• 제목/요약/키워드: Protein denaturation

검색결과 163건 처리시간 0.034초

Stabilization of Rat Serum Proteins Following Oral Administration of Fish Oil

  • Saso, Luciano;Valentini, Giovanni;Mattei, Eleonora;Panzironi, Claudio;Casini, Maria Luisa;Grippa, Eleonora;Silvestrini, Bruno
    • Archives of Pharmacal Research
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    • 제22권5호
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    • pp.485-490
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    • 1999
  • The mechanism of action of fish oil (FO), currently used in different chronic inflammatory conditions such as rheumatoid arthritis (RA), is not completely understood, although it is thought that it could alter the metabolism of endogenous autacoids. In addition, we hypothesized that the known capability of fatty acids (FA) of stabilizing serum albumin and perhaps other proteins, may be of pharmacological relevance considering that it is shared by other anti-rheumatic agents (e.g. nonsteroidal antiinflammatory drugs). Thus, we studied the effect of oral administration of FO and corn oil (CO), a vegetable oil with a different composition, on the stability of rat serum proteins, evaluated buy a classical in vitro method based on heat-induced protein denaturation. FO, and, to a lower extent, CO inhibited heat-induced denaturation of rat serum (RS): based on the inhibitory activity (EC50) of the major fatty acids against heat-induced denaturation of RS in vitro, it was possible to speculate the in vivo effects of palmitic acid (C16:0) and eicosapentaenoic acid (EPA, C20:5, n-3) may be more relevant than that of linolenic acid (C18:2). To better investigate this phenomenon, we extracted albumin from the serum of animals treated or not with FO with a one-step affinity chromatography technique, obtaining high purity rat serum albumin preparations (RSA-CTRL and RSA-FO), as judged by SDS-PAGE with Coomassie blue staining. When these RSA preparations were heated at $70^{\circ}C$ for 30 min, it was noted that RSA-FO was much more stable than RSA-CTRL, presumably due to higher number of long chain fatty acids (FA) such as palmitic acid or EPA. In conclusion, we provided evidences that oral administration of FO in the rat stabilizes serum albumin, due to an increase in the number of protein bound long chain fatty acids (e.g. palitic acid and EPA). We speculate that the stabilization of serum albumin and perhaps other proteins could prevent changes of antigenicity due to protein denaturation and glycosylation, which may trigger pathological autoimmune responses, suggesting that this action may be involved in the mode of action of FO in RA and other chronic inflammatory diseases.

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우유의 열처리가 우유품질과 영양가에 미치는 영향: IV. 우유의 열처리가 우유단백질의 이화학적 성질과 영양에 미치는 영향 (Effects of Heat Treatment on the Nutritional Quality of Milk. IV. Effects of Heat Treatment on the Physical and Nutritional Properties of Milk Protein)

  • 정종욱;정지윤;민태선;오세종
    • Journal of Dairy Science and Biotechnology
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    • 제35권4호
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    • pp.270-285
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    • 2017
  • Among milk proteins, caseins are not subjected to chemical changes during heat treatment of milk; however, whey proteins are partially denatured following heat treatment. The degree of whey protein denaturation by heat treatment is decreased in the order of high temperature short time (HTST) > low temperature long time (LTLT) > direct-ultra-high temperature (UHT) > indirect-UHT. As a result of heat treatment, several changes, including variations in milk nitrogen, interactions between beta-lactoglobulin and k-casein, variations in calcium sulfate and casein micelle size, and delay of milk coagulation by chymosin action, were observed. Lysine, an important essential amino acid found in milk, was partially inactivated during heat treatment. Therefore, the available amount of lysine decreased slightly (1~4% decrease) after heat treatment, However, the influence of heat treatment on the nutritional value of milk was negligible. Nutritional value and nitrogen balance did not differ significantly between UHT and LTLT in milk. In conclusion, our results showed that heat treatment of milk did not alter protein quality. Whey proteins denatured to a limited extent during the heat treatment process, and the nutritional value and protein quality were unaffected by heat treatment.

