• 제목/요약/키워드: ${\alpha}$-lactalbumin

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토끼 항 ${\alpha}-Lactalbumin$ 항혈청에 대한 유청단백질 가수분해물의 항원성 (Antigenicity of Whey Protein Hydrolysates Against Rabbit Anti ${\alpha}-Lactalbumin$ Antiserum)

  • 하월규;전석락;김정완;이수원;이재영;손동화
    • 한국식품과학회지
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    • 제26권4호
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    • pp.436-441
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    • 1994
  • Chymotrypsin, trypsin, pancreatin, 그리고 Aspergillus oryzae 유래 단백질분해효소의 in vitro처리에 의하여 유청단백질(WPI)의 가수분해물(WPH)중 ${\alpha}-LA$ 유래의 항원성변화를 조사하기 위하여 토끼 항 ${\alpha}-LA$ 항혈청을 이용한 competitive inhibition ELISA(cELISA)와 heterologous PCA를 실시하였다. cELISA에 의하여 WPH의 monovalent항원성을 분석한 결과, pepsin전처리는 chymotrypsin, trypsin 그러고 pancreatin 가수분해물의 항원성을 더욱 감소시키는 효과가 있었으며, 열 전처리는 Asp. oryzae 유래효소 및 trypsin 가수분해물의 항원성을 더욱 감소시켰다 전체적으로 ${\alpha}-LA$유래의 monovalent 항원성은 효소처리에 의하여 $10^{-2.5}-10^{-5.5}$배 또는 그 이하로 저하되었으며, 특히 열 및 pepsin 전처리후 trypsin으로 가수분해한 경우(TDP)의 항원성은 거의 상실되었다. WPH의 가수분해도와 ${\alpha}-LA$유래의 monovalent 항원성 감소는 그다지 일치하지 않았다. Guinea pig를 이용한 PCA test에 의하여 ${\alpha}-LA$유래의 polyvalent 항원성을 분석한 결과 WPI 및 ${\alpha}-LA$는 양성으로 높게 나타났으나, WPH는 전처리유무에 관계없이 모두 음성으로 나타났다. 이는 WPI의 가수분해로 생성된 ${\alpha}-LA$유래의 peptide가 특이항체와 결합은 가능하나 생체내에서 알레르기를 유발하지 않음을 뜻하였다. 따라서, 유청단백질을 효소로 가수분해하면 유청단백질중 ${\alpha}-LA$의 allergenicity는 쉬 파괴됨을 알 수 있었다.

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유청 단백질 가수분해물의 유화특성 (Emulsifying Properties of Whey Protein Hydrolysates)

  • 양희진;이수원
    • 한국축산식품학회지
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    • 제23권1호
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    • pp.63-69
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    • 2003
  • 본 연구는 단백질분해효소로 whey protein을 가수분해하여 얻은 가수분해물의 용해도와 유화특성의 변화를 측정하기 위해 실시하였다. Whey protein concentrates를 porcine trypsin(E : S=1 ; 3,000)으로 pH 8.0, 37$^{\circ}C$에서 6시간 동안 가수분해한 whey protein 가수분해물의 유화활성은 분해 4시간째에 가장 높게 나타났으며, 이 때 가수분해도는 5.50%이었다. whey protein의 효소가수분해로 whey protein 중의 $\alpha$-lactalbumin은 분해가 잘 일어나지 않으나 $\beta$-lactoglobulin은 분해 초기부터 급속히 분해되며 유화력 상승에 관여하는 여 러개의 저분자량 peptide를 생성하였다. 가수분해물의 용해도는 가수분해시간이 지남에 따라 증가세를 보이다가 5시간부터 조금씩 감소 추세를 보였으며, pH에 따라서는 등전점 부근인 pH4~5에서 용해도가 가장 낮았으나 가수분해시간이 증가함에 따라 이 부근의 용해도가 현저히 증가하였으며 pH 6이상에서는 pH가 증가함에 따라 용해도도 증가하였다. 유화활성은 용해도의 결과와 거의 비슷한 결과를 나타내었다. 유화 안정성은 분해시간이 지남에 따라 조금씩 증가함을 보여주었으나, 가수분해 4시간부터 pH 8 이상의 PH에서 급격한 증자를 나타내었다.

