• 제목/요약/키워드: protein hydrolysis

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달걀 단백질의 Allergenicity에 관한 연구 (A Study on the Allergenicity of Egg Protein)

  • 정은자
    • 한국식품영양학회지
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    • 제11권2호
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    • pp.228-236
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    • 1998
  • 달걀의 Allergenicity를 감소시킬 수 있는 방안을 강구하고자 물리적 처리, 축합 인산염 처리 및 효소처리를 하여 Guinea pig를 이용한 Passive Cutaneous Anaphylaxis(PCA) inhibition 실험과 Non Proteic Nitrogen(NPN)정량을 통한 가수분해율의 측정결과 다음과 같은 결론을 얻었다. 달걀의 allergenicity는 가열에 의해 감소하였으며 가열시간이 길수록 단백질 가수분해율 및 PCA inhibition을 증가 시켰다. Ultraviolet 조사와 Microwave 조사는 단백 가수분해율과 PCA inhibition을 증가 시켜서 allergenicity를 저하시켰으며 ultraviolet이 저해효과가 더 컸으며 부화 달걀은 allergenicity를 감소시키지 않은 것으로 나타났다. 효소처리는 단백질의 가수분해율 및 PCA inhibition을 증가 시키며 allergenicity를 현저히 감소시켰으며 alcalase의 재해효과가 더 컸다. Polyphosphate의 참가는 단백질의 가수분해는 유도하지 않았으나 PCA inhibition을 증가 시키며 allergenicity를 감소시켰다. Allergenicity를 감소시키기 위한 처리를 한 달걀 gel의 주사전자현미경 사진은 효소처리 시 표면이 밝게 나타나서 단백질이 분해되었음을 알 수 있었고 neutrase가 alcalase보다 밝게 나타났으나 반응시간의 증가에 따라 모든 효소 표면이 밝게 나타났다. Instron에서 달걀 gel의 경도를 측정한 결과 효소와의 반응시간이 길수록 경도가 감소하는 경향을 보였다.

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Characterization of Yeast Protein Hydrolysate for Potential Application as a Feed Additive

  • Ju Hyun Min;Yeon Ju Lee;Hye Jee Kang;Na Rae Moon;Yong Kuk Park;Seon-Tea Joo;Young Hoon Jung
    • 한국축산식품학회지
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    • 제44권3호
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    • pp.723-737
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    • 2024
  • Yeast protein can be a nutritionally suitable auxiliary protein source in livestock food. The breakdown of proteins and thereby generating high-quality peptide, typically provides nutritional benefits. Enzyme hydrolysis has been effectively uesed to generate peptides; however, studies on the potential applications of different types of enzymes to produce yeast protein hydrolysates remain limited. This study investigated the effects of endo- (alcalase and neutrase) and exotype (flavourzyme and prozyme 2000P) enzyme treatments on yeast protein. Endotype enzymes facilitate a higher hydrolysis efficiency in yeast proteins than exotype enzymes. The highest degree of hydrolysis was observed for the protein treated with neutrase, which was followed by alcalase, prozyme 2000P, and flavourzyme. Furthermore, endotype enzyme treated proteins exhibited higher solubility than their exotype counterparts. Notably, the more uniform particle size distribution was observed in endotype treated yeast protein. Moreover, compared with the original yeast protein, the enzymatic protein hydrolysates possessed a higher content of β-sheets structures, indicating their higher structural stability. Regardless of enzyme type, enzyme treated protein possessed a higher total free amino acid content including essential amino acids. Therefore, this study provides significant insights into the production of protein hydrolysates as an alternative protein material.

Volatile Compound, Physicochemical, and Antioxidant Properties of Beany Flavor-Removed Soy Protein Isolate Hydrolyzates Obtained from Combined High Temperature Pre-Treatment and Enzymatic Hydrolysis

  • Yoo, Sang-Hun;Chang, Yoon Hyuk
    • Preventive Nutrition and Food Science
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    • 제21권4호
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    • pp.338-347
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    • 2016
  • The present study investigated the volatile compound, physicochemical, and antioxidant properties of beany flavor-removed soy protein isolate (SPI) hydrolyzates produced by combined high temperature pre-treatment and enzymatic hydrolysis. Without remarkable changes in amino acid composition, reductions of residual lipoxygenase activity and beany flavor-causing volatile compounds such as hexanol, hexanal, and pentanol in SPI were observed after combined heating and enzymatic treatments. The degree of hydrolysis, emulsion capacity and stability, 2,2-diphenyl-1-picrylhydrazyl radical scavenging activity, and superoxide radical scavenging activity of SPI were significantly increased, but the magnitudes of apparent viscosity, consistency index, and dynamic moduli (G', G") of SPI were significantly decreased after the combined heating and enzymatic treatments. Based on these results, it was suggested that the enzymatic hydrolysis in combination with high temperature pre-treatment may allow for the production of beany flavor-removed SPI hydrolyzates with superior emulsifying and antioxidant functionalities.

