• Food Science of Animal Resources
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• v.22 no.2
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• pp.179-182
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• 2002

Using differential scanning calorimetry (DSC), changes underwent by a mixture of $\alpha$-lactalbumin ($\alpha$-La) and $\beta$-lactoglobulin ($\beta$-Lg) during heat treatment were studied, yielding useful information for the dairy industry. Results of the DSC showed that the heat denaturation temperature of the hobo-$\alpha$-La was higher than that of apo-$\alpha$-La, suggesting hole-$\alpha$-La‘s greater stability. The denaturation temperature of a mixture of holo-$\alpha$-La and $\beta$-Lg was also slightly lower than that of holo-$\alpha$-La alone. The denaturation temperature of an apo-$\alpha$-La and $\beta$-Lg mixture was higher than that of holo-$\alpha$-La and $\beta$-Lg, suggesting that the heat stability of apo-$\alpha$-La was increased by $\beta$-Lg. Based on these results, it is possible to conclude that a mixture of holo-$\alpha$-La and $\beta$-Lg is more intensively affected by an increase in temperature than other samples, and that free sulphydryl groups seem to take part in this heat-induced denaturation.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.6
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• pp.898-904
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• 2006

Effects of sodium bicarbonate (SBC) injection on meat quality and functionality of porcine M. longissimus lumborum were investigated. Fifteen pigs ($100{\pm}5kg$) were randomly selected at a commercial slaughter plant. After slaughtering the loins were dissected from the carcass before chilling at approximately 30 minutes post mortem. The loins were divided into four cuts for sample treatment, and SBC of 0.25 M, 0.40 M and 0.75 M was injected (2% w/w) using a syringe. As SBC injection level was increased, muscle pH increased significantly (p<0.05). SBC injection decreased lightness ($L^*$) values on the surface of muscle. Moreover, with injection of SBC, drip loss %, cooking loss % and shear force were significantly (p<0.05) decreased, whereas WHC and $Na^+$ content were significantly (p<0.05) increased. From panel testing of uncooked pork loin, no significant differences (p>0.05) were found in aroma, off-flavor and drip between injection of SBC at different levels and the control, although color and acceptability were significantly lower (p<0.05) in control pork loin compare with injection of SBC at 0.75 M. In cooked pork loin from the panel test, aroma, flavour, off-flavour and juiciness were found to be similar (p>0.05) on all treatments, but tenderness and acceptability were significantly higher (p<0.05) with injection of SBC at 0.75 M than for control loin. Myofibrillar protein solubility of muscles treated with SBC was significantly (p<0.05) higher than that of the control, although no significant differences (p>0.05) were found in sarcoplasmic protein solubility between the treatments. These results indicated that SBC injection into pre-rigor porcine M. longissimus lumborum could improve ultimate pork quality characteristics such as meat color, water-holding capacity, and could inhibit muscle protein denaturation due to an increase in muscle pH.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.8
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• pp.1186-1194
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• 2019

Objective: The influence of broiler carcass scalding conditions on chicken breast meat quality parameters was investigated. Methods: Two hundred and seventy Cobb broiler chickens from 42 to 48 days old were slaughtered according to the standard industry practice and scalded in five temperature/time combinations-$T_1$, $54^{\circ}C/210s$; $T_2$, $55^{\circ}C/180s$; $T_3$, $56^{\circ}C/150s$; $T_4$, $57^{\circ}C/120s$; $T_5$, $58^{\circ}C/90s$. Results: Scalding temperature increase resulted in higher values of external and ventral lightness and in protein functionality reduction-determined by emulsification capacity and protein denaturation-in chicken breast fillets 24 h post-mortem. Protein secondary structures had conformational changes, with a decrease of the ${\alpha}$-helix and an increase of the ${\beta}$-sheet and ${\beta}$-turn proportions, mainly in $T_1$ and $T_5$ samples, determined by Fourier-transform infrared spectroscopy in an attenuated reflectance mode analysis. The chemical composition, pH, water holding capacity and Warner-Bratzler shear force did not differ among the treatments. In the fatty acid profile, the 18:1n-9 was lower in $T_5$, which suggested that the high scalding-temperature could have caused the lipid oxidation. The values of the polyunsaturated fatty acids (PUFA), such as 22:2, 20:4n-6, and 22:6n-3, were highest in the $T_5$, thus being related to the phospholipid cellular membrane collapse in this experimental condition and subsequent release of these PUFA. Conclusion: Intermediate scalding-parameters avoided the negative changes in the chicken meat quality.

