• 제목/요약/키워드: -lactoglobulin

검색결과 96건 처리시간 0.023초

Effects of Genetic Variants of ${\kappa}$-casein and ${\beta}$-lactoglobulin and Heat Treatment of Milk on Cheese and Whey Compositions

  • Choi, J.W.;Ng-Kwai-Hang, K.F.
    • Asian-Australasian Journal of Animal Sciences
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    • 제15권5호
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    • pp.732-739
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    • 2002
  • Milk samples with different phenotype combination of $\{kappa}$-casein and ${\beta}$-lactoglobulin and different preheating temperatures of 30, 70, 75 and $80^{\circ}C$ were used for cheesemaking under laboratory conditions. For the 853 batches of cheese, mean composition was 59.64% total solids, 30.24% fat and 23.66% protein, and the whey contained 6.93% total solids, 0.30% fat and 0.87% protein. Least squares analysis of the data indicated that heating temperature of the milk and ${\kappa}$-CN/${\beta}$-LG phenotypes had significant effects on cheese and whey compositions. The total solids, fat and protein contents of cheese were negatively correlated with preheating temperatures of milk. Cheese from BB/BB phenotype milk had the highest and those from AA/AA phenotype milk had the lowest concentrations of total solids, fat and protein. Mean recoveries of milk components in the cheese were 53.71% of total solids, 87.15% of fat, and 80.32% of protein. For the 10 different types of milk, maximum recoveries of milk components in cheese occurred with preheating temperature of $70^{\circ}C$ or $75^{\circ}C$ and lowest recoveries occurred at $80^{\circ}C$. The whey averaged 6.94% total solids, 0.30% fat and 0.87% protein. Losses of milk components in the whey were lowest for milk preheated at $80^{\circ}C$ and for milk containing the BB/BB phenotype.

Comparative and Structural Analysis of the Interaction between β-Lactoglobulin type A and B with a New Anticancer Component (2,2'-Bipyridin n-Hexyl Dithiocarbamato Pd(II) Nitrate)

  • Divsalar, A.;Saboury, A.A.;Mansoori-Torshizi, H.;Hemmatinejad, B.
    • Bulletin of the Korean Chemical Society
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    • 제27권11호
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    • pp.1801-1808
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    • 2006
  • The interaction between whey carrier protein $\beta$-lactoglobulin type A and B (BLG-A and -B) and 2,2'-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate (BPHDC-Pd(II)), a new heavy metal complex designed for anticancer property, was investigated by fluorescence spectroscopy combined with chemometry and circular dichroism (CD) techniques. A strong fluorescence quenching reaction of BPHDC-Pd(II) to BLG-A and -B was observed. Hence, BPHDC-Pd(II) complex can be bound to both BLG-A and -B, and quench the fluorescence spectra of the proteins. The quenching constant was determined using the modified Stern-Volmer equation. The binding parameters were evaluated by fluorescence quenching method. The results of binding study provided evidences presence of two and three sets of binding sites on the BLG-B and -A, respectively, for BPHDC-Pd(II) complex. Using fluorescence spectroscopy and chemometry, the ability of BLG-A and -B to form an intermediate upon interaction with BPHDC-Pd(II) complex was assessed. CD studies displayed that under influence of different concentrations of BPHDC-Pd(II) complex, the regular secondary structure of BLG-B had no significant changes, whereas for BLG-A a transition from $\alpha$-helix to $\beta$-structure was appeared. The results for both of BLG-A and -B displayed that BPHDC-Pd(II) complex can induce a conformational transition from the native form to an intermediate state with a slightly opened conformation, which is detectable with chemometry analyses.

Poly(ethyleneglycol)과 인산염용액이 형성하는 2상계에서의 단백질 분획에 관한 연구 (Protein Partition in an Aqueous Poly (ethyleneglycol)-salt Two-phase System)

