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Differences in pork myosin solubility and structure with various chloride salts and their property of pork gel

  • Hyun Gyung Jeong;Jake Kim;Seonmin Lee;Kyung Jo;Hae In Yong;Yun-Sang Choi;Samooel Jung
    • Journal of Animal Science and Technology
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    • v.65 no.5
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    • pp.1065-1080
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    • 2023
  • The solubility and structure of myosin and the properties of pork gel with NaCl, KCl, CaCl2, and MgCl2 were investigated. Myofibrillar proteins (MPs) with phosphate were more solubilized with NaCl than with KCl (p < 0.05). CaCl2 and MgCl2 showed lower MP solubilities than those of NaCl and KCl (p < 0.05). The α-helix content of myosin was lower in KCl, CaCl2, and MgCl2 than in NaCl (p < 0.05). The pH of pork batter decreased in the order of KCl, NaCl, MgCl2, and CaCl2 (p < 0.05). The cooking yield of the pork gel manufactured with monovalent salts was higher than that of the pork gel manufactured with divalent salts (p < 0.05). The pork gel manufactured with KCl and MgCl2 showed lower hardness than that of the pork gel manufactured with NaCl. The solubility and structure of myosin were different with the different chloride salts and those led the different quality properties of pork gel. Therefore, the results of this study can be helpful for understanding the quality properties of low-slat meat products manufactured by replacing sodium chloride with different chloride salts.

Foaming Capacity and Foaming Stability of Protein Recovered from Red Crab Processing Water (홍게 가공회수 단백질의 거품 형성력 및 안정성)

  • Kim, Yong-Jin;Sin, Tae-Seon;O, Hun-Il
    • The Korean Journal of Food And Nutrition
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    • v.9 no.3
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    • pp.325-330
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    • 1996
  • Foaming capacity (FC) and stability (FS) of protein recovered from red crab (Chitinonecetes opilio) processing in water and soybean protein isolate were determined at pH 2.0~10.0 in water and NaCl solution. The FC values for both proteins showed the lowest values at the isoelectric point (pH 4.0) and increased nth an increase in pH above the isoelectric point. FC of RCP was higher than that of SPI at pH 10.0 in water and both NaCl solutions. FC of SPI increased with an increase in NaCl concentration at pH 4.0 and 6.0, but FC of RCP was not affected. The highest FS values for both proteins were obtained at pH 4.0 in water. At pH 2.0, FC of RCP decreased with NaCl concentration increase, but FS increased. NaCl concentration had little effect on FS of RCP at pH 4.0 and 6.0, but the FS decreased at pH 10.0. FS of SPI was similar to that of RCP at pH 2.0 and increased with NaCl concentration Increase from 0.1 to 0.5M NaCl at pH 10.0.

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Effect of Mercuric Chloride (In Vitro) on the Function of Human Polylnorphonuclear Leukocytes(PMNs) (수은이 시험관내 사람 다형핵백혈구의 기능에 미치는 영향)

  • 한형미;윤은이;김순한;김옥연;김효정;선우연
    • Biomolecules & Therapeutics
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    • v.1 no.2
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    • pp.131-136
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    • 1993
  • In the present study, the effect of $HgCl_2$on the function of human peripheral polymorphonuclear leukocytes(PMNs) was examined. PMNs were isolated from human peripheral blood with density centrifugation in Ficoll-Paque. The cells were then incubated with $0.5{\sim}5{\mu}M\;HgCl_2$and glass adherence, chemotactic activity and erythrocyte-antibody rosette forming activity were measured. $HgCl_2$ decreased the function of PMNs in all three aspects tested. $HgCl_2$significantly diminished glass adherence(40.5 {\mu}M: 92{\pm}12%$ (percentage of control, $mean{\pm}$ S.D.); 41 {\mu}M: 46{\pm}11%,$ P<0.01; $3{\mu}M: 35{\pm}7%,$P<0.01;$5{\mu}M:49{\pm}10%,$ P<0.01). Similarly, significant differences were observed in chemotactic activity after $HgCl_2$treatment compared with control (control: $0.95{\pm}0.14mm; 0.5 {\mu}M: 0.91{\pm}0.11 mm; 1 {\mu}M: 0.77{\pm}0.16mm, P<0.05; 3{\mu}M: 0.61{\pm} 0.06mm, P<0.01; 5{\mu}M: 0.15{\pm}0.03 mm, P<0.01).$ Also, 4HgCl_2$decreased the percentage of rosette-forming PMNs, indicating diminished phagocytic activity of PMNs upon $HgCl_2$ exposure compared with control (control: $58{\pm}4%; 1{\mu}M: 53{\pm}4%, p<0.05; 3{\mu}M: 49{\pm}3%, P<0.01; 5{\mu}M: 46{\pm}3%, P<0.01).$ Cell viability was not antered after $HgCl_2$treatment (483{\pm}5%$ viability in control PMNs versus $81{\pm}8%$ viability in $5{\mu}M$ Hg-treated PMNs), suggesting that the impaired PMN function after $HgCl_2$treatment was not due to nonspecific cytotoxicity induced by $HgCl_2$. $HgCl_2$-induced decrease in the function of PMNs may have some implications in depressed host susceptibilityupon bacterial challenge after mercury exposure.