Principal Milk Components in Buffalo, Holstein Cross, Indigenous Cattle and Red Chittagong Cattle from Bangladesh

  • Islam, M.A.;Alam, M.K.;Islam, M.N.;Khan, M.A.S.;Ekeberg, D.;Rukke, E.O.;Vegarud, G.E.
    • Asian-Australasian Journal of Animal Sciences
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    • 제27권6호
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    • pp.886-897
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    • 2014
  • The aim of the present study was to get a total physical and chemical characterization and comparison of the principal components in Bangladeshi buffalo (B), Holstein cross (HX), Indigenous cattle (IC) and Red Chittagong Cattle (RCC) milk. Protein and casein (CN) composition and type, casein micellar size (CMS), naturally occurring peptides, free amino acids, fat, milk fat globule size (MFGS), fatty acid composition, carbohydrates, total and individual minerals were analyzed. These components are related to technological and nutritional properties of milk. Consequently, they are important for the dairy industry and in the animal feeding and breeding strategies. Considerable variation in most of the principal components of milk were observed among the animals. The milk of RCC and IC contained higher protein, CN, ${\beta}$-CN, whey protein, lactose, total mineral and P. They were more or less similar in most of the all other components. The B milk was found higher in CN number, in the content of ${\alpha}_{s2}-$, ${\kappa}$-CN and ${\beta}$-lactalbumin, free amino acids, unsaturated fatty acids, Ca and Ca:P. The B milk was also lower in ${\beta}$-lactoglobulin content and had the largest CMS and MFGS. Proportion of CN to whey protein was lower in HX milk and this milk was found higher in ${\beta}$-lactoglobulin and naturally occuring peptides. Considering the results obtained including the ratio of ${\alpha}_{s1}-$, ${\alpha}_{s2}-$, ${\beta}$- and ${\kappa}$-CN, B and RCC milk showed best data both from nutritional and technological aspects.

알파-락트알부민의 열처리에 의한 겔화 특성 (Gelation Properties of ${\alpha}-Lactalbumin$ by Heat Treatment)

  • 박인덕;홍윤호
    • 한국식품과학회지
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    • 제27권6호
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    • pp.909-914
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    • 1995
  • 알파-락트알부민(${\alpha}-La$)의 열처리에 의한 겔 특성을 조사하기 위하여 ${\alpha}-La$ 농도, 염의 종류와 농도, 티올시약(NEM, DTT)의 농도를 달리해 $90^{\circ}C$에서 40분간 가열하여 만든 ${\alpha}-La$의 겔형성 시간과 용해성을 측정하였다. 겔형성 시간은 ${\alpha}-La$, NaCl, $CaCl_2$, DTT의 농도가 증가할수록 감소하였으나 NEM의 경우는 그와 반대로 나타났고 ${\alpha}-La$ 용액의 겔형성은 NEM $20{\sim}50\;mM$ 경우를 제외하고는 전부 40분 내에 이루어졌다. 용해성은 ${\alpha}-La$, NaCl, $CaCl_2$, DTT의 농도가 증가함에 따라 감소하였으나 NEM의 경우는 NEM의 농도증가에 따라 용해성은 증가하는 양상을 나타내었다. 표준완충용액에 용해된 겔의 용해성은 각각 $10.4{\sim}51.3%$, $9.2{\sim}35.4%$, $11.1{\sim}35.0%$, $8.0{\sim}9.5%$, 그리고 $96.8{\sim}56.2%$였고, 8M urea와 0.5% SDS를 함유한 표준완충용액에서는 더 높은 값인 $41.8{\sim}81.3%$, $41.9{\sim}64.1%$, $43.5{\sim}69.8%$, $29.6{\sim}38.5%$, 그리고 $77.4{\sim}98.9%$로 각각 나타났다. DTT를 함유한 것은 모든 조건에서 거의 100%에 달하는 용해성을 나타내었다. 이상으로 ${\alpha}-La$의 겔형성 속도와 용해성은 여러인자 즉, 단백질 농도, 염의 종류와 농도, 티올시약의 농도 등에 의해 영향을 받고, 겔형성 속도가 증가될수록 겔의 용해성은 감소함을 알수 있었다.