  • 이삼빈;이철호
    • 한국식품과학회지
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    • 제19권4호
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    • pp.285-289
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    • 1987
  • Poly(ethylene glycol)과 인산염 용액(PPB)이 형성 하는 액상 이상계에서 단백질의 분획 거동을 관찰하였다. PEG(12%)/PPB(12%) 액상 이상계에서 단백질의 표면 소수성이 다른 BSA, ${\beta}-lactoglobulin$, ovalbumin 모두 PPB-rich phase인 하층부로 몰려 그 분획계수는 대단히 낮았다. PPB의 농도를 15%로 증가 시키면 하층부의 전위는 +50mV 에서 0으로 낮아져 단백질의 분획계수가 다소 증가하는 경향을 나타내었다. PPB의 제2인산염과 제일인산염의 몰 비율을 1.43에서 9.55로 증가시키면 이상계의 상 하층부 부피비(Vt/Vb)가 다소 감소되면서 분획계수는 증가하였다. PPB농도를 $14{\sim}26%$로 증가시키면 이상계의 부피비는 1.5에서 0.39로 현저히 감소하면서 단백질의 분획계수는 ${\beta}-lactoglobalin$의 경우 74배, BSA 32배, ovalbumin 12배, lysozyme 5배로 크게 증가하였다.

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Production and Characterization of Beta-lactoglobulin/Alginate Nanoemulsion Containing Coenzyme Q10: Impact of Heat Treatment and Alginate Concentrate

  • Lee, Mee-Ryung;Choi, Ha-Neul;Ha, Ho-Kyung;Lee, Won-Jae
    • 한국축산식품학회지
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    • 제33권1호
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    • pp.67-74
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    • 2013
  • The aims of this research were to produce oil-in-water ${\beta}$-lactoglobulin/alginate (${\beta}$-lg/Al) nanoemulsions loaded with coenzyme $Q_{10}$ and to investigate the combined effects of heating temperature and alginate concentration on the physicochemical properties and encapsulation efficiency of ${\beta}$-lg/Al nanoemulsions. In ${\beta}$-lg/Al nanoemulsions production, various heating temperatures (60, 65, and $70^{\circ}C$) and alginate concentrations (0, 0.01, 0.03, and 0.05%) were used. A transmission electron microscopy was used to observe morphologies of ${\beta}$-lg/Al nanoemulsions. Droplet size and zeta-potential values of ${\beta}$-lg/Al nanoemulsions and encapsulation efficiency of coenzyme $Q_{10}$ were determined by electrophoretic light scattering spectrophotometer and HPLC, respectively. The spherically shaped ${\beta}$-lg/Al nanoemulsions with the size of 169 to 220 nm were successfully formed. The heat treatments from 60 to $70^{\circ}C$ resulted in a significant (p<0.05) increase in droplet size, polydispersity, zeta-potential value of ${\beta}$-lg/Al nanoemulsions, and encapsulation efficiency of coenzyme $Q_{10}$. As alginate concentration was increased from 0 to 0.05%, there was an increase in the polydispersity index of ${\beta}$-lg/Al nanoemulsions and encapsulation efficiency of coenzyme $Q_{10}$. This study demonstrates that heating temperature and alginate concentration had a major impact on the size, polydispersity, zeta-potential value and encapsulation efficiency of coenzyme $Q_{10}$ in ${\beta}$-lg/Al nanoemulsions.

Bioaccessibility of β-Lactoglobulin Nanoemulsions Containing Coenzyme Q10: Impact of Droplet Size on the Bioaccessibility of Coenzyme Q10

  • Ha, Ho-Kyung;Lee, Mee-Ryung;Lee, Won-Jae
    • 한국축산식품학회지
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    • 제38권6호
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    • pp.1294-1304
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    • 2018
  • The aims of this research were to examine the effect of heating temperature (65, 75, and $85^{\circ}C$) and $CaCl_2$ concentration level (3, 4, and 5 mM) on the physicochemical properties of ${\beta}$-lactoglobulin (${\beta}$-lg) nanoemulsions (NEs) and to study how the droplet size of NEs affects the bioaccessibility (BA) of coenzyme $Q_{10}$ ($CoQ_{10}$). The droplet size of NEs and BA of $CoQ_{10}$ was assessed by particle size analyzer and UV-Vis spectrophotometer, respectively. An increase in heating temperature and $CaCl_2$ concentration level resulted in a significant (p<0.05) increase in the droplet size of NEs while there were no significant differences in polydispersity index and zeta-potential of NEs. When NEs containing $CoQ_{10}$ were incubated in simulated small intestinal phases, an increase in the droplet size and polydispersity index of NEs was observed. This indicated that NEs were not stable in small intestine and digestion of NEs occurred. As heating temperature and $CaCl_2$ concentration level were decreased, a significant (p<0.05) increase in BA of $CoQ_{10}$ was observed. There was a significant (p<0.05) increase in BA of $CoQ_{10}$ with a decrease in the droplet size of NEs. In conclusion, heating temperature and $CaCl_2$ concentration level were key-parameters affecting the initial droplet size of NEs and BA of $CoQ_{10}$ was negatively correlated with initial droplet size of NEs.

