21.4-26.3) to good (15.7-16.3), and the cohesiveness level changed from intermediate (1.27-1.36) to low (1.18-1.19) after fluidized bed agglomeration. In addition, the wetting time of the agglomerated MPI/SMP mixtures was effectively reduced to 4.67-58.3 s by fluidized bed agglomeration. These findings may be useful for manufacturing protein-enriched dairy powders with good instant properties.

• Food Science and Preservation
• /
• v.5 no.1
• /
• pp.65-71
• /
• 1998

The changes in gel characteristics of soy protein as a result of various reagents that alter specific interactions which affect the formation and textural properties of gels, were studied. The reagents were added to 15% soy protein solutions prior to heat treatment. The gels were not formed with urea, indicating that hydrogen bonds significantly contributed to the formation and hardness of soy protein gel. Hydrophobic interactions and disulfide bonds compensated for hydrogen bonds and the contributions of electrostatic interactions to gel hardness are relatively insignificant. The farce primarily responsible for gel cohesiveness appeared to be disulfide bonds, because a significant decrease in cohesiveness was found only with the presence of N-ethylmaleimide. Adhesiveness decreased only with the addition of urea, and thus the contribution of hydrogen bonding to adhesiveness of gel could be concluded to be resent. However, adhesiveness was suggested to be interpreted not only wile molecular forces involved in gel formation but also with hydration properties of protein.

• 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 Food Science and Technology
• /
• v.20 no.5
• /
• pp.625-630
• /
• 1988

Phosphorylation of soy protein by sodium trimetaphosphate and acetylation of soy protein by acetic anhydride were performed. Then, the functional properties of modified soy proteins were compared with that of unmodified soy protein. Isolated soy protein prepared from defatted soybean flake had protein content of 92.7% as moisture-free basis. The phosphorylated soy protein showed higher solubility, foaming properties, and water holding capacity than unmodified soy protein. Acetylation of soy protein increased emulsification activity and foaming properties greatly, whereas decreased the solubility at pH 8.0. Isoelectric pHs of phosphorylated and acetylated soy protein were shifted to acidic regions(pH 3.0 and pH 4.0) from pH 5.0, which was the isoelectric pH of unmodified soy protein. Soy protein seems to be aggregated during phosphorylation and acetylation procedure, judging form Sepharose CL-4B gel filtration profiles. The modified soy proteins showed increased mobilities to anode direction in disc-gel electrophoresis.

• Food Science of Animal Resources
• /
• v.43 no.6
• /
• pp.1031-1043
• /
• 2023

The purpose of this study was to investigate the functional properties of salt-soluble proteins obtained from Protaetia brevitarsis (PB) and Tenebrio molitor (TM) larvae, the interaction between these proteins and pork myofibrillar protein (MP) in a gel system. The gel properties of salt-soluble protein extracts showed that the PB had a higher viscosity than the TM protein. However, the TM protein had higher gel strength compared with the PB protein. The gelation characteristics of the pork MP gel systems added with lyophilized insect salt-soluble protein powder showed to decrease slightly viscosity compared with MP alone. Adding the TM or PB protein powder did not affect the pork MP's hydrophobicity and sulfhydryl group levels. Furthermore, the protein bands of the MP did not change with the type or amount of insect salt-soluble protein. The cooking yields of the pork MP gels containing PB or TM protein powder were higher than those without insect protein. Regardless of the type of insect salt-soluble protein added, the pork MP's gel strength decreased. Furthermore, as the level of insect powder increased, the surface protein structure became rough and porous. The results demonstrated that proteins extracted from PB and TM larvae interfered with the gelation of pork MP in a gel system.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.21 no.5
• /
• pp.573-579
• /
• 1992

The influence of succinylation on several functional properties of fungal protein (Aspergillus fumigatus) was investigated. Fungal protein was succinylated to 20.7 and 85.3% by addition of 2.5 and 10% succinic anhydride, respectively. Succinylated fungal protein decreased the absorbance at 260nm, nucleic acid and carbohydrate, but increased the proteinous nitrogen and protein extraction in fungal protein. Succinylation had an enhancing effect on the functional properties as much as the degree of it was increased. Oil retention of succinylated fungal protein was higher about from two to five times than those of milk casein. Nitrogen solubility of succinylated fungal protein was increased to 32 and 51% than that of milk casein and soy flour. Emulsifying activity and stability were increased in proportion to the succinylated degree of fungal protein. As the result of succinylation increase more than 80%, emulsifying activity increased about 8.4 times. In conclusion, succinylated fungal protein improved functional properties, compared with nonsuccinylated fungal protein, milk casein and soy flour.

• Preventive Nutrition and Food Science
• /
• v.3 no.2
• /
• pp.175-179
• /
• 1998

Some functional properties and nutritive value were determined for the protein concentrated fractionated from chrysanthemum flower in orer to renew interest in the flowers as food. Proximate components of chrysanthemum flower protein concentration (FPC) showed 61.2% protein, 2.0% fat and 35.2% carbhydrate on a dry basis. In amino acid composition of FPC, glutamic acid was the highest in the content, follwoed by aspartic acid, leucine and lysine. The ratio of essential/ total amino acids(E/T) was 0.42, showing a higher level of essential amino acids compared to the FAO reference protein. Digestibility of chrysanthemum FPC by pepsin and trypsin was lwoer than that of casein and was negatively correlative to both water and fat absorptions. Similar characteristics were determined between chrysanthemum FPC and milk casein in their emulsifying activity and emulsion stability. This results indicate that flowers or petals of chrysanthemum might be developed as a good source of protein.