• Journal of the Korea Organic Resources Recycling Association
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• v.6 no.1
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• pp.43-52
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• 1998

The objective of this study is to investigate the optimum conditions of extracting collagen without chrome ion from the leather waste. The effect of temperature, pH, and the concentration of alkaline solution on the collagen extraction has been studied. The result indicated that the incipient denatured temperature of collagen measured by viscosity was $25^{\circ}C$ and the complete denatured temperature was $31.5^{\circ}C$. The optimum solubilization condition for temperature was between $15^{\circ}C$ and $20^{\circ}C$, pH was 1.5, the concentration of alkaline solution was 3% of sodium hydroxide. The almost complete chrome ion separation was possible around the pH of 1.5. The separation efficiency of chrome ion from tannery waste was more than 99.5%. Extraction efficiency of crude protein from leather waste was about 89.5%. The hydroxyproline and collagen content in the extracted crude protein were 8.53% and 63.62%, respectively.

• BMB Reports
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• v.35 no.2
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• pp.155-164
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• 2002

The structural aspects of ervatamin B have been studied in different types of alcohol. This alcohol did not affect the structure or activity of ervatamin B under neutral conditions. At a low pH (3.0), different kinds of alcohol have different effects. Interestingly, at a certain concentration of non-fluorinated, aliphatic, monohydric alcohol, a conformational switch from the predominantly $\alpha$-helical to $\beta$-sheeted state is observed with a complete loss of tertiary structure and proteolytic activity. This is contrary to the observation that alcohol induces mostly the $\alpha$helical structure in proteins. The O-state of ervatamin B in 50% methanol at pH 3.0 has enhanced the stability towards GuHCl denaturation and shows a biphasic transition. This suggests the presence of two structural parts with different stabilities that unfold in steps. The thermal unfolding of ervatamin B in the O-state is also biphasic, which confirms the presence of two domains in the enzyme structure that unfold sequentially. The differential stabilization of the structural parts may also be a reflection of the differential stabilization of local conformations in methanol. Thermal unfolding of ervatamin B in the absence of alcohol is cooperative, both at neutral and low pH, and can be fitted to a two state model. However, at pH 2.0 the calorimetric profiles show two peaks, which indicates the presence of two structural domains in the enzyme with different thermal stabilities that are denatured more or less independently. With an increase in pH to 3.0 and 4.0, the shape of the DSC profiles change, and the two peaks converge to a predominant single peak. However, the ratio of van't Hoff enthalpy to calorimetric enthalpy is approximated to 2.0, indicating non-cooperativity in thermal unfolding.

• BMB Reports
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• v.35 no.2
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• pp.143-154
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• 2002

The structural and functional aspects of ervatamin B were studied in solution. Ervatamin B belongs to the $\alpha+\beta$ class of proteins. The intrinsic fluorescence emission maximum of the enzyme was at 350 nm under neutral conditions, and at 355 nm under denaturing conditions. Between pH 1.0-2.5 the enzyme exists in a partially unfolded state with minimum or no tertiary structure, and no proteolytic activity. At still lower pH, the enzyme regains substantial secondary structure, which is predominantly $\beta$-sheet conformation and shows a strong binding to 8-anilino-1-napthalene-sulfonic acid (ANS). In the presence of salt, the enzyme attains a similar state directly from the native state. Under neutral conditions, the enzyme was stable in urea, while the guanidine hydrochloride (GuHCl) induced equilibrium unfolding was cooperative. The GuHCl induced unfolding transition curves at pH 3.0 and 4.0 were non-coincidental, indicating the presence of intermediates in the unfolding pathway. This was substantiated by strong ANS binding that was observed at low concentrations of GuHCl at both pH 3.0 and 4.0. The urea induced transition curves at pH 3.0 were, however, coincidental, but non-cooperative. This indicates that the different structural units of the enzyme unfold in steps through intermediates. This observation is further supported by two emission maxima in ANS binding assay during urea denaturation. Hence, denaturant induced equilibrium unfolding pathway of ervatamin B, which differs from the acid induced unfolding pathway, is not a simple two-state transition but involves intermediates which probably accumulate at different stages of protein folding and hence adds a new dimension to the unfolding pathway of plant proteases of the papain superfamily.

• Journal of Pharmaceutical Investigation
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• v.39 no.6
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• pp.423-429
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• 2009

Liposomes have been used as one of the efficient carriers for drug delivery. In this study, anionic liposomes of which surface was modified by using both electrostaic interaction between anionic liposomes and cationically charged BSA molecules at lower pH than isoelectric point (pI) of BSA and denaturation of the BSA-coated liposomes by thermal treatment. The thermally denatured BSA-coated liposomes (DBAL) had mean particle diameter of 125.2${\pm}$1.7 nm and zeta potential value of -22.4${\pm}$4.5 mV. Loading efficiency of model drug, doxorubicin (DOX), into liposomes was 83.0${\pm}$2.6%. Results of in vitro stability study of DBAL in blood plasma showed that the mean particle diameter of DBAL 400 did not increase in blood plasma and adsorption of plasma protein was much less than plain or anionic liposomes. Intracellular uptake of DBAL 400 evaluated by confocal microscopy observation was higher than that of PEG liposomes.

