• Food Science of Animal Resources
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• v.39 no.2
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• pp.296-308
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• 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 Applied Biological Chemistry
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• v.42 no.4
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• pp.180-185
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• 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.

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

• Food Science of Animal Resources
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• v.30 no.6
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• pp.886-895
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• 2010

The level of fat and salt can affect the product quality and storage stability of processed meats. Additionally, consumers' demands require dietary guidelines for developing low-fat/salt functional foods. Microbial transglutaminase (MTGase), which enhances textural properties by catalyzing protein-protein cross-linkages, was introduced to develop healthier lowfat/salt meat products. The potential possibilities of low-fat/salt processed meats were reviewed under optimal conditions for functional ingredients from several previous studies. The addition of non-meat protein (e.g. sodium caseinate and soy protein isolates), hydrocolloids (e. g. konjac flour, carrageenan, and alginates), and MTGase alone or in combination with other functional ingredients improved textural and sensory properties similar to those of regularly processed meats. When MTGase was combined with hydrocolloids (konjac flour or sodium alginate) or other functional ingredients, gelling properties of meat protein were improved even at a low salt level. Based on these reviews, functional ingredients combined with new processing technologies could be incorporated into processed meats to improve the functionality of various low-fat/salt meat products.

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

• International Journal of Industrial Entomology and Biomaterials
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• v.48 no.2
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• pp.86-97
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• 2024

Alkaline- or salt-assisted extractions have been widely used to extract edible insect proteins, however, there is a need for extraction techniques that balance cost-efficient production as well as preserving the protein properties. Mealworm proteins (Tenebrio molitor larvae) were extracted using three different extraction methods-alkali (AMP), salt (SMP), and water (WMP)-and then physicochemical and techno-functional properties were examined. AMP had high yield, protein, and amino acid contents, whereas WMP had high moisture, ash, and fat contents. SDS-PAGE showed a wide range of molecular weights in WMP whereas mostly low molecular weights were observed in AMP and SMP. AMP had poor protein solubilities compared to SMP and WMP across all pHs. AMP had enhanced water-holding capacity and emulsion stability, whereas WMP had improved oil-holding capacity and foaming properties. WMP formed a gel with and without the transglutaminase. The physicochemical and techno-functional properties demonstrated that water-soluble mealworm protein was superior to alkali-and salt-soluble mealworm proteins. Considering the cost efficiency and minimal impact on the environment as well, a cold press juicer could be utilized for mass production of mealworm protein compared to the conventional methods of protein extraction using alkali and salt.

• Food Science and Preservation
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• v.31 no.3
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• pp.346-359
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• 2024

Although ovalbumin makes up 54% of the total egg white proteins, individual protein usage is rare. The primary applications of ovalbumin in the food industry relate to other proteins, such as whole egg whites. Ovalbumin has remarkable functional properties, such as those of gelation, foaming, and emulsification, which are crucial in the processing of food, however, its application as a standalone functional protein is severely constrained due to separation issues. In recent years, new methodologies for the large-scale separation of ovalbumin have emerged. Meantime, ovalbumin was identified as a good source to produce bioactive peptides with a variety of functional properties, including antibacterial, antioxidant, and angiotensin-converting-enzyme inhibitory actions, according to research. Newly discovered bioactive peptides from ovalbumin can be used in the food sector in addition to their well-known functional properties to create health-promoting products. Benefits extend beyond the food business to numerous other sectors, such as the pharmaceutical and cosmetic industries. Consequently, a gap between the existing and prospective future uses is found. The main goals of this study were to determine some possible factors for the long-term neglect of the major protein and to determine the growing potential for applications of ovalbumin and peptides.

• Food Science and Biotechnology
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• v.18 no.4
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• pp.889-894
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• 2009

Barley proteins are expected to have unique functional properties due to their high content of alcohol soluble protein, hordein. Since the barley proteins obtained by conventional isoelectric precipitation method cannot represent hordein fraction, barley proteins were fractionated to albumin, globulin, glutelin, and hordein with respect to extraction solvents. Functional properties and film-forming properties of solubility-fractionated barley proteins were investigated to explore their potential for human food ingredient and industrial usage. The 100 g of total barley protein comprised 5 g albumin, 23 g globulin, 45 g glutelin, and 27 g hordein. Water-binding capacities of barley protein isolates ranged from 140-183 mL water/100 g solid. Hordein showed the highest oil absorption capacity (136 mL oil/100 g), and glutelin showed the highest gelation property among the fractionated proteins. In general, the barley protein fractions formed brittle and weak films as indicated by low tensile strength (TS) and percent elongation at break (E) values. The salt-soluble globulin fraction produced film with the lowest TS value. Although films made from glutelin and hordein were dark-colored and had lower E values, they could be used as excellent barriers against water transmission.

• Preventive Nutrition and Food Science
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• v.11 no.1
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• pp.73-77
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• 2006

Ground pork was irradiated with an electron beam (e-beam) at a dose of 0, 1.5, 3, 5 and 10 kGy and the changes in various functional and other associated properties of salt-soluble proteins extracted from the pork were evaluated. Irradiation did not affect turbidity and the disulfide content of pork salt-soluble protein, but the content of sulfhydryls and the hydrophobocity of salt-soluble protein increased. This indicates that protein degradation occurred when the pork was e-beam irradiated and that the sulfhydryls and hydrophobic moieties buried inside the proteins were exposed to the outside environment. However, these degraded protein molecules did not form large protein aggregates through disulfide bridges. The emulsifying capacity of the pork increased with irradiation, which could be the result from increased hydrophobicity of pork salt-soluble protein. Water holding capacity of pork was not affected bye-beam irradiation.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.3
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• pp.219-223
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• 1990

Myofibrillar protein from Alaska pollack was modified with acetic anhydride at pH 7.5 and $25^{\circ}C$ and changes in functional properties as affected by the degree of modification were determined. Acetylation of myofibrillar protein resulted in protein with unique functional properties dependent upon the degree of acetylation. By selecting appropriate degree of modification it was possible to control protein solubility heat coagulability calcium precipitability foaming and emulsion capa-city.