Functional Characteristics of Whey Protein-Derived Peptides Produced Using Lactic Acid Bacteria Hydrolysis

  • Jae-Yong Lee;Dong-Gyu Yoo;Yu-Bin Jeon;Se-Hui Moon;Ok-Hee Kim;Dong-Hyun Lee;Cheol-Hyun Kim
    • Journal of Dairy Science and Biotechnology
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    • 제41권1호
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    • pp.34-43
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    • 2023
  • Hydrolysis of whey-derived proteins using lactic acid bacteria (LAB) utilizes the mass culture method and fermentation of LAB to produce effective bioactive peptides. Whey protein has the biological potential of its precursors, but the active fragments may not be released depending on the hydrolysis method. As an alternative to these problems, the nutritional and bioactive functionality of the hydrolysis method have been reported to be improved using LAB for whey protein. Peptide fractions were obtained using a sample fast protein liquid chromatography device. Antioxidant activity was verified for each of the five fractions obtained. In vitro cell experiments showed no cytotoxicity and inhibited nitric oxide production. Cytokine (IL [interleukin]-1α, IL-6, tumor necrosis factor-α) production was significantly lower than that of lipopolysaccharides (+). As a result of checking the amino acid content ratio of the fractions selected through the AccQ-Tag system, 17 types of amino acids were identified, and the content of isoleucine, an essential amino acid, was the highest. These properties show their applicability for the production of functional products utilizing dietary supplements and milk. It can be presented as an efficient method in terms of product functionality in the production of uniform-quality whey-derived peptides.

Evaluation of Protein Hydrolysis and Amino Acid Ratio among Different Goat Cuts by in vitro Digestion Model

  • Jei, Oh;Joohyun, Kang;Susie, Kim;Jeonghyun, Cho;Yohan, Yoon
    • 한국식품위생안전성학회지
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    • 제37권6호
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    • pp.411-417
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    • 2022
  • 본 연구는 생후 12개월령의 염소를 사용하여 앞다리, 뒷다리, 등심 및 갈비 부위로 분할하여 in vitro 소화실험을 통해 부위별 단백질 가수분해도 및 아미노산 조성을 조사하였다. 이 때, 소고기 및 돼지고기의 분할육을 이용하여 염소고기와 비교, 분석하였다. 염소고기 분할육 중 뒷다리(8.32%) 및 갈비(8.32%)가 가장 높게 단백질 가수분해도가 나타났으며, 염소고기의 갈비 부위는 갈비 분할육 중 가장 높은 단백질 가수분해율을 보였던 돼지고기(8.57%)와 유의 차가 없었다 (P>0.05). In vitro 소화 전에는 염소고기 분할 육 중 등심에서 글리신(11.03%)이, 앞다리에서 글루타민(53.44%)이 다른 고기 종류 및 분할육들에 비해 유의적으로 높은 비율로 포함된 것이 확인되었다(P<0.05). In vitro 소화 후에는 염소고기 갈비 부위에서 라이신(17.54%)이 가장 높은 비율로 포함된 것으로 확인되었으며, 소 갈비 부위보다 유의적으로 높았다(P<0.05). 본 연구는 염소고기 분할육의 단백질 가수분해도 및 아미노산 조성을 제공하며 단백질 소화양상 및 생체 이용률을 평가하기 위한 기초 자료로써 활용되어질 수 있을 것으로 사료된다.

Effects of injection of hydrolysis plasma protein solution on the antioxidant properties in porcine M. Longissimus Lumborum

  • Seo, Hyun-Woo;Seo, Jin-Kyu;Yang, Han-Sul
    • Journal of Animal Science and Technology
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    • 제58권8호
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    • pp.31.1-31.8
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    • 2016
  • Background: Plasma protein hydrolysates have been shown to possess antioxidant activity. However, no report has yet to examine the antioxidant effects of injection of plasma protein hydrolysates on meat quality. Therefore, in this study, the effects of injection of hydrolysis plasma protein solution on meat quality and storability were investigated in porcine M. longissimus lumborum. Methods: Twelve pigs were randomly selected at a commercial slaughter plant and harvested. Dissected loins were injected with one of five solutions: C- control (untreated), T1- 10 mM phosphate buffer solution (PBS), T2- 10 mM PBS with 0.01 % butylated hydroxytoluene, T3- 10 mM PBS with 5 % plasma proteins, and T4- 10 mM PBS with 5 % hydrolysis plasma proteins. Results: T3 and T4 induced greater reduction in protein content of the loin muscle than other treatments. T2 resulted in the lowest pH as well as highest cooking loss. After a storage period of 3-7 days, both lightness and redness of meat were unaffected by all injection treatments. However, yellowness was significantly elevated by treatment with T4 relative to the control. T4 also resulted in the lowest shear force (a measure of meat toughness), suggesting improvement of texture or tenderness. Further, T4 resulted in the most stable TBARS values during storage, indicating that this treatment might retard rancidity in meat. Conclusion: Injection of porcine M. longissimus lumborum with hydrolysis plasma protein solution could improve overall pork quality, including tenderness and storability.