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Effect of Transglutaminase Addition on the Physicochemical Properties of Sodium Caseinate and Whey Proteins

  • Jeong, Ji-Eun;Hong, Youn-Ho
    • 한국축산식품학회지
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    • 제29권4호
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    • pp.415-422
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    • 2009
  • In this study, several factors were analyzed in an effort to determine the effects of transglutaminase (TGase) treatment on sodium caseinate (NaCN), ${\alpha}--lactalbumin$ (${\alpha}-La$), and ${\beta}-lactoglobulin$ (${\beta}-Lg$) polymerization reactions. The results of SDSPAGE showed that NaCN was slightly hydrolyzed to molecular weights of 50-400 kDa according to activation time. ${\alpha}-La$ formed high-molecular polymers of 30-300 kDa, whereas ${\beta}-Lg$ remained almost completely unhydrolyzed. Melting temperatures of NaCN, ${\alpha}-La$ with and without TGase were all in the range of $100{\pm}10^{\circ}C$ under the endothermic curve, and the melting temperature of ${\beta}-Lg$ with TGase was lower than that with TGase. When the proteins were incubated for 3 h with TGase, the micrographic structures showed a small quantity of sediment and broad layers. The final ${\alpha}-La$ residues remained at a level of 21.38%, and the TGase-treated ${\alpha}-La$ was confirmed to have undergone a profound loss of mass, to 18.25%. The DPPH-radical scavenging activity of NaCN and ${\beta}-Lg$ with TGase treatment was higher than that observed in the untreated sample, while those of ${\alpha}-La$ increased with concentration.

포유류의 종에 따른 초유 단백질의 변화에 대한 분석 (Analysis of Changes in Colostrum Proteins by Mammalian Species)

  • 김승희;김완섭
    • Journal of Dairy Science and Biotechnology
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    • 제35권2호
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    • pp.105-111
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    • 2017
  • 젖소, 한우, 돼지, 그리고 산양의 초유 중 단백질의 변화를 초일부터 7일까지 조사하였다. 돼지의 초유를 제외한 젖소, 한우, 그리고 산양의 초유에서 면역글로불린, 락토페린, 락토퍼옥시데이스, 혈청 알부민, IgG heavy chain, 그리고 IgG light chain은 분만 후, 초일 함량이 현저히 높았고, 2일째부터 급격히 감소하는 것을 보여 주었다. 그리고 ${\alpha}_{S2}$-카세인, ${\alpha}_{S1}$-카세인, ${\beta}$-카세인, ${\kappa}$-카세인, ${\beta}$-락토글로불린 및 ${\alpha}$-락트알부민은 분만 직후부터 7일까지 현저한 함량의 차이는 나타나지 않았다. 한편, 돼지 초유의 경우는 모든 단백질이 분만 후, 초일부터 2일까지 높은 함량을 나타내었다.

감마선 조사된 우유단백질에 대한 우유 알러지 환자의 IgE 결합능의 변화 (Changes of Binding Ability of Milk-Hypersensitive Patients질 IgE to Gamma-Irradiated Milk Proteins)

  • 조경환;육홍선;이주운;이수영;변명우
    • 한국식품영양과학회지
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    • 제30권3호
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    • pp.505-509
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    • 2001
  • This study was carried out to evaluate the application of food irradiation technology as a method for reducing milk allergies. Bovine $\alpha$-casein, $\beta$-casein, $textsc{k}$-casein, $\alpha$-lactalbumin(ALA), $\beta$-lactoglobulin (BLG) and serum albumin (BSA) were used as model allergens of milk proteins and the proten solution (2.0 mg/mL) with 0.01 M phosphate buffered saline (pH 7.4) was irradiated at 3, 5 and 10 kGy. Using milk-hypersensitive patients IgE (MHP-IgE), the changes of binding ability to irradiated proteins were observed by competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA). Affinity of MHP-IgE to milk proteins was higher in ALA and BLG than that of other proteins. Standard curve to each non-irradiated protein could be made with MHP-IgE for quantifying milk allergens. Binding abilities of MHP-IgE to the irradiated proteins, however, decreased with different slopes of the standard curves. Sensitivity of gamma irradiation was higher in ALA and BLG than of other proteins. These results indicated that irradiation technology can be used to reduce the milk hypersensitivity.

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Separation of Lactoferrin from Model Whey Protein Mixture by Reverse Micelles Formed by Cationic Surfactant

  • Noh, Kyung-Hyun;Rhee, Min-Suk;Imm, Jee-Young
    • Food Science and Biotechnology
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    • 제14권1호
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    • pp.131-136
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    • 2005
  • The selective extraction behavior of lactoferrin (Lf) from whey protein mixture was examined using reverse micelles formed by the cationic surfactant, cetyldimethylammonium bromide (CDAB). The major whey proteins, including ${\beta}$-lactoglobulin, ${\alpha}$-lactalbumin and bovine serum albumin, were solubilized from aqueous phase to organic phase while Lf was recovered in the aqueous phase. The solubilization behaviors of the proteins were manipulated by the process parameters such as the pH and salt concentration of the aqueous phase and the surfactant concentration in the organic phase. Efficient forward extraction was achieved with sodium borate buffer (50 mM, pH 9) containing 50 mM KCl and organic phase containing 100 mM CDAB. Based on SDS-PAGE and densitometry, about 96% of the initial Lf remained in the aqueous phase after forward extraction. The dialyzed Lf fully maintained its bacteriostatic activity against E. coli O157:H7.

