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

• Food Science of Animal Resources
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• v.39 no.4
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• pp.576-584
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• 2019

This study was performed to evaluate the physicochemical properties of myofibrillar protein (MP) gels containing pork skin gelatin at different salt concentrations. MP gels were prepared to the different salt levels (0.15, 0.30, and 0.45 M) with or without 1.0% of pork skin gelatin. Cooking yield (CY), gel strength, shear stress were measured to determine the physical properties, and SDS-polyacrylamide gel electrophoresis, scanning electron microscopy, fourier transform infrared spectroscopy, sulfhydryl group and protein surface hydrophobicity was performed to figure out the structural changes among the proteins. The addition of gelatin into MP increased CYs and shear stress. MP at 0.45 M salt level had the highest CY and shear stress, as compared to MPs at lower salt concentrations. As the salt concentration of MP gels increased, the microstructure became the compact and wet structures, and decreased the amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$. MP with gelatin showed a decreased amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$ compared to MP without gelatin. The addition of gelatin to MP did not affect the sulfhydryl group, but the sulfhydryl group decreased as increased salt levels. MP mixtures containing gelatin showed a higher hydrophobicity value than those without gelatin, regardless of salt concentration. Based on these results, the addition of gelatin increased viscosity of raw meat batter and CY of MP gels for the application to low salt meat products.

• Korean Journal of Food Science and Technology
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• v.23 no.4
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• pp.428-432
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• 1991

This study was carried out to investigate the effect of NaCl, pH and phosphate on the functional properties of a mixed system of plasma protein and myofibrillar proteins. The solubility of plasma protein, myofibrillar protein and the mixture (plasma+myofibrillar protein) increased according to the increase of NaCl concentration ($0{\sim}4%$) and pH $pH4{\sim}8$). The solubility, emulsifying activity and capacity of the mixture were lower than those of plasma protein, whereas higher than those of myofibrillar protein. The gel strength of the mixture and myofibrillar protein showed a significant increase when NaCl concentration was increased from 2 to 3%. The gel strength of myofibrillar protein increased about four times when 0.3% polyphosphate added to the sample containing 2% NaCl, whereas the moisture loss of the mixture and myofibrillar protein decreased significantly. The gel strength of plasma protein, myofibrillar protein and the mixture increased slightly at $3{\sim}5%$ protein concentration, whereas the gel strength of those increased significantly as the protein concentration increased from 5 to 9%.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.229-239
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• 2019

The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.

• Korean Journal of Food Science and Technology
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• v.25 no.3
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• pp.295-298
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• 1993

This study was carried out to investigate the effects of heating temperature, heating time and protein concentration on the gel properties and heat stability of a mixed system of pork plasma and myofibrillar to increase the utility of porcine blood as protein resources of the food industry, especially meat processing industry. The solubility of plasma protein and mixture (plasma + myofibrillar protein) decreased significantly at $70^{\circ}C\;to\;90^{\circ}C$ when heating temperature rised, whereas myofibrillar protein decreased slightly at $40^{\circ}C\;to\;60^{\circ}C$, and the gel strength and the turbidity of those increased significantly at these heating temperatures. The solubility of plasma protein and mixture decreased when the heating time increased at $75^{\circ}C$, whereas the gel strength and turbidity increased, and the solubility, the gel strength and the turbidity of myofibrillar protein showed no changes.

• Food Science of Animal Resources
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• v.40 no.2
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• pp.254-261
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• 2020

The aim of this study was to evaluate quality characteristics of pork myofibrillar protein (MP) added with cornstarch as affected by different pH values and salt cocnentrations. MP mixtures were prepared with three different pH values (pH 6.00, 6.25, and 6.50) and three different salt concentrations (0.15, 0.30, and 0.45 M). Cooking yield (CY), gel strength, viscosity, and scanning electron microscopy were measured to evaluate characteristics of MPs. CYs of MPs with cornstarch at above pH 6.25 or salt 0.30 M were increased compared to those at pH 6.00 or salt 0.15 M. However, gel strengths of MPs at salt 0.45 M were higher than those at salt 0.30 M. In microstructure analysis, MP gels with increasing pH value and salt concentration showed compact and uniform structure. Thus, MP gels with pH 6.25 and salt concentration of 0.30 M would be better for manufacturing meat products containing cornstarch to increase their water holding ability.