Enzymatic Hydrolysis of Egg Yolk Protein in Continuous Packed Column Operation

  • Kang, Byung-Chul;Lee, Sang-Uk
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2003년도 생물공학의 동향(XIII)
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    • pp.485-489
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    • 2003
  • Enzymatic hydrolysis of egg yolk Protein was carried out in continuous packed column reactor Five supports for enzyme immobilization were evaluated in this study. We investigated the optimum operation variables - pH, temperature, and flow rate in continuous reactor operation.

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메주 단백질 가수분해 효소 처리가 탈지 우유 단백질의 응고물 형성 및 소화율에 미치는 영향 (Modifications of Skim Milk Protein by Meju Protease and Its Effect on Acid Clotting and Digestibility)

  • 이진실
    • Journal of Nutrition and Health
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    • 제26권8호
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    • pp.998-1005
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    • 1993
  • This study was attempted to investigate the effects of enzymatic modification of milk protein with Meju protease on its acid clotting and digestibility. The proteases used in this study were isolated from Meju(fermented soybeans) and had specific acticity of 250 units/mg protein at pH 7.0. These proteases were found to be at least 3 different isoenzymes of different pH optima(pH 4.0, 6.0, 10.0). The optimum temperature was 5$0^{\circ}C$. Hydrolyzed skim milk showed 30.5% degree of hydrolysis for 1 hr. and 36.4% degree of hydrolysis for 3.5 hrs. of protease treatment at pH 7.0. Upon acidification to pH 4.0, skim milk produced large and dense coagulum, but the coagulum was getting smaller by protease treatment. Generally, digestability of skim milk at pH 4.0 was lower than pH 2.0. At pH 4.0, native skim milk and control group had problem with hydrolysis of skim milk protein. Among protease treated groups, 1 hour treated skim milk was most effectively hyrolyzed at pH 4.0.

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Hydrolysis of Rice Bran Oil Using Immobilized Lipase in a Stirred-Batch Reactor

  • Murty, V.Ramachandra;Bhat, Jayadev;Muniswaran, P.K.A.
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제7권6호
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    • pp.367-370
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    • 2002
  • Candida cylindracea lipase was immobilized by adsorption on acid washed glass beads. It was observed that protein loading of the support depends on the size of the particle, with smaller particle containing higher amount of protein per unit weight. Initial reaction rate linearly varied up to enzyme concentration of 17.25 U/mL. Amount of free fatty acids produced was linearly proportional up to the enzyme loading of 1650 $\mu$g/g of bead. Achievement of chemical equilibrium took longer time in the case of less protein loading. Degree of hydrolysis was found to decrease in second and third consecutive batch operations on repeated use of immobilized lipase.

Enhancement of Water-solubilities of Protein-bound Polysaccharides Contained in the Basidiocarps of Ganoderma lucidum by Hydrolyzing with Chymotrypsin

  • Park, Won-Bong;Cheong, Jae-Yeon;Jung, Won-Tae
    • Archives of Pharmacal Research
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    • 제19권5호
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    • pp.423-428
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    • 1996
  • Optimum conditions for hydrolysis were investigated to enhance water-solubilities of protein-bound polysaccharides in the basidiocarps of Ganoderma lucidum by treating chymotrypsin. We also attempted with Ganoderma lucidum residue remaining after extracting hot water-soluble compoents in Ganoderma lucidum. After hydrolyzing under optimum conditions (20 ppm chymotrypsin, 2% Gampderma lucidum or 6% Ganoderma lucidum residue, at pH 10 and at $ 40^{\circ}C$), the amounts of total protein and carbohydrate of hydrolysate were measured. Michaelis constant, $K_{m}$, and maximum rate, $V_{max}$, calculated by Lineweaver-Buck plot for the hydrolysis of Ganoderma lucidum were 1.73% and 0.073%/min respectively and those for hydrolysis of Ganoderma lucidum residue were 2.40% and 0.033%/min respectively. The amount of polysaccharide isolated from Ganoderma lucidum (100 g) treated with chymotrypsin was only 3.07 g, but significantly increased amount (14.34 g) of polysaccharides was isolated from Ganoderma lucidum residue (100 g) treated with chymotrypsin. The protein-bound polysaccharide was isolated from the non-hydrolyzed and hydrolyzed sample and molecular weights of the polysaccharide were measured by Sepharose CL-48 gel filtration.

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