• Korean Journal of Food Science and Technology
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• v.25 no.6
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• pp.632-636
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• 1993

Gel strength of fish protein at various processing conditions such as heating temperature, heating time and salt content was determined by using compressive stress and residual delay time of ultrasonic wave. The compressive stress, interpreted as indicating the relative gel strength, was increased with increasing the heating temperature and heating time, and with decreasing the salt content, while the delay time of ultrasonic wave reduced, indicating that the gel strength and the delay time are inverse proportion. The result of the multiple regression analysis with factorial design showed that the model equation consisted with delay time and processing condition variables gave the good prediction of the gel compressive stress which was coincided with compressive stress measured.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.2
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• pp.187-194
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• 1992

Rhizopus oryzae CJ-2114 was selected for its strong polygalacturonase activity among various strains of mold found in soil. It was found that the production of polygalacturonase reached to maximum when the wheat bran medium containing 1% albumin, 1% sorbitol and 0.2% (NH$_4$)$_2$C$_2$O$_4$was cultured for 96 hrs at 3$0^{\circ}C$. Polygalacturonase was purified 11.13 fold from Rhizopus oryzae CJ-2114. The purification procedures include ammonium sulfate treatment, gel filtration on Sephadex G-75, G-150 and DEAE-cellulose ion exchange chromatography. Yield of the enzyme purification was 40.3% .Purified enzyme was confirmed as a single band by the polyacrylamide gel electrophoresis. When the purified enzyme was applied to SDS-poly-acrylamide gel electrophoresis, the molecular weight was estimated to be 47,000. The amino acid composition indicated relatively high contents of glutamic acid and glyrine.

• 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.

• Food Science of Animal Resources
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• v.40 no.4
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• pp.588-600
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• 2020

The effect of age (22, 30, 38, and 46 days) on Beijing duck breast myosin gels was investigated. The results showed that the water holding capacity (WHC) and gel strength were markedly improved at the age of 30 days. Differential scanning calorimetry suggested that the myosin thermal ability increased at the age of 30 and 38 days (p<0.05). A compact myosin gel network with thin cross-linked strands and small regular cavities formed at the age of 30 days, which was resulted from the higher content of hydrophobic interactions and disulfide bonds. Moreover, the surface hydrophobicity of myosin extracted from a 30-day-old duck breast decreased significantly under temperature higher than 80℃ (p<0.05). This study illustrated that myosin extracted from a 30-day-old duck's breast enhanced and stabilized the WHC, thermal stability and molecular forces within the gel system. It concluded that age is an essential influencing factor on the myosin thermal stability and gel quality of Beijing duck due to the transformation of fibrils with different myosin character.

• Food Science of Animal Resources
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• v.30 no.5
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• pp.746-754
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• 2010

Response surface methodology was adopted to model and optimize the effects of microbial transglutaminase (TG) and calcium alginate (CA) systems of various ratios on the gelation characteristics of porcine myofibrillar protein (MP) at various salt levels. The CA system consisting of sodium alginate (SA), calcium carbonate (CC) and glucono-$\delta$-lactone (GdL) showed no remarkable changes in the salt-soluble fraction, and only minor effects on electrostatic interactions were observed. Increasing CA concentration caused acid-induced hydrophobic interactions in MPs, resulting in increased MP gel strength. The TG system, containing TG and sodium caseinate (SC), induced cold-set MP gelation by formation of covalent bonding. The main advantage of the combined system was a higher cooking yield when the MP gel was heated. These results indicated that 0.7% TG combined with 0.8% CA system can form a viscoelastic MP gel, regardless of salt levels.

• Food Science of Animal Resources
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• v.31 no.6
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• pp.817-826
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• 2011

The technological effects of Makgeolli lees fiber (0, 0.5, 1.0, 2.0, and 4.0%) on chicken salt-soluble breast meat proteins in a model system on proximate composition, physicochemical properties, and textural properties were investigated. Makgeolli lees fiber was obtained from Makgeolli brew processing, and the by-products showed good dietary fiber. The moisture and ash contents, water holding capacity, redness, yellowness, hardness, and apparent viscosity of chicken salt-soluble meat protein heat-induced gel systems with Makgeolli lees fiber were all higher than the control without Makgeolli lees fiber. However, protein solubility and electrophoretic patterns did not differ among the control and treatments with Makgeolli lees fiber samples. The chicken salt-soluble protein heat-induced gel systems incorporating Makgeolli lees fiber had improved water holding capacity, textural properties, and viscosity due to Makgeolli lees fiber addition. These results suggest that the addition of 4.0% Makgeolli lees fiber to gel is helpful to improve the physical properties of heat-induced gels.