• Food Science of Animal Resources
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• v.35 no.1
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• pp.50-57
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• 2015

Fish sarcoplasmic protein (SP) is currently dumped as waste from surimi industry and its recovery by practical method for being the non-meat ingredient in meat industry would be a strategy to utilize effectively the fish resource. This study was aimed to apply pH treatment for fish SP recovery and evaluated its effect on pork myofibrillar protein (MP) gel. The pH values of fish SP were changed to 3 and 12, and neutralized to pH 7 before lyophilizing the precipitated protein after centrifugation. Acid-treated fish SP (AFSP) showed about 4-fold higher recovery yield than that of alkaline-treated SP and water absorption capacity was also about 1.2-fold greater. Because of the high recovery yield and water absorption capacity, AFSP was selected to incorporate into MP with/without microbial transglutaminase (MTG). The effects of AFSP and MTG on the physicochemical and rheological characteristics of MP and MP gel were evaluated. MTG induced an increase shear stress of the MP mixture and increase the breaking force of MP gels. MP gel lightness was decreased by adding AFSP. MP gel with MTG showed higher cooking loss than that without MTG. A reduction of cooking loss was observed when the AFSP was added along with MTG, where the insoluble particles were found. Therefore, AFSP could be contributed as a water holding agent in meat protein gel.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.1
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• pp.144-151
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• 2019

Objective: Curdlan has been widely used as a gelling agent in various food systems. This study was performed to evaluate the rheological properties of pork myofibrillar protein (MP) with different levels of curdlan (0.5% to 1.5%) and its application to low-fat model sausages (LFS). Methods: MP mixtures were prepared with 0.5%, 1.0%, and 1.5% of curdlan. Cooking loss (%), gel strength (gf), shear stress (Pa), and scanning electron microscopy were measured. Physicochemical and textural properties of LFS containing different levels of curdlan were measured. Results: The shear stress of MP mixtures increased with increasing levels of curdlan. MP gels with increased levels of curdlan decreased cooking loss and increased gel strength (p<0.05). The MPs with 1.0% and 1.5% of curdlan were observed more compact three-dimensional structure than those with 0.5% curdlan. Increased curdlan level in LFS affected redness ($a^{\star}$) and yellowness ($b^{\star}$) values. Although expressible moisture of LFS did not differ among curdlan levels, LFSs with various levels of curdlan decreased cooking loss as compared to control sausages. Hardness values (2,251 to 2,311 gf) of LFS with 0.5% and 1.0% curdlan was increased and differ from those (1,901 gf) of control sausages. Conclusion: The addition of 1.0% curdlan improved the functional and textural properties of LFS.

• Food Science of Animal Resources
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• v.44 no.3
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• pp.586-606
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• 2024

The study was performed to determine the effect of faba bean protein isolate (FBPI) alone or in combination with microbial transglutaminase (MTG) on the rheological properties of pork myofibrillar protein gel (MPG), and physiochemical and textural properties of reduced-salt, low-fat pork model sausages (LFMSs). The cooking yields of MPGs with MTG or FBPI alone decreased and increased, respectively. However, the combination of FBPI and MTG was similar to the control (CTL) without FBPI or MTG. Gel strength values of MPG added with both FBPI and MTG were higher than treatments with FBPI or MTG alone. The hydrophobicity values of CTL were lower than those of MPG with FBPI alone, whereas the addition of MTG decreased the hydrophobicity of MPGs. The incorporation of FBPI alone or in combination with MTG decreased sulfhydryl groups (p<0.05). Shear stress values of MPGs with MTG tended to be higher than those of non-MTG treatments at all shear rates, and the addition of FBPI into MPGs increased shear stress values. Reduced-salt (1.0%) LFMSs with FBPI alone or combined with MTG had both lower cooking loss and expressible moisture values than those of CTL and similar values to the reference sample (REF, 1.5% salt). Textural properties of reduced-salt LFMSs with FBPI or MTG were similar to those of REF. These results demonstrated that the combination of FBPI and MTG could improve the water binding capacity and textural properties of pork MPGs and LFMSs and might be suitable for application in the development of healthier meat products.

• 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.