• Food Science of Animal Resources
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• v.36 no.5
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• pp.583-593
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• 2016

The aim of this study was to investigate the effects of morphological characteristics of porcine muscle fibers on growth performance, muscle fiber characteristics, and pork quality taken from the longissimus dorsi muscle. A total of 239 crossbred pigs (164 castrated males and 75 females) were used in this study. Experimental pigs were categorized by the total number of muscle fiber (TNF: High and Low) and cross sectional area of muscle fiber (CSAF: Large, Middle, and Small). Their combinations were classified into six groups (High-Large, HL; High-Middle, HM; High-Small, HS; Low-Large, LL; Low-Middle, LM; Low-Small, LS). The TNF and CSAF were significantly (p<0.05) correlated with growth rate and carcass productivity, while the only of the type I number had no meaningful relationships excluding the correlation with loin area (p<0.001). The proportion of type I area was positively correlated with pH_{45 min} while the proportion of type IIB area was negatively correlated with pH_{45 min} and pH_{24 h} (p<0.05). Drip loss and protein denaturation had strong relationships with the proportion of type IIB number or area. The HL group exhibited the greatest growth performance. In addition, the HL group had significantly greater values in protein solubility than the other groups. In conclusion, this study suggest that high TNF combined to large CSAF improve the ultimate lean meat productivity and assure normal meat quality simultaneously with increased both proportion of number and area of type I, type IIA muscle fibers and lowered proportion of number and area of type IIB.

• Asian-Australasian Journal of Animal Sciences
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• v.32 no.5
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• pp.701-710
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• 2019

Objective: This study investigated the effect of different acute heat stress (HS) levels on chicken meat quality and ultra-structure. Methods: Chickens were randomly divided into 7 groups to receive different HS treatments: i) $36^{\circ}C$ for 1 h, ii) $36^{\circ}C$ for 2 h, iii) $38^{\circ}C$ for 1 h, iv) $38^{\circ}C$ for 2 h, v) $40^{\circ}C$ for 1 h, vi) $40^{\circ}C$ for 2 h, and vii) un-stressed control group ($25^{\circ}C$). Blood cortisol level, breasts initial temperature, color, pH, water holding capacity (WHC), protein solubility and ultra-structure were analyzed. Results: HS temperatures had significant effects on breast meat temperature, lightness ($L^*$), redness ($a^*$), cooking loss and protein solubility (p<0.05). The HS at $36^{\circ}C$ increased $L^*{_{24h}}$ value (p<0.01) and increased the cooking loss (p<0.05), but decreased $a^*{_{24h}}$ value (p<0.05). However, as the temperature increased to $38^{\circ}C$ and $40^{\circ}C$, all the values of $L^*{_{24h}}$, cooking loss and protein denaturation level decreased, and the differences disappeared compared to control group (p>0.05). Only the ultimate $pH_{24h}$ at $40^{\circ}C$ decreased compared to the control group (p<0.01). The pH in $36^{\circ}C$ group declined greater than other heat-stressed group in the first hour postmortem, which contributed breast muscle protein degeneration combining with high body temperature, and these variations reflected on poor meat quality parameters. The muscle fiber integrity level in group $40^{\circ}C$ was much better than those in $36^{\circ}C$ with the denatured position mainly focused on the interval of muscle fibers which probably contributes WHC and light reflection. Conclusion: HS at higher temperature (above $38^{\circ}C$) before slaughter did not always lead to more pale and lower WHC breast meat. Breast meat quality parameters had a regression trend as HS temperature raised from $36^{\circ}C$. The interval of muscle fibers at 24 h postmortem and greater pH decline rate with high body temperature in early postmortem period could be a reasonable explanation for the variation of meat quality parameters.

• Applied Biological Chemistry
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• v.36 no.3
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• pp.163-171
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• 1993

The collagens from filefish (Novoden modestus) and cod (Gadus macrocephalus Tilesius) skin were isolated and their physicochemical properties were investigated. Glutamic acid, hydroxyproline, valine and phenylalanine in the filefish skin collagen (FSC) were presented at higher levels than those of cod skin collagen (CSC), but the contents of glycine, proline and serine were contrary. The content of essential amino acids of FSC (265 residues/1000 residues) was higher than CSC (229 residues). The solubilities of both collagens were the lowest at pH 7.0, but precipitously increased at acid zone(below pH 5.0). FSC has lower viscosity than CSC. Furthermore, while the viscosities of both collagens were the lowest at pH 7.0, the viscosities of FSC and CSC were the highest at pH 4.0 and pH 2.0, respectively. The denaturation temperature of $FS(25^{\circ}C)$ was higher than $CSD\;(17^{\circ}C)$. The free hydrophobic residue contents of FSC and CSC tended to increase till $60^{\circ}C,\;and\;50^{\circ}C$ respectively, and to decrease thereafter. Hydration capacities of both collagens were the lowest at pH 7.0, and CSC had the superior hydration capacity to FSC. In addition, emulsifying and emulsifying stability of CSC was also superior to FSC.