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Effect on the change of ginsenosides, pH and color by NaCl concentration (NaCl 농도가 인삼의 ginsenoside 함량과 pH 및 색의 변화에 미치는 영향)

  • Park, Myung-Han;Lee, Jong-Won;Lee, Jong-Tae;Kim, Kyo-Chang
    • Applied Biological Chemistry
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    • v.36 no.4
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    • pp.260-264
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    • 1993
  • In order to determine the stability of ginseng components in this salt concentration when used to ginseng as additive ingredient of sauces or seasonings, we study on the content and charactristic of ginsenosides and changes in pH and color, ginseng tail and ginseng extract were treated with various concentration of NaCl solution. In this experiment, extract of ginseng tail were increased in pH as NaCl concentration were increased, but ginseng extract have not changed evidently. The both solution were decreased in color as the salt concentration were increased. Yield of n-butanol extract was decreased in 5% NaCl concentration, while it was increased in the above concentration, and ginseng extract was changed higher than ginseng tail. Ginsenosides content were increased in 5% NaCl concentration, both $ginsenosied-Rb_1$, $-Rb_2$, -Rc, -Rd of diol line and ginsenoside-Re of triol line and increased in above NaCl concentration. Especially ginsenoside-Re showed to sensitive response to the changes of the salt concentration.

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Solubilization of BSA into AOT Reverse Micelles Using the Phase-Transfer Method: Effects of pH and Salts (상 접촉법을 이용한 BSA의 AOT 역미셀으로 가용화: pH와 염의 영향)

  • 노선균;강춘형
    • KSBB Journal
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    • v.16 no.1
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    • pp.48-53
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    • 2001
  • Bovine serum albumin(BSA) was solubilized into the reverse micellar phase consisting of sodium bis(2-ethylhexyl) sulfosuccinate(AOT) and isooctane using the phase transfer method. Of particular interest in this study were the effects of pH and the added salt type and concentration on the solubilization efficiency. When univalent or divalent salts such as KCl, NaCl, $MgCl_2$, or $CaCl_2$ were added to the aqueous phase at a concentration of 0.1 M, maximum solubilization efficiency was attained at a pH ranging from 5 to 7, depending on the added salt type. Increased salt concentration up to 1 M resulted in an increased solubilization efficiency for $CaCl_2$ and NaCl, while the addition of $MgCl_2$ beyond 0.1 M showed an anomalous trend. Further, it was noteworthy that too a large extent the protein precipitated in the interface between the organic and aqueous phases at lower pHs and lower salt concentrations. The size of the reverse micelle water pool was estimated by measuring the molar ratio of the surfactant to the water, $W_0$. Irrespective of pH in the aqueous phase, the resulting value of $W_0$ was almost constant, eg., 20 for $MgCl_2$ . However, the value of $W_0$ decreased with increased salt concentration in the cases of KCl and $CaCl_2$.

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Characterization of Acidic Carboxymethylcellulase Produced by a Marine Microorganism, Psychrobacter aquimaris LBH-10 (해양미생물 Psychrobacter aquimaris LBH-10가 생산하는 산성 carboxymethylcellulase의 특성에 대한 연구)

  • Kim, Hye-Jin;Gao, Wa;Lee, You-Jung;Chung, Chung-Han;Lee, Jin-Woo
    • Journal of Life Science
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    • v.20 no.4
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    • pp.487-495
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    • 2010
  • A microorganism hydrolyzing carboxymethylcellulose (CMC) was isolated from seawater, identified as Psychrobacter aquimaris by analysis of 16S rDNA sequences, and named P. aquimari LBH-10. This strain produced an acidic carboxymethylcellulase (CMCase), which hydrolyzed carboxymethylcellulose (CMC), cellobiose, curdlan, filter paper, p-nitrophenyl-$\beta$-D-glucopyranoside (pNPG), pullulan, and xylan, but there was no detectable activity on avicel and cellulose. The optimal temperature for CMCase produced by P. aquimari LBH-10 was $50^{\circ}C$ and more than 90% of its original activity was maintained at broad temperatures ranging from 20 to $50^{\circ}C$ after 24 hr. The optimal pH of the CMCase was 3.5, and more than 70% of its original activity was maintained under acidic conditions between pH 2.5 and 7.0 at $50^{\circ}C$ after 24 hr. The optimal pH of CMCase produced by P. aquimaris LBH-10 seems to be lower than those produced by any other bacterial and fungal strain. $CoCl_2$, EDTA, and $PbCl_2$ at a concentration of 0.1 M enhanced CMCase-produced P. aquimaris LBH-10, whereas $HgCl_2$, KCl, $MnCl_2$, $NiCl_2$, and $SrCl_2$ inhibited it.

