• Asian-Australasian Journal of Animal Sciences
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• 제19권7호
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• pp.1054-1058
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• 2006

The purpose of this study was to use pig blood plasma transglutaminase (TGase) combined with thrombin and fibrinogen as a binder, which was applied to restructured meat, and to investigate its effect on the restructured meat quality. Pig meat was obtained 10 h post mortem from a traditional market was ground using a 10 mm aperture plate. A binder admixture was added (TGase:thrombin:fibrinogen mixed as 0.5:1:20 (v/v/v) to which was added 12% of its volume of 0.25 M calcium chloride) at 0, 5, 10, 15 and 20% of meat weight. Measurements included cooking loss, shrinkage rate, shear value, total plate count, pH value, TBA value, color difference, tension strength and sensory evaluation. The results showed that ground meat containing 20% w/w of binder admixture had higher cooking loss, shrinkage rate and shear value (p<0.05). Addition of different percentages of binder admixture did not affect total plate count, pH value, TBA value, and sensory evaluation of restructured meat (p>0.05). Tension strength was increased with increased level of binder admixture. Addition up to 15% binder admixture to restructured meat showed better scores of sensory texture, flavor and total acceptability (p<0.05).

• Asian-Australasian Journal of Animal Sciences
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• 제19권1호
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• pp.137-143
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• 2006

The purpose of this study was to prepare a binder containing porcine blood transglutaminase (TGase), thrombin and fibrinogen. Extracted TGase, thrombin and fibrinogen were used alone or mixed with different proportions of their volume (v/v/v) by nine combinations as follows were 0.5:1:15, 0.5:1:20, 0.5:1:25, 1:1:15, 1:1:20, 1:1:25, 1.5:1:15, 1.5:1:20 and 1.5:1:25, respectively. Five ml of each combination were mixed with 0.6 ml of 0.25 M calcium chloride before experiment. After storage at 4C for 0, 1, 2, 3, 4 and 5 weeks, enzyme activity, total plate count, pH value, and SDS-PAGE of TGase, thrombin and fibrinogen were tested and pH value, clotting time and gel strength of the nine combination binders were determined. The results showed that total plate count of thrombin and pH value of TGase were significantly higher (p<0.05) than in other treatments. SDS-PAGE results showed that purified TGase, thrombin and fibrinogen from porcine blood plasma compared with commercial products (Sigma) had the same band patterns and nine different combination binders had no significant effect. Enzymatic activity of TGase and thrombin decreased as storage time increased. Total plate count of TGase, thrombin and fibrinogen and clotting time of the binder increased as storage time increased. The higher amount of fibrinogen in combinations, the stronger the gel strength.

• Bulletin of the Korean Chemical Society
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• 제33권1호
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• pp.100-104
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• 2012

Thrombin is a serine protease that catalyzes the conversion of soluble fibrinogen to insoluble fibrin, and thus induces physiological and pathological blood coagulation. Therefore, it is important to detect thrombin in blood serum for purposes of diagnosis. To achieve this goal, it has been suggested that a 15-mer aptamer strongly binds with thrombin to form a G-quartet structure of the aptamer. Generally, 5'-end thiol-functionalized aptamer has been used as an anti-thrombin binder. Herein, we evaluate the possibility of utilizing a 3'-SH aptasensor for thrombin detection using SPR spectroscopy, and compare the enhancement of the electrochemical signal of the thrombin-aptamer bound on a porous gold substrate. Although the two aptamers have similar configurations, in SPR analysis, the 3'-SH aptamer was a effective aptasensor as well as 5'-SH aptamer. Results from electrochemical analysis showed that the porous gold substrate acted as a good substrate for an aptasensor and demonstrated 5-fold enhancement of current change, as compared to gold thin film.