• Proceedings of the Korean Powder Metallurgy Institute Conference
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• 2006.09a
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• pp.55-55
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• 2006

• Food Science of Animal Resources
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• v.36 no.1
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• pp.29-36
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• 2016

This study was performed to investigate the role of pH and temperature postmortem, and to demonstrate the importance of these factors in determining meat quality. Postmortem pH_45min (pH at 45 min postmortem or initial pH) via analysis of Pearson’s correlation showed high positive correlation with pH change pH_c24 (pH change from pH_45min to pH_24h postmortem). However, postmortem pH after 24 h (pH_24h or ultimate pH) had a high negative correlation with pH change, pH_c24, CIE L*, and protein content. Initial temperature postmortem (T_1h ) was positively associated with a change in temperature from 45 min to 24 h postmortem (T_c24) and cooking loss, but negatively correlated with water holding capacity. Temperature at 24 h postmortem (T_24h) was negatively associated with T_c24. Collectively, these results indicate that higher initial pH was associated with higher pH_c24, T_1h, and T_c24. However, higher initial pH was associated with a reduction in carcass weight, backfat thickness, CIE a* and b*, water holding capacity, collagen and fat content, drip loss, and cooking loss as well as decreased shear force. In contrast, CIE a* and b*, drip loss, cooking loss, and shear force in higher ultimate pH was showed by a similar pattern to higher initial pH, whereas pH_c24, carcass weight, backfat thickness, water holding capacity, fat content, moisture content, protein content, T_1h, T_24h, and T_c24 were exhibited by completely differential patterns (p<0.05). Therefore, we suggest that initial pH, ultimate pH, and temperatures postmortem are important factors in determining the meat quality of pork.

• Bulletin of the Korean Chemical Society
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• v.34 no.9
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• pp.2597-2603
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• 2013

The reactions of hydrated $CdCl_2$, $MnCl_2$, and $NiCl_2$ with 2,2'-bipyidine-3,3',6,6'-tetracarboxylic acid ($H_4bptc$) afforded the mononuclear [$Cd^{II}(H_2bptc)(H_2O)_3]{\cdot}H_2O$ (1), linear $\{[Cd(H_2bptc)(H_2O)]{\cdot}3H_2O\}_n$ (2), 3-D heterobimetallic $[NaCd(Hbptc)(H_2O)]$ (3), layer $[Mn(H_2bptc)(H_2O)]_n$ (4) and a dinuclear compound $[Ni_2(H_2bptc)-(H_2O)_2]{\cdot}6H_2O$ (5). These compounds have been characterized by elemental analysis, IR, and their structures have been determined by X-ray crystallography. The thermal stabilities of 1-3 were measured by thermogravimetric analysis (TGA) and their solid state luminescence properties together with the free ligand $H_4bptc$ were investigated at room temperature.

• Korean Journal of Materials Research
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• v.23 no.5
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• pp.266-270
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• 2013

The hydrogen storage properties of pure $MgH_2$ were studied and compared with those of pure Mg. At the first cycle, pure $MgH_2$ absorbed hydrogen very slowly at 573 K under 12 bar $H_2$. The activation of pure $MgH_2$ was completed after three hydriding-dehydriding cycles. At the $4^{th}$ cycle, the pure $MgH_2$ absorbed 1.55 wt% H for 5 min, 2.04 wt% H for 10 min, and 3.59 wt% H for 60 min, showing that the activated $MgH_2$ had a much higher initial hydriding rate and much larger $H_a$ (60 min), quantity of hydrogen absorbed for 60 min, than did activated pure Mg. The activated pure Mg, whose activation was completed after four hydriding-dehydriding cycles, absorbed 0.80 wt% H for 5 min, 1.25 wt% H for 10 min, and 2.34 wt% H for 60 min. The particle sizes of the $MgH_2$ were much smaller than those of the pure Mg before and after hydriding-dehydriding cycling. The pure Mg had larger hydrogen quantities absorbed at 573K under 12 bar $H_2$ for 60 min, $H_a$ (60 min), than did the pure $MgH_2$ from the number of cycles n = 1 to n = 3; however, the pure $MgH_2$ had larger $H_a$ (60 min) than did the pure Mg from n = 4 to n = 6.