상업적 응유효소의 탈지유에 대한 단백질 분해 작용 (Comparative Study of Proteolytic Activities of Some Commercial Milk Clotting Enzymes on Bovine Skim Milk)

  • 신현수;김상범;임종우
    • Journal of Animal Science and Technology
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    • 제44권6호
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    • pp.801-808
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    • 2002
  • 상업적 단백질 분해 효소에 0.02% $CaCl_2$를 첨가하여 응유 활성화를 시킨 탈지유에 대한 분해 작용의 결과를 요약하면 다음과 같다. 다양한 효소별 가수분해 시간에 따른 가수분해도는 미생물 유래 효소와 trypsin은 pepsin과 papain W-40보다 높은 분해도를 나타냈다. 12% TCA 용액에 가용성인 NPN의 양은 trypsin이 가장 높은 분해도를 나타내었고 rennet과 pepsin이 가장 낮은 분해도를 보였다. 전기영동에 있어서 trypsin과 protease S는 $\alpha$- lactalbumin을 분해하였고 papain w-40은 $\beta$- lactoglobulin을 미약하게 분해하였으며 neutrase 1.5는 90분 이후부터 $\alpha$-lactalbumin과 $\beta$-lactoglobulin을 분해하였다. Rennet과 비교한 전기영동상에서는 rennet에 의해 분해 되지 않은 ${\alpha}_s$- casein과 $\beta$-casein을 trypsin과 protease S가 다량 분해하였고 $\kappa$-casein은 rennet에 비해 papain W-40이 상당 수준의 분해상을 나타내었다. 이상의 결과 가수분해도 및 NPN 양은 trypsin, neutrase 1.5 및 protease S가 다른 효소에 비해 높게 나타났으며, 전기영동상에서는 pepsin과 neutrase 1.5가 rennet과 유사한 경향을 나타내었다.

국내 주요 알레르기 원인 식품에 대한 조사 (Study of the Most Common Allergic Foods in Korea)

  • 손대열;윤광로;이상일
    • 한국식품과학회지
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    • 제34권5호
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    • pp.885-888
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    • 2002
  • 본 연구의 목적은 우리나라의 식품으로 인한 알레르기 발생 빈도를 파악하며 주 알레르기 원인 식품을 파악하는 것이다. 삼성서울병원에 알레르기 증상으로 1998년 5월부터 2001년 8월까지 방문한 환자의 혈청 특이 IgE 항체를 대상 식품에 대해 CAP 시스템을 이용하여 조사하였다. 총 9054건의 CAP 검사가 난백, 난황, 우유, ${\alpha}-lactalbumin,\;{\beta}-lactoglobulin$, 카세인, 밀, 쌀, 메밀, 대두, 복숭아, 게, 새우, 돼지고기, 쇠고기, 닭고기, 참치, 연어, 고등어 및 혼합식품에 대해 1707명의 방문자를 중심으로 이루어졌다. 조사 결과 CAP 수치가 +2(0.7 U/mL) 이상인 값을 양성으로 판단하였으며 CAP 검사결과 11.3% (1022/9054건)가 양성이었다. 각 알레르기 원인 식품별로는 난백이 336건, 우유가 266건, 난황이 95건, 대두가 76건 ${\alpha}-lactalbumin$ 이 69건, 카세인이 61건, ${\beta}-lactoglobulin$이 58건, 메밀이 39건, 밀이 12건, 쇠고기 3건, 게 2건, 쌀, 새우, 돼지고기, 닭고기, 고등어 가 각각 1건, 복숭아, 참치, 연어 혼합식품이 각각 0건이었다. 우리나라에서 제일 많은 5대 알레르기 원인 식품으로 계란, 우유, 대두, 메밀 및 밀이 확인되었으며 환자 1인당 평균 2가지의 알레르기 원인 식품을 갖고 있는 것으로 확인되었다.

