• 한국식품영양과학회지
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• 제34권9호
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• pp.1434-1442
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• 2005

수입산 밀가루(ASW+AH)와 쌀가루(오대)를 첨가한 혼합된에 transglutaminase를 첨가하여 반죽 물성 및 가공적 싶을 조사한 결과는 다음과 같다. Mixograph의 결과에서, 수입산 밀가루(ASW+AH)에 transglutaminase를 첨가한 mixograph 특성은 transglutaminase를 첨가할수록 각각 stability가 증가하다가 5,000 ppm 이상에서 감소하는 것으로 나타났다. 수입산 밀가루에 쌀가루(오대)를 첨가할수록 mixograph 패턴은 매우 불규칙하고 불안정한 패턴을 보여주고 있으며, stability, midline peak time, midline peak height, width at peak등의 파라메터 측정치와 특정한 관련성을 보이지 않았다. 그러나 수입산 밀가루(ASW+AH)와 쌀가루(오대)의 혼합분에 transglutaminase를 첨가함에 따라 이러한 불규칙성이 감소하였다. Farinograph의 결과에서, 수입산 밀가루(ASW+AH)에 첨가한 쌀가루(오대) 함량이 증가할수록 stability와 valormeter value는 급격히 감소하고 weakness는 크게 증가하여 매우 약하고 안정성이 낮은 반죽을 형성하였다. 그러나 transglutaminase를 첨가함에 따라 수입산 밀가루(ASW+AH)에 쌀가루(오대)를 첨가한 복합분의 stability와 valormeter value는 증가하였고, weakness는 감소하였다. 수분 흡수량은 대조군인 수입산 밀가루(ASW+AH)의 반죽에 비하여 쌀가루(오대) 혼합비율이 커질수록 증가하였으며, transglutaminase를 첨가함에 따라 수분 흡수량이 감소하는 경향을 가졌다. Peak time은 수입산 밀가루(ASW+AH)와 쌀가루(오대)를 첨가할수록 짧은 경 향을 나타내었으며, 두 반죽 모두 ttansglutaminase 를 첨가할수록 길어지는 경향을 나타내었다 조리면의 기계적 조직감을 Texture profile analysis(TPA)로 측정한 결과, 쌀가루(오대)를 첨가하여 제조한 혼합분(10, 30, $50\%$)에 transglutaminase(3000, 1000, 7000 ppm)를 첨가함에 따라 검성, 씹힘성, 견고성 등 TPA 파라메터 값이 증가하였고, 10,000 ppm 첨가시에는 비슷한 수치를 나타내거나 감소하였다. 관능평가 결과에서는 쌀가루를 $30\%$ 첨가한 혼합분으로 제조한 조리면의 조직감(씹힘성, 견고성)은 수입산 밀가루에 비해서 낮게 평가되었으나, transglutaminase를 7,000 ppm 첨가한 쌀 혼합분 조리면의 씹힘성이 향상되었다.

• 한국축산식품학회지
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• 제29권5호
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• pp.590-598
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• 2009

The aim of this study was to model and optimize the calcium alginate (CA) and microbial transglutaminase (TG) systems to form a cold-set myofibrillar protein (MP) gel containing 0.1 M or 0.3 M NaCl using a response surface methodology. The gel strengths of cold-set and heat-induced MP gels, and cooking yields were measured. All measured parameters showed determination coefficients ($R^2$) above 0.7 without a lack-of-fit. The CA system had the best results with component ratios of 1.0:0.3:1.0 corresponding to sodium alginate, calcium carbonate and glucono-$\delta$-lactone, respectively, and was favourable at 0.1 M NaCl. In contrast, the TG system only had an effect on cold-set MP gelation at 0.3 M salt, and the optimal ratio of TG to sodium caseinate was 0.6:0.5. By combining the two systems at 0.3 M NaCl, an acceptable cold-set MP gel with an improved texture and high cooking yield could be formed. Therefore, these results indicated that the functionality of the cold-set MP gel could be enhanced by combining these two optimized gelling system.