Quality parameters of chicken breast meat affected by carcass scalding conditions

  • Silva-Buzanello, Rosana Aparecida da;Schuch, Alexia Francielli;Gasparin, Andre Wilhan;Torquato, Alex Sanches;Scremin, Fernando Reinoldo;Canan, Cristiane;Soares, Adriana Lourenco
    • Asian-Australasian Journal of Animal Sciences
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    • 제32권8호
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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.

Orthokinetic Stability of $\beta$-Lactoglubulin-Stabilized Emulsions : Effects of Protein Heat Treatment and Surfactant Addition

  • Hong, Soon-Taek
    • Preventive Nutrition and Food Science
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    • 제3권2호
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    • pp.133-142
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    • 1998
  • Effects of protein heat treatment and surfactant additionoo the orthokindetic stability of $\beta$-lactoglobulin-stabilized emulsions have been investigated under turbulent flow conditions. In studies on protein-stabilized emulsions, samples which had been subjected to heat treatment(i.e. the protein solution orthe emulsion) have been found to be more prone to orthokinetic coalescene than the untreated ones. The emulsions stabilized with protein heated above the denaturation temperature(i.e. 7$0^{\circ}C$) showed the bigger initial average droplet size, which resulted in an increased orthokinetic coalescenece rate. The storage of the protein-stabilized emulsion at high temperature prior to the shearing experiment also made the emulsion less stable in the shear field. Interestingly. the addition of DATEM has been found to produce a substantial increase in orthokinetic stability of the heat-denatured protein-stabilized emulsion system, although Tween 20 is the opposite case.

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Protective Effect of Biological Osmolytes against Heat- and Chaotropic Agent-Induced Denaturation of Bacillus licheniformis γ-Glutamyl Transpeptidase

  • Lo, Huei-Fen;Chi, Meng-Chun;Lin, Min-Guan;Lan, Yuan-Gin;Wang, Tzu-Fan;Lin, Long-Liu
    • Journal of Microbiology and Biotechnology
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    • 제28권9호
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    • pp.1457-1466
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    • 2018
  • In the present study, the stabilizing effect of four different biological osmolytes on Bacillus licheniformis ${\gamma}$-glutamyl transpeptidase (BlGGT) was investigated. BlGGT appeared to be stable under temperatures below $40^{\circ}C$, but the enzyme retained less than 10% of its activity at $60^{\circ}C$. The tested osmolytes exhibited different degrees of effectiveness against temperature inactivation of BlGGT, and sucrose was found to be the most effective among these. The use of circular dichroism spectroscopy for studying the secondary structure of BlGGT revealed that the temperature-induced conformational change of the protein molecule could be prevented by the osmolytes. Consistently, the molecular structure of the enzyme was essentially conserved by the osmolytes at elevated temperatures as monitored by fluorescence spectroscopy. Sucrose was further observed to counteract guanidine hydrochloride (GdnHCl)-and urea-induced denaturation of BlGGT. Taken together, we observed evidently that some well-known biological osmolytes, especially sucrose, make a dominant contribution to the structural stabilization of BlGTT.

The Effect of Cryoprotectants on the Properties of Pacific Sand Lance Ammodytes personatus Girard Surimi During Frozen Storage

  • Yoo, Byung-Jin
    • Fisheries and Aquatic Sciences
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    • 제17권3호
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    • pp.291-298
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    • 2014
  • We investigate the effects of cryoprotectant mixtures on the quality of sand lance surimi (SLS) during storage at $-30^{\circ}C$. We monitored freeze-induced denaturation of myofibrillar protein in SLS and examined the texture profile of SLS gel. Freeze-induced denaturation was assessed by evaluating SLS $Ca^{+2}$-ATPase activity. SLS gels prepared with sorbitol or sucrose and a mixture of both as cryoprotectant. Higher concentrations of cryoprotectants resulted in significantly higher residual SLS $Ca^{+2}$-ATPase activity at the same storage time (P < 0.05). Residual $Ca^{2+}$-ATPase activity of SLS prepared with sorbitol was higher than that of sucrose when cryoprotectant concentration and storage period were same. A blend of sorbitol and sucrose resulted in a stronger cryoprptective effect of SLS myofibrillar protein than did sorbitol or sucrose alone. The presence of a phosphate compound in SOP (3% sorbitol + 0.2% phosphate compound) resulted in higher SLS $Ca^{2+}$-ATPase activity than that of did 5% sorbitol. The hardness, brittleness, and elasticity values and a folding test of the SLS gels were significantly affected by cryoprotectant concentrations and the storage time. Preference scores and acceptance for texture in a sensory evaluation of the SLS gels increased with increasing sorbitol or sucrose concentration.