한국재래산양 β-lactoglobulin 유전자 5'flanking 영역의 염기서열 분석 (Nucleotide Sequences of β-lactoglobulin Gene 5'Flanking Region in Korean Native Goat)

  • 류승희;한성욱;서길웅;상병찬
    • 농업과학연구
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    • 제28권2호
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    • pp.78-84
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    • 2001
  • 본 연구는 한국 재래산양의 ${\beta}$-lactoglobulin(${\beta}$-LG) 유전자 발현조절부위의 특성을 구명하기 위하여 PCR기법으로 specific primer를 이용하여 ${\beta}$-LG 발현조절부위를 증폭한 후 염기서열을 분석하여 Sheep종의 ${\beta}$-LG유전자 발현조절부위의 염기서열상의 차이를 분석하였다. 한국 재래산양의 genomic DNA로부터 PCR기법을 이용하여 ${\beta}$-LG 유전자 발현조절부위를 증폭한 결과 Sheep종에서 보고된 바와 같이 1,077bp의 단편크기로 증폭되었음을 확인할 수 있었다. Sheep종에서 보고된 ${\beta}$-LG 발현조절 부위의 염기서열과 한국재래산양에서 분석된 염기서열간의 차이는 총 897개의 염기중 46개의 nucleotide에서 차이를 나타내어 94.9%의 상동성을 보였다. 특히 한국재래산양과 Sheep종간 염기서열상의 차이는 Sheep종의 T염기가 재래산양의 C염기로 치환되었거나 반대로 Sheep종의 C염기가 재래산양에서 T염기로 치환되어 있음을 확인할 수 있었다. 이상의 결과에서 ${\beta}$-LG유전자 발현조절부위의 염기서열은 재래산양과 Sheep 종간에 높은 상동성을 보였으나 이들 종간의 발현조절부위의 염기서열상의 차이에 대한 유전자 발현조절 관계와 전사요소는 앞으로 연구가 더 진행되어야 할 것으로 사료된다.

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The Relation between Genetic Polymorphism Markers and Milk Yield in Brown Swiss Cattle Imported to Slovakia

  • Chrenek, P.;Huba, J.;Vasicek, D.;Peskovicova, D.;Bulla, J.
    • Asian-Australasian Journal of Animal Sciences
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    • 제16권10호
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    • pp.1397-1401
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    • 2003
  • The aim of this study was to determine genotypes of four genetic markers and to investigate their association with milk production traits in Brown Swiss cattle imported to Slovakia. The bovine $\kappa$-casein, $\beta$-lactoglobulin, growth hormone and prolactin genotypes of 107 cows were identified by polymerase chain reaction. Effects all four genetic markers on milk, fat, protein and lactose yields and fat, protein and lactose percentage were estimated from a data set of 249 lactations. The frequency of desirable B allele of $\kappa$-casein gene to milk production was 0.46, alleles A of $\beta$-lactoglobulin gene was 0.55, allele and L of growth hormone gene was 0.45 and allele A and B of bovine prolactin gene were 0.61 and 0.39. The results of milk production obtained in our work showed that BB genotypes of $\kappa$-CN gene, AA genotypes of $\beta$-LG gene, LL genotypes of bGH gene were significantly associated with better milk production traits, mainly about the fat content. Association of a bovine prolactin genotypes with milk production were not found.

Comparison of Size-Exclusion Chromatography and Flow Field-Flow Fractionation for Separation of Whey Proteins

  • Kang, Da-Young;Moon, Jae-Mi;Lee, Seung-Ho
    • Bulletin of the Korean Chemical Society
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    • 제32권4호
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    • pp.1315-1320
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    • 2011
  • Whey protein (WP) is a mixture of proteins, and is of high nutritional values. WP has become an important source of functional ingredients in various health-promoting foods. In this study, size-exclusion chromatography (SEC) and asymmetrical flow field-flow fractionation (AsFlFFF) were used for separation and analysis of whey proteins. It was found that a lab-prepared WP from raw milk is mostly of ${\beta}$-lactoglobulin with small amount of higher molecular weight components, while a commercial whey protein isolate (WPI) powder contains relatively larger amount of components other than ${\beta}$-lactoglobulin, including IgG and protein aggregates. Results suggest that AsFlFFF provides higher resolution for the major whey proteins than SEC in their normal operation conditions. AsFlFFF could differentiate the BSA and Albumin, despite a small difference in their molecular weights, and also was able to separate much smaller amount of aggregates from monomers. It is noted that SEC was able to show the presence of low molecular weight components other than the major whey proteins in the WP samples, which AsFlFFF could not show, probably due to the partial loss of those low molecular weight species through the membrane.