• Journal of the Korean Magnetics Society
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• v.5 no.5
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• pp.679-682
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• 1995

The observed high-field magnetization curves of $Sm_{2}Fe_{17}N_{3.0}$ at 4.2 K and 296 K are well reproduced by the calculation using the Sm-Fe exchange field $2\mu\textrm{B}H_{ex}\;=\;320\;K$ and two crystalline electric field parameters ${A_{0}}^{2}=\;-910\;K$ and ${A_{1}}^{0}=\;200\;K$. The calculation shows that during the magnetization process along the hard axis at 4.2 K, the Sm moment rotates toward the direction antiparallel to H when H < 110 kOe and then returns to the field direction with further increase of the field. At 296 K, the Sm moment rotates toward the direction antiparallel to H monotonously with increasing field and finally becomes antiparallel to H when $H{\geq}H_{A}=210\;kOe$. The particular magnetization process of the Sm moment can be explained by the field-induced noncollinear coupling between the spin and orbital moments of the Sm ion.

• Proceedings of the Korean Nuclear Society Conference
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• 2005.05a
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• pp.337-338
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• 2005

• International Journal of Industrial Entomology and Biomaterials
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• v.8 no.2
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• pp.189-194
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• 2004

Amylase isozyme based three multivoltine viz., N+p, Np, N+ $p^{cho}$ and two bivoltine-D6+p, D6p syngenic lines (Syn. L) were developed from germplasm (GP) stocks Nistari (N) and D6 respectively. haemolymph isozyme pattern at pH 7.0 and 8.5 depicted a total 11 number (Am $y_{1 to 6}$ at pH 7.0 and Am $y^{l to 5}$ at pH 8.5) of native proteins (NP) of various sizes are amylase isozyme expressers. Among eleven NPs, two NPs of 770 kDa (Am $y^{6}$ at pH 7.0) and 376 kDa (Am $y^3$ at pH 8.5) are $\alpha$-amylase expressers and remaining NPs of 370, 364, 350, 329 and 274 kDa at pH 7.0 and 206, 292, 416, 725 kDa at pH 8.5 are $\beta$-amylase expressers. Accordingly, digestive juice amylase isozyme pattern at aforesaid pH also depicted a total number of 10 NPs (Am $y^{1 to 5}$) at each pH 7.0 and 8.5 are amylase expressers of which NP of 387 kDa (Am $y^4$ at pH 7.0) and 780 kDa (Am $y^{5}$ at pH 8.5) are a-amylase expresser. Remaining NPs of 338,297 ＆ 216 kDa at pH 7.0 and 370, 341, 329 ＆302 kDa at pH 8.5 are $\beta$-amylase expresser. Recurrent backcross lines (RBL) viz., N+pRBL and NpRBL were developed through introgression of high shell weight character (a multigenic trait) to be used further for congenic line (Con. L) development and to understand any association with introgressed character. Isozyme pattern in haemolymph of RBLs depicted only one $\alpha$-amylase of 770 kDa at pH 7.0 and 376 kDa at pH 8.0 with three and four respective $\beta$-amylase bands but in bivoltine lines numbers of $\beta$-amylase bands vary between 1 to 2 at aforesaid pH. Variability was also observed in digestive juice of multivolitine and its RBLs but bivoltine lines express null activity at both pH except appearance of one very week $\alpha$-amylase band D6+p at pH 8.5. Overall study suggests that not a single NP at both pH is common for expression of any band of amylase isozyme i.e., a totally different set of proteins are the amylase isozyme expresser at specific pH and no molecular factor of amylase is associated in developed RBLs which showed improvement on survival, single cocoon shell weight (SCSW) and single filament length over receptor parents.s.s.s.

