• 제목/요약/키워드: Milk Proteins

검색결과 227건 처리시간 0.028초

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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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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2-DE and MALDI-TOF MS-based identification of bovine whey proteins in milk collected soon after parturition

  • Lee, Jae Eun;Lin, Tao;Kang, Jung Won;Shin, Hyun Young;Lee, Joo Bin;Jin, Dong Il
    • 농업과학연구
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    • 제45권4호
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    • pp.635-643
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    • 2018
  • Bovine milk is widely consumed by humans and is a primary ingredient of dairy foods. Proteomic approaches have the potential to elucidate complex milk proteins and have been used to study milk of various species. Here, we performed a proteomic analysis using 2-dimensional electrophoresis (2-DE) and matrix assisted laser desorption ionization-time of flight mass spectrometer (MALDI-TOF MS) to identify whey proteins in bovine milk obtained soon after parturition (bovine early milk). The major casein proteins were removed, and the whey proteins were analyzed with 2-dimensional polyacrylamide gel electrophoresis (2-D PAGE). The whey proteins (2 mg) were separated by pI and molecular weight across pH ranges of 3.0 - 10.0 and 4.0 - 7.0. The 2-DE gels held about 300 to 700 detectable protein spots. We randomly picked 12 and nine spots that were consistently expressed in the pH 3.0 - 10.0 and pH 4.0 - 7.0 ranges, respectively. Following MALDI-TOF MS analysis, the 21 randomly selected proteins included proteins known to be present in bovine milk, such as albumin, lactoferrin, serum albumin precursor, T cell receptor, polymeric immunoglobulin receptor, pancreatic trypsin inhibitor, aldehyde oxidase and microglobulin. These proteins have major functions in immune responses, metabolism and protein binding. In summary, we herein identified both known and novel whey proteins present in bovine early milk, and our sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed their expression pattern.

Evaluation of Physicochemical and Textural Properties of Low-Fat/Salt Sausages Manufactured with Two Levels of Milk Proteins

  • Lee, Hong-C.;Chin, Koo-B.
    • 한국축산식품학회:학술대회논문집
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    • 한국축산식품학회 2004년도 제34차 추계 국제 학술대회
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    • pp.218-222
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    • 2004
  • Low-fat (< 3%)/salt(< 1%) sausages were manufactured with two levels (1, 2%) of milk proteins(whey protein and sodium caseinate) to compensate for the textural problems due to reduced fat and salt(%). The addition of two levels of milk proteins into these meat products did not affect the most physicochemical and textural properties. As compared to regular-fat counterpart, higher expressible moisture of low-fat/salt sausages were observed. In addition, low-fat/salt sausages containing more than 2% of milk proteins reduced the textural hardness and gumminess, resulting in significantly lower these values, as compared to regular-fat counterparts. These results indicated that the low-fat/salt sausages were successfully manufactured with the addition of these milk proteins at the lower than 1% to improve the textural difference, however further research will be performed to improve the water holding capacity in these products.

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Chemical Composition, Nitrogen Fractions and Amino Acids Profile of Milk from Different Animal Species

  • Rafiq, Saima;Huma, Nuzhat;Pasha, Imran;Sameen, Aysha;Mukhtar, Omer;Khan, Muhammad Issa
    • Asian-Australasian Journal of Animal Sciences
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    • 제29권7호
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    • pp.1022-1028
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    • 2016
  • Milk composition is an imperative aspect which influences the quality of dairy products. The objective of study was to compare the chemical composition, nitrogen fractions and amino acids profile of milk from buffalo, cow, sheep, goat, and camel. Sheep milk was found to be highest in fat ($6.82%{\pm}0.04%$), solid-not-fat ($11.24%{\pm}0.02%$), total solids ($18.05%{\pm}0.05%$), protein ($5.15%{\pm}0.06%$) and casein ($3.87%{\pm}0.04%$) contents followed by buffalo milk. Maximum whey proteins were observed in camel milk ($0.80%{\pm}0.03%$), buffalo ($0.68%{\pm}0.02%$) and sheep ($0.66%{\pm}0.02%$) milk. The non-protein-nitrogen contents varied from 0.33% to 0.62% among different milk species. The highest r-values were recorded for correlations between crude protein and casein in buffalo (r = 0.82), cow (r = 0.88), sheep (r = 0.86) and goat milk (r = 0.98). The caseins and whey proteins were also positively correlated with true proteins in all milk species. A favorable balance of branched-chain amino acids; leucine, isoleucine, and valine were found both in casein and whey proteins. Leucine content was highest in cow ($108{\pm}2.3mg/g$), camel ($96{\pm}2.2mg/g$) and buffalo ($90{\pm}2.4mg/g$) milk caseins. Maximum concentrations of isoleucine, phenylalanine, and histidine were noticed in goat milk caseins. Glutamic acid and proline were dominant among non-essential amino acids. Conclusively, current exploration is important for milk processors to design nutritious and consistent quality end products.

우유의 생리활성 물질 (Bioactive Components in Milk)

  • 김근배
    • Journal of Dairy Science and Biotechnology
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    • 제28권1호
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    • pp.43-52
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    • 2010
  • In addition to the nutritional values, milk has a wide range of bioactive compounds which have been found to be increasingly important for physiological and biochemical functions on human metabolism and health. Bioactive components in milk comprise specific proteins, peptides, lipids and carbohydrates. Especially, milk proteins are known to exert a wide range of nutritional, functional, and biological activities. And milk proteins are considered the most important source of bioactive peptides, including antihypertensive, antithrombotic, antimicrobial, antioxidative, immunomodulatory, and opioid peptides. Many ingredients containing specific bioactive peptides derived from milk protein hydrolysates have been launched on the market and are currently under development. In future studies more emphasis should be given to the health-promoting effect in the well-defined human clinical studies for the successful development of function foods based on the milk-derived bioactive components.