A Study of Characteristics of Pectinesterase, Polygalacturonase and Peroxidase in Kimchi Materials (김치재료에 존재하는 Pectinesterase, Polygalacturonase 및 Peroxidase 특성에 관한 연구)

  • Park, Hee-Ok;Kim, Kee-Hyun;Yoon, Sun
    • Journal of the Korean Society of Food Culture
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    • v.5 no.4
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    • pp.443-448
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    • 1990
  • The object of this study was to investigate the characteristics of pectinesterase(PE), polygalacturonase(PG) and Peroxidase(POD) in Kimchi materials. The results were as follows : 1. The specific activities of PEs in Korean cabbage, Korean raddish, garlic and ginger were 200 unit/mg protein, 23.1 unit/mg protein, 0.8 unit/mg protein and 32 unit/mg protein, respectively. The optimum pHs of PEs in all materials were between 7 to 8. The concentrations of NaCl, $CaCl_2$ which showed the highest activities of PEs were $0.2{\sim}0.3M$ NaCl, 50 mM $CaCl_2$ in Korean cabbage and raddish, 0.05 M NaCl, 20 mM $CaCl_2$ in garlic and 0.2 M NaCl, 20 mM $CaCl_2$ in ginger. 2. The specific activities and the optimum pHs of PGs were 1.5 unit/mg protein and pH 4.5 in Korean cabbage, 1.6 unit/mg protein and $pH\;4.5{\sim}5.5M$ in Korean raddish, 0.06 unit/mg protein and $pH\;3.0{\sim}3.5M$ in garlic, and 0.06 unit/mg protein and $CaCl_2$ in ginger. The concentrations of NaCl, $CaCl_2$ which showed the highest activities of PGs were $0.1{\sim}0.2M$ NaCl and $0.15{\sim}0.2mM$ mM $CaCl_2$ in all materials. 3. The specific activities and the optimum pHs of PODs in Korean cabbage, Korean raddish, garlic and ginger were 71.3 unit/mg protein ; pH 6.0. 769 unit/mg protein ; pH 5.5, 1.09 unit/mg protein ; pH 4.5 and 12.7 unit/mg protein ; $pH\;5.0{\sim}5.5M$, respectively. POD activities were not decreased in Korean cabbage, but decreased in Korean raddish by the increase of NaCl, $CaCl_2$ concentrations. In garlic and ginger, POD activities were a little slightly affected by the increase of NaCl, $CaCl_2$ concentrations.

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The Study on Emulsifying and Foaming Properties of Buckwheat Protein Isolate (분리 메밀 단백질의 유화 및 기포특성에 관한 연구)