• Bulletin of the Korean Chemical Society
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• v.29 no.3
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• pp.585-589
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• 2008

Second-order rate constants (kN) have been measured for reactions of Y-substituted phenyl 2-thiophenecarboxylates (6a-h) with morpholine and piperidine in 80 mol % H2O/20 mol % DMSO at 25.0 0.1 oC. The Brnsted-type plot for the reactions of 6a-h with morpholine is linear with b lg = 1.29, indicating that the reactions proceed through a tetrahedral zwitterionic intermediate (T?). On the other hand, the Brnsted-type plot for the reactions of 6a-h with piperidine exhibits a downward curvature, implying that a change in the rate-determining step occurs on changing the substituent Y in the leaving group. Dissection of kN into microscopic rate constants (i.e., k1 and k2/k1 ratio) has revealed that k1 is smaller for the reactions of 6a-h than for those of Y-substituted phenyl 2-furoates (5a-h), while the k2/k1 ratio is almost the same for the reactions of 5a-h and 6a-h. It is also reported that modification of the nonleaving group from the furoyl (5a-h) to the thiophenecarbonyl (6a-h) does not influence pKao (defined as the pKa at the center of the Brnsted curvature) as well as the k2/k1 ratio.

• Journal of the Korean Electrochemical Society
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• v.9 no.1
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• pp.19-28
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• 2006

The phase-shift method for determining the Langmuir, Frumkin, and Temkin adsorption isotherms ($\theta_H\;vs.\;E$) of H for the cathodic $H_2$ evolution reaction (HER) at a Pt/0.1 M KOH solution interface has been proposed and verified using cyclic voltammetric, differential pulse voltammetric, and electrochemical impedance techniques. At the Pt/0.1 M KOH solution interface, the Langmuir and Temkin adsorption isotherms ($\theta_H\;vs.\;E$), the equilibrium constants ($K_H=2.9X10^{-4}mol^{-1}$ for the Langmuir and $K_H=2.9X10^{-3}\exp(-4.6\theta_H)mol^{-1}$ for the Temkin adsorption isotherm), the interaction parameters (g=0 far the Langmuir and g=4.6 for the Temkin adsorption isotherm), the rate of change of the standard free energy of $\theta_H\;with\;\theta_H$ (r=11.4 kJ $mol^{-1}$ for g=4.6), and the standard free energies (${\Delta}G_{ads}^{\circ}=20.2kJ\;mol^{-1}$ for $k_H=2.9\times10^{-4}mol^{-1}$, i.e., the Langmuir adsorption isotherm, and $16.7<{\Delta}G_\theta^{\circ}<23.6kJ\;mol^{-1}$ for $K_H=2.9\times10^{-3}\exp(-4.6\theta_H)mol^{-1}$ and $0.2<\theta_H<0.8$, i.e., the Temkin adsorption isotherm) of H for the cathodic HER are determined using the phase-shift method. At intermediate values of $\theta_H$, i.e., $0.2<\theta_H<0.8$, the Temkin adsorption isotherm ($\theta_H\;vs.\;E$) corresponding to the Langmuir adsorption isotherm ($\theta_H\;vs.\;E$), and vice versa, is readily determined using the constant conversion factors. The phase-shift method and constant conversion factors are useful and effective for determining the Langmuir, Frumkin, and Temkin adsorption isotherms of intermediates for sequential reactions and related electrode kinetic and thermodynamic data at electrode catalyst interfaces.

• Journal of Microbiology and Biotechnology
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• v.14 no.2
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• pp.415-416
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• 2004

Crystals of six new Bacillus thuringiensis serovarieties [coreanensis (H25), konkukian (H34), leesis (H33), seoulensis (H35), sooncheon (H41), and yosoo (HI8a18c)] with different H-antigens, which are toxic to Bombyx mori and/or mosquito larvae, were serologically quite distinct from each other.