THE RELATIONSHIP BETWEEN MILK PROTEIN PHENOTYPES AND LACTATION TRAITS IN AYRSHIRES AND JERSEYS

  • Kim, S.;Ng-Kwai-Hang, K.F.;Hayes, J.F.
    • Asian-Australasian Journal of Animal Sciences
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    • 제9권6호
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    • pp.685-693
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    • 1996
  • A total of 3,610 Ayrshire and 1,711 Jersey cows were phenotyped for the genetic variants of ${\alpha}_{s1}$-casein, ${\beta}$-casein, $\chi$-casein, ${\beta}$-lactoglobulin and ${\alpha}$-lactalbumin. Least squares analyses showed possible associations between milk protein phenotypes and lactational production traits. Depending on lactation number, ${\beta}$-casein phenotypes in Ayrshires were associated with milk production ($A^2A^2$ > $A^1A^2$ > $A^1A^1$), and with milk protein content. In the third lactation, Ayrshire cows with ${\beta}$-casein $A^1A^1$ produced milk with 3.43% fat compared to 3.37% fat for ${\beta}$-casein $A^2A^2$. In Ayrshire, $\chi$-casein phenotypes affected the protein content during the three lactations (BB > AB > AA) and ${\beta}$-lactoglobulin phenotypes significantly influenced the milk fat during the first lactation (4.06% for AA and 3.97% for BB). In Jerseys, protein content of milk was influenced by phenotypes of ${\alpha}_{s1}$-casein(3.98% for CC v/s 3.86% for BB in the first lactation). In the third lactation, $\chi$-casein AA of Jersey milk contained 5.35% fat compared to 4.82% for phenotype BB. The effects of ${\beta}$-lactoglobulin phenotypes on protein content were apparent in Jerseys during the second lactation with the A variant being superior to the B (4.00% for AA v/s 3.87% for BB).

STUDIES ON BIOCHEMICAL POLYMORPHISM OF MILK PROTEIN AS GENETIC MARKERS IN PIGS

  • Chung, E.R.;Han, S.K.;Shin, Y.C.;Chung, H.Y.;Kim, J.E.
    • Asian-Australasian Journal of Animal Sciences
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    • 제5권2호
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    • pp.285-294
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    • 1992
  • Biochemical polymorphisms of sow's milk proteins, $\beta$-casein ($\beta$-CN), $\beta$-lactoglobulin ($\beta$-LG), post-lactoglobulin (post-LG), $\alpha$-lactalbumin ($\alpha$-LA) and X-protein, as genetic markers for major pig breeds (Landrace, Yorkshire, Duroc, Hampshire and cross bred) in Korea were determined by starch gel electrophoresis. Phenotype and gene frequencies at all marker loci were estimated and genetic differences among breed populations were analyzed. Three $\beta$-CN phenotypes (AA, AB and BB) controlled by two codominant alleles (${\beta}-CN^A$ and ${\beta}-CN^B$), four $\beta$-LG phenotypes (AA, AC, $AC^{\pm}$ and CC) controlled by two codominant alleles (${\beta}-LG^A$ and ${\beta}-LG^C$) and ten X-protein phenotypes (AA, BB, CC, DD, AB, AC, AD, BC, BD and CD) controlled by four codominant alleles ($X^A,\;X^B,\;X^C\;and\;X^D$) were identified. In addition, a genetically controlled polymorphism of post-LG was found for the first time in sow's milk protein. Three different phenotypes (AA, AB and BB) were designated $post-LG^A$ and $post-LG^B$. Of the five marker loci examined, $\alpha$-LA locus was observed to lack any individual variation in all breeds studied. All populations were in Hardy-Weinberg equilibrium for all loci. There were marked breed differences for phenotype and gene frequencies in the post-LG and X-protein marker loci. However, there were little differences between breeds in the gene frequencies at the $\beta$-CN and $\beta$-LG marker loci.