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Effects of Milk Proteins and Gums on Quality of Bread Made from Frozen Dough following Freeze-Thaw Cycles

  • Yun, Young;Eun, Jong-Bang
    • Food Science and Biotechnology
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    • 제15권5호
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    • pp.805-813
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    • 2006
  • The quality of frozen bread dough made with the milk proteins casein (C), whey (W), and the gums sodium alginate (A) and ${\kappa}$-carrageenan (K), was investigated to develop methods to suppress the deterioration of the frozen dough quality. The control had a lower dough volume than dough with additives during freeze-thaw cycles. In bread stored at $5^{\circ}C$, the moisture content of bread prepared with whey plus sodium alginate (WA) decreased less than that of the control. The control also had a lower specific loaf volume than breads made with added milk proteins and gums. The hardness of the control bread and bread made with casein plus sodium alginate (CA) and whey plus ${\kappa}$-carrageenan (WK) increased during freeze-thaw cycles, although that of the control increased more than the others. There was no significant difference in sensory preference among breads with and without milk proteins and gums. Addition of CA and WA improved the baking quality by reducing the deterioration of frozen dough and retarding the staling of bread.

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.

Development and evaluation of probiotic delivery systems using the rennet-induced gelation of milk proteins

  • Ha, Ho-Kyung;Hong, Ji-Young;Ayu, Istifiani Lola;Lee, Mee-Ryung;Lee, Won-Jae
    • Journal of Animal Science and Technology
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    • 제63권5호
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    • pp.1182-1193
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    • 2021
  • The aims of this study were to develop a milk protein-based probiotic delivery system using a modified rennet-induced gelation method and to determine how the skim milk powder concentration level and pH, which can affect the rennet-induced intra- and inter-molecular association of milk proteins, affect the physicochemical properties of the probiotic delivery systems, such as the particle size, size distribution, encapsulation efficiency, and viability of probiotics in simulated gastrointestinal tract. To prepare a milk protein-based delivery system, skim milk powder was used as a source of milk proteins with various concentration levels from 3 to 10% (w/w) and rennet was added to skim milk solutions followed by adjustment of pH from 5.4 or 6.2. Lactobacillus rhamnosus GG was used as a probiotic culture. In confocal laser scanning microscopic images, globular particles with a size ranging from 10 ㎛ to 20 ㎛ were observed, indicating that milk protein-based probiotic delivery systems were successfully created. When the skim milk powder concentration was increased from 3 to 10% (w/w), the size of the delivery system was significantly (p < 0.05) increased from 27.5 to 44.4 ㎛, while a significant (p < 0.05) increase in size from 26.3 to 34.5 ㎛ was observed as the pH was increased from 5.4 to 6.4. An increase in skim milk powder concentration level and a decrease in pH led to a significant (p < 0.05) increase in the encapsulation efficiency of probiotics. The viability of probiotics in a simulated stomach condition was increased when probiotics were encapsulated in milk protein-based delivery systems. An increase in the skim milk powder concentration and a decrease in pH resulted in an increase in the viability of probiotics in simulated stomach conditions. It was concluded that the protein content by modulating skim milk powder concentration level and pH were the key manufacturing variables affecting the physicochemical properties of milk protein-based probiotic delivery systems.

출산 후 경과한 날에 따른 한국인 산모의 모유 단백체 분석 (Proteomic analysis of Korean mothers' human milk at different lactation stages; postpartum 1, 3, and 6 weeks)

  • 박종문;이후근;송승현;한원호;김미정;이주현;강남미
    • 분석과학
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    • 제30권6호
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    • pp.348-354
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    • 2017
  • 이 연구는 출산 후 1, 3, 6주가 경과한 산모에서 얻은 모유의 단백체 발현 양상과 과 발현 단백질을 검출하는 것을 목적으로 하였다. 샷 건 정량 단백체 분석법을 이용하여 모유 중의 단백질을 동정하였고, 각 수유단계 간에 정량적 비교를 하였다. 각 주의 모유 샘플은 두 명의 산모로부터 얻어진 모유를 혼합하였고, 각 샘플 마다 3회 반복 실험을 하였다. Casein은 모유 내에 가장 많이 존재하는 단백질로서 실험의 정확성을 위하여 제거하였고, 트립신을 이용한 절편 화로 모유 단백질들을 펩타이드로 변환하였다. 처리된 펩타이드들은 역상 C18 미세관 크로마토그래피 및 이온-트랩 질량분석기를 이용하여 분석하였으며, Spectra Counting으로 단백질의 정량적 비교를 하였다. 각 샘플 당, 80-109 개의 단백질을 중복 제거한 후 동정하였다. 당화 단백질, metabolic enzyme, 및 lactoferrin, Carboxylic ester hydrolase, Clusterin을 포함하는 chaperon 효소들이 주로 검출되었다. 각 반복실험에서 재현성 있게 검출되는 63개의 단백질에 대한 정량적 비교분석 결과 25개의 단백질이 통계적으로 유의하게 수유단계에 따라 변화하는 것을 확인할 수 있었고, 특히 Ig lambda-7 chain C region과 Tenascin은 시간에 따라 현저하게 감소하였다. 향후 이와 같은 수유 단계에 따른 모유 내 단백의 변화가 생리적으로 가지는 의미에 관하여 추가적인 연구가 필요하다 생각된다.