우유에서의 알레르겐 저감화 방법 (Allergenicity Reduction of Milk)

  • 하월규
    • Journal of Dairy Science and Biotechnology
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    • 제26권1호
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    • pp.27-36
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    • 2008
  • This review was written to introduce updated data on the structure and function of the major milk proteins identified as allergens, the characterization of their epitopes in each allergenic milk proteins, and the reduction of milk protein allergenicity. Most mammalian milk protein, even protein present at low concentration, are potential allergens. Epitopes identified in milk proteins are both conformational(structured epitope) and sequential epitopes(linear epitope), throughout the protein molecules. Epitopes on casein and whey proteins are reported to be sequential epitope and conformational epitopes, respectively. Conformational epitopes on whey protein are changed into sequential epitope by heat denaturation during heat treatment. Several methods have been proposed to reduce allergenicity of milk proteins. Most ideal and acceptable method to make hypoallergenic milk or formula, so far, is the hydrolysis of allergenic milk proteins by enzymes that has substrate specificity, such as pepsin, trypsin, or chymotrypsin. Commercial formulas based on milk protein hydrolysate are available for therapeutic purpose, hypoantigenic formula for infants from families with a history of milk allergy and hypoallergenic formula for infants with existing allergic symptoms.

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연체류의 근원섬유단백질에 열 안정성에 관한 연구 (Studies on the Thermostability of Myofibrillar Proteins of Mollusca)

  • 신완철;송재철;김영호
    • 한국식품영양학회지
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    • 제10권2호
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    • pp.160-165
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    • 1997
  • 오징어의 actomyosin과 myosin은 3$0^{\circ}C$에서 최대 Vmax를 나타냈고 대합의 actomyosin과 myosin은 35$^{\circ}C$에서, HMM은 $25^{\circ}C$에서 최대 Vmax를 보였다. 또한 근원섬유단백질의 열 안정성은 염농도의 차이에 따라 크게 변하여 염농도가 높을수록 변성의 정도가 컸으며 대합의 근원섬유단백질이 오징어의 근원섬유단백질보다 높은 열 안정성을 나타냈다. 근원섬유단백질에 3%의 에탄올을 첨가하여 가온하면 변성은 가속화되었으며 변성속도에 있어서도 동물간에 차이가 있는 것으로 나타났다.

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The Effects of the Injection of Proteolytic Enzymes and Ginger Extract into M. pectoralis profundus of Beef on Intramuscular Connective Tissue and Myofibrillar Protein

  • Moon, Sung-Sil;Ko, Kyung-Hee;Mullen, Ann-Maria;Ward, Paddy;Park, Yong-Hyun;Park, Su-Min
    • 한국축산식품학회:학술대회논문집
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    • 한국축산식품학회 2006년도 정기총회 및 제37차 춘계 국제학술발표대회
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    • pp.94-97
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    • 2006
  • Proteolytic enzymes and ginger extract were effective on tenderising M. pectoralis profundus, resulting in higher collagen solubility, a decrease of melting denaturation temperature and WBSF compared with the control. Comparing all treatments, bromelain treatment showed to be higher for collagen solubility than other treatments, but no significant differences in onset and melting denaturation temperature of intramuscular connective tissue were found. These corresponded to WBSF results. The present study indicates that ginger extract might be effectively able to be utilised in pilot level as better alternatives to bromelain and papain for tenderisation of tough meat, such as cull cow and beef cuts with many collagen.

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