• Korean Journal of Agricultural Science
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• v.10 no.1
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• pp.156-165
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• 1983

This experiment was carried out to elucidate the drying characteristics of onion and dehumidifying effect of air using the silica gel and to reuse it by solar collector. The results were summarized as follows. 1. It takes 14hours to regenerate to silica gel of 8% moisture content from saturated silica gel in conditions of $28^{\circ}c$ temperature and 55% relative humidity. 2. When sample was recycled through solar collector, the result of drying was 1/2 times more efficient than that of mat drying. 3. Average thermal efficiency of solar collector was 25% during the experimental period. 4. Browning extent was reduced to 1/2 times at heated air blow drying system using drying chamber.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.5
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• pp.803-810
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• 1995

Co-immobilized mixed culture system(A-Z system) composed of two different oxygen-demanding strains, aerobic(Aspergillus awamori) and anaerobic(Zymomonas mobilis) strains, in a Ca-alginate gel beads was developed to increase ethanol production from raw starch as a carbon source. Optimal mixture ratio of A. awamori and Z. mobilis was $1.25{\times}10^{9}\;spores/L-gel$ and 0.5g cells/L-gel, respectively. After 120 hours of cultivation, gel beads distinguished oxygen-rich surface for A. awamori from oxygen-deficient central part for Z. mobilis. At A-Z culture system, yield of ethanol on glucose, $Y_{p/s}=0.18$, was very low and there was high leakage of cells from surface of gel beads. At A-Z 36 cultrue system with changing silicon check valve for cotton plug at 36 hours in A-Z culture system, there was no cell leakage from gel beads, pH was maintained at around 4.3 during cultivation, and yield of ethanol on glucose, $Y_{p/s}=0.36$, showed 2 times higher than that of control culture system(cotton plug culture).

• Food Science and Preservation
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• v.30 no.4
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• pp.589-601
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• 2023

Malaysian honey is rich in nutrients and bioactive compounds, which can be a healthy alternative to refined sugar in food production. However, liquid honey's viscous and sticky nature makes it unpreferable in industrial handling. This study, an atomization system coupled with vacuum drying to produce honey powders to overcome the problem. Three types of Malaysian honey, namely Acacia, Gelam, and Tualang, were encapsulated in Ca-alginate gel beads using the atomization system. The density viscosity, and surface tension of the honey-alginate solutions were measured, and the concentration of honey and alginate influenced the physical properties of the solutions. Honey-encapsulated gel beads in the size range of 2.16-2.92 mm were produced using the atomization system with the air-liquid mass flow rate ratios of 0.22-0.31, Weber number (We) of 112-545, and Ohnersorges number (Oh) of 0.35-10.46. Gel bead diameter can be predicted using a simple mathematical model. After vacuum drying, the honey gel powder produced was in the size range of 1.50-1.79 mm. Results showed that honey gel powders with good encapsulation efficiency and high honey loading could be produced using the atomization system and vacuum drying.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.5
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• pp.721-733
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• 2019

Objective: The objectives of this study were to investigate the thermal gelation properties and molecular forces of actomyosin extracted from two classes of chicken breast meat qualities (normal and pale, soft and exudative [PSE]-like) during heating process to further improve the understanding of the variations of functional properties between normal and PSE-like chicken breast meat. Methods: Actomyosin was extracted from normal and PSE-like chicken breast meat and the gel strength, water-holding capacity (WHC), protein loss, particle size and distribution, dynamic rheology and protein thermal stability were determined, then turbidity, active sulfhydryl group contents, hydrophobicity and molecular forces during thermal-induced gelling formation were comparatively studied. Results: Sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed that protein profiles of actomyosin extracted from normal and PSE-like meat were not significantly different (p>0.05). Compared with normal actomyosin, PSE-like actomyosin had lower gel strength, WHC, particle size, less protein content involved in thermal gelation forming (p<0.05), and reduced onset temperature ($T_o$), thermal transition temperature ($T_d$), storage modulus (G') and loss modulus (G"). The turbidity, reactive sulfhydryl group of PSE-like actomyosin were higher when heated from $40^{\circ}C$ to $60^{\circ}C$. Further heating to $80^{\circ}C$ had lower transition from reactive sulfhydryl group into a disulfide bond and surface hydrophobicity. Molecular forces showed that hydrophobic interaction was the main force for heat-induced gel formation while both ionic and hydrogen bonds were different significantly between normal and PSE-like actomyosin (p<0.05). Conclusion: These changes in chemical groups and inter-molecular bonds affected protein-protein interaction and protein-water interaction and contributed to the inferior thermal gelation properties of PSE-like meat.