  • 손경희;최희선
    • Korean journal of food and cookery science
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    • v.9 no.1
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    • pp.43-51
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    • 1993
  • Buckwheat protein isolate was tested for the effects of pH, addition of sodium chloride and heat treatment on solubility, emulsion capacities, emulsion stability, surface hydrophobicity, foam capacities and foam stability. The solubility of buckwheat protein isolate was affected by pH and showed the lowest value at pH 4.5, the isoelectric point of buckwheat protein isolate. The solubility significantly as the pH value reached closer to either ends of the pH, i.e., pH 1.0 and 11.0. The effects of NaCl concentration on solubility were as follows; at pH 2.0, the solubility significantly decreased when NaCl was added; at pH 4.5, it increased above 0.6 M; at pH 7.0 it increased; and at pH 9.0 it decreased. The solubility increased above $80^{\circ}C$, at all pH ranges. The emulsion capacity was the lowest at pH 4.5. It significantly increased as the pH approached higher acidic or alkalic regions. At pH 2.0, when NaCl was added, the emulsion capacity decreased, but it increased at pH 4.5 and showed the maximum value at pH 7.0 and 9.0 with 0.6 M and 0.8 M NaCl concentrations. Upon heating, the emulsion capacity decreased at acidic pH's but was maximised at pH 7.0 and 9.0 on $60^{\circ}C$ heat treatment. The emulsion stability was the lowest at pH 4.5 but increased with heat treatment. At acidic pH, the emulsion stability increased with the increase in NaCl concentration but decreased at pH 7.0 and 9.0. Generally, at other pH ranges, the emulsion stability was decreased with increased heating temperature. The surface hydrophobicity showed the highest value at pH 2.0 and the lowest value at pH 11.0. As NaCl concentrationed, the surface hydrophobicity decreased at acidic pH. The NaCl concentration had no significant effects on surface hydrophobicity at pH 7.0, 9.0 except for the highest value observed at 0.8 M and 0.4 M. At all pH ranges, the surface hydrophobicity was increased, when the temperature increased. The foam capacity decreased, with increased in pH value. At acidic pH, the foam capacity was decreased with the increased in NaCl concentration. The highest value was observed upon adding 0.2 M or 0.4 M NaCl at pH 7.0 and 9.0. Heat treatments of $60^{\circ}C$ and $40^{\circ}C$ showed the highest foam capacity values at pH 2.0 and 4.5, respectively. At pH 7.0 and 9.0, the foam capacity decreased with the increased in temperature. The foam stability was not significantly related to different pH values. The addition of 0.4 M NaCl at pH 2.0, 7.0 and 9.0 showed the highest stability and the addition of 1.0 M at pH 4.5 showed the lowest. The higher the heating temperature, the lower the foam stability at pH 2.0 and 9.0. However, the foam stability increased at pH 4.5 and 7.0 before reaching $80^{\circ}C$.

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Catalytic Activity of Ga(Ⅲ)-, In(Ⅲ)- and Tl(Ⅲ)-porphyrin Complexes (Ga(Ⅲ), In(Ⅲ) 및 Tl(Ⅲ) 금속이온을 포함한 Metalloporphyrin 착물의 촉매적 특성)

  • Park, Yu Chul;Na, Hun Gil;Kim, Seong Su
    • Journal of the Korean Chemical Society
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    • v.39 no.5
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    • pp.364-370
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    • 1995
  • The catalytic oxidations of several olefins in $CH_2Cl_2$ have been investigated using non-redox metalloporphyrin (M=Ga(III), In(III), Tl(III)) complexes as catalyst and sodium hypochlorite as terminal oxidant. Porphyrins were $(p-CH_3O)TPP,\;(p-CH_3)TPP,\;TPP,\;(p-F)TPP,\;(p-Cl)TPP\;and\;(F_20)TPP$ (TPP=tetraphenylporphyrin), and olefins were $(p-CH_3O)-,\;(p-CH_3)-,\;(p-H)-,\;(p-F)-,\;(p-Cl)-\;and\;(p-Br)styrene$styrene and cyclopentene and cyclohexene. The substrate conversion yield was discussed according to the substituent effects of metalloporphyrin and substrate, and the radius effect of non-redox metal ion. The conversion yield of substrate by changing the substituent of TPP increased in the order of $p-CH_3O$ < $p-CH_3$ < H < p-F < p-Cl, which was consistent with the sequence of $4{\sigma}$ values of TPP. But the substituent effect of substrate on the conversion yield decreased with increasing the ${\sigma}^+$ values on substrates in the order of p-CH3O > p-CH3 > H > p-Cl > p-Br. For the oxidation of several olefins, the complexes of In(III)- and Tl(III)-porphyrins turned out to be more active catalysts than Ga(III)-porphyrin.

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Extraction of Short Peptide Using Supported Liquid Membranes (Supported Liquid Membrane을 이용한 Short Peptide의 추출)

  • Lee, Jae-Heung;Park, Ki-Moon
    • Food Science of Animal Resources
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    • v.25 no.3
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    • pp.340-343
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    • 2005
  • The objective of this work was to study separation of short peptide (glycine-tyrosine) by using supported liquid membranes (SLMs) containing Aliquat as a cationic carrier, In the present investigation, the influence of pH of donor phase, concentrations of carrier and salt concentrations of acceptor phase on separation flux rate were investigated. Below pH 7.0 the flux rate was not affected by NaCl concentration or carrier concentration. However, the rate was increased significantly above pH 7.0. The rate with Hossain's SLM(H-SLM) containing $20\%$ Aliquat was about 3-fold higher with pH 9.0 at 0.25 M NaCl and 10-fold higher with pH 8.0 at 1.0 M NaCl than that with Duggan's SLM(D-SLM) containing $8\%$ Aliquat respectively. Furthermore, the rate with H-SLM was 10-fold higher at 1.0 M NaCl than the rate with 0.25 M NaCl, In conclusion, it would appear that the rate of separation was facilitated by using high salt concentrations together with high carrier concentrations above pH 7.0.