• 한국축산식품학회지
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• 제34권6호
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• pp.808-814
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• 2014

This study investigated the effect of gum arabic (GA) combined with microbial transglutaminase (TG) on the functional properties of porcine myofibrillar protein (MP). As an indicator of functional property, heat-set gel and emulsion characteristics of MP treated with GA and/or TG were explored under varying NaCl concentrations (0.1-0.6 M). The GA improved thermal gelling ability of MP during thermal processing and after cooling, and concomitantly added TG assisted the formation of viscoelastic MP gel formation. Meanwhile, the addition of GA decreased cooking yield of MP gel at 0.6 M NaCl concentration, and the yield was further decreased by TG addition, mainly attributed by enhancement of protein-protein interactions. Emulsion characteristics indicated that GA had emulsifying ability and the addition of GA increased the emulsification activity index (EAI) of MP-stabilized emulsion. However, GA showed a negative effect on emulsion stability, particularly great drop in the emulsion stability index (ESI) was found in GA treatment at 0.6 M NaCl. Consequently, the results indicated that GA had a potential advantage to form a viscoelastic MP gel. For the practical aspect, the application of GA in meat processing had to be limited to the purposes of texture enhancer such as restructured products, but not low-salt products and emulsion-type meat products.

• Asian-Australasian Journal of Animal Sciences
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• 제20권8호
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• pp.1285-1291
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• 2007

This research investigated variation in the improvement of the texture of chicken and pork sausages induced by microbial transglutaminase (MTG). The extractability of myofibrillar proteins from these sausages as well as the ${\varepsilon}-({\gamma}-glutamyl)$lysine (G-L)　content were also investigated. MTG treatment of sausages significantly increased the breaking strength values in both meat types, especially for samples incubated at $40^{\circ}C$. However, values of the breaking strength in both meat types were increased differently. The variation in protein extractability of samples incubated at $40^{\circ}C$ for both meat types could lead to some consideration of the mechanisms and the high accessions of myosin heavy chain (MHC) to MTG. SDS-PAGE analysis showed significant changes in the density of the bands after adding MTG, especially for the pork samples in which the bands disappeared totally. The G-L content in the presence of MTG was double that in control samples of both meat types. This study suggests that the binding ability of myofibrillar proteins with MTG is strong. This leads us to suggest that MTG functions positively with different improvements in the texture of chicken and pork products that are treated mechanically, such as sausages. Variability in gel improvement level between chicken and pork sausages was observed; this resulted from the variation in meat proteins in response to MTG, as well as to the original glutamyl and lysine content.

• Asian-Australasian Journal of Animal Sciences
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• 제16권2호
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• pp.269-276
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• 2003

We studied the gel properties of porcine collagen with microbial transglutaminase (MTGase) as a catalyst. A creep meter was used to measure the mechanical properties of gel. The results showed samples with high concentration of MTGase gelled faster than those with a low concentration of MTGase. The gel strength increased with incubation time and the peaks of breaking strength for 0.1, 0.2 and 0.5% MTGase were obtained at 40, 20 and 10 min incubation time, respectively. According to SDS-PAGE, the MTGase was successfully created a collagen polymer with an increase in molecular weight, whereas no change in formation was shown without MTGase. The sample with 0.5% MTGase began to polymerize after 10 or 20 min incubation at $50^{\circ}C$, and complete polymerization occurred after 40-60 min incubation. Scanning electron microscopic analysis revealed that the gel of porcine collagen in the presence of MTGase produced an extremely well cross-linked network. The differential scanning calorimetric analysis showed the peak thermal transition of porcine collagen gel was at $36^{\circ}C$, and that with MTGase no peak was detected during heating from 20 to $120^{\circ}C$. The melting point of porcine collagen gel could be controlled by MTGase concentration, incubation temperature and protein concentration. Knowledge of the structural and physicochemical properties of porcine collagen gel catalyzed with MTGase could facilitate their use in food products.

• 한국축산식품학회지
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• 제35권6호
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• pp.841-846
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• 2015

This study was investigated to determine the effect of microbial transglutaminase (MTG) with or without red bean protein isolate (RBPI) on the porcine myofibrillar protein (MP) gel functionality at different pH values (pH 5.75-6.5). Cooking yield (CY, %), gel strength (GS, gf), differential scanning calorimetry (DSC), and scanning electron microscopy (SEM) were determined to measure gel characteristics. Since no differences were observed the interaction between 1% RBPI and pH, data were pooled. CY increased with the addition of 1% RBPI, while it was not affected by pH values. GS increased with increased pH and increased when 1% RBPI was added, regardless of pH. There were distinctive endothermic protein peaks, at 56.55 and 75.02℃ at pH 5.75, and 56.47 and 72.43℃ at pH 6.5 in DSC results, which revealed decreased temperature of the first peak with the addition of 1% RBPI and increased pH. In SEM, a more compact structure with fewer voids was shown with the addition of 1% RBPI and increased pH from 5.75 to 6.5. In addition, the three-dimensional structure was highly dense and hard at pH 6.5 when RBPI was added. These results indicated that the addition of 1% RBPI at pH 6.5 in MTG-mediated MP represent the optimum condition to attain maximum gel-formation and protein gel functionality.

• 한국축산식품학회지
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• 제35권1호
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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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• 제31권1호
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• pp.129-137
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• 2018

Objective: The objective of this research was to evaluate the physico-chemical, microbiological and sensorial qualities of restructured steaks processed from beef trimmings (grade I and II) and frozen beef (fresh beef as control and frozen beef). Methods: Beef trimmings from commercial butcher were collected, designated into 4 treatments differing in beef trimmings grade and freezing, processed into restructured steaks with 1% microbial transglutaminase and then analyzed for product quality. Results: The results showed that all meat from different groups could be tightly bound together via cross-linking of myosin heavy chain and actin as observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Microbial counts of psychrotrophic and mesophilic bacteria were not affected by treatments (p>0.05), and no detectable of thermophilic bacteria were found. Regarding effect of beef trimmings grade, steaks made from beef trimmings grade II (16.03% fat) showed some superior sensorial qualities including higher tenderness score (p<0.05) and tendency for higher scores of juiciness and overall acceptability (p<0.07) than those made from beef trimmings grade I (2.15% fat). Moreover, a hardness value from texture profile analysis was lower in steaks processed from beef trimmings grade II than those made from grade I (p<0.05). Although some inferior qualities in terms of cooking loss and discoloration after cooking were higher in steaks made from beef trimmings grade II than those made from beef trimmings grade I (p<0.05), these differences did not affect the sensory evaluation. Frozen beef improved the soft texture and resulted in effective meat binding as considered by higher cohesiveness and springiness of the raw restructured product as compared to fresh beef (p<0.05). Conclusion: The results indicated the most suitable raw beef for producing restructured steaks without detrimental effect on product quality was beef trimmings grade II containing up to 17% fat which positively affected the sensory quality and that frozen beef trimmings increased tenderness and meat binding of restructured beef steaks.

• Asian-Australasian Journal of Animal Sciences
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• 제15권8호
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• pp.1204-1209
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• 2002

Polymerization of heated or unheated pig skin collagen using microbial transglutaminase (MTGase) was investigated. Pig skin collagen samples were heated or left unheated, then enzymatically polymerized with MTGase. SDS-PAGE was conducted to confirm the intermolecular polymer and the results showed similar bands between samples without MTGase and unheated samples with MTGase. The polymerized product of pig skin collagen was not formed in unheated samples, even when MTGase was added during incubation. Different results were obtained from samples heated at $80^{\circ}C$ and $100^{\circ}C$ for 2 min, whereas the SDS-PAGE pattern indicated that a polymer band was generated in both cases. The heat treatment successfully modified the native structure of collagen and also made collagen more reactable in the MTGase polymerization system. Scanning Electron Microscope (SEM) investigation of pig skin collagen showed a biopolymer structure through intermolecular collagen crosslinking, while there were no intermolecular crosslinks in samples not treated with MTGase. There were no significant differences in fibril diameter between treated samples and controls. These results suggest that heat treatment of native pig skin collagen enhanced the polymerization capability of MTGase.

• 한국축산식품학회지
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• 제44권3호
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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.