• 제목/요약/키워드: degree of protein hydrolysis

검색결과 101건 처리시간 0.018초

효소처리한 참깨박 농축단백질의 가수분해정도에 따른 기능성 (functional Properties of Sesame Protein Concentrate as Degree of Hydrolysis by Enzyme Treatments)

  • 윤시혜;박정륭;전정례
    • 동아시아식생활학회지
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    • 제4권3호
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    • pp.87-96
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    • 1994
  • This study was carried out to investigate the effect of hydrolysis by proteolytic enzymes on the functional properties of sesame protein concentrate. Sesame protein concentrate was hydrolyzed with papain, pepsin and trypsin to obtain 10% and 20% degree of hydrolysis. The nirogen solubility in water was increased with increasing the degree of hydrolysis. Bulk density was increased by enzymatic hydrolysis but water absorption capacity was increased only in the case of pepsin-hydrolyzed SPC. Higher fat absorption capacity was found in SPC with 10% DH than SPC with 20% DH. Emulsifying activity was also increased by enzymatic hydrolysis except SPC with 10% DH by papain.

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우유 단백질의 Allergenicity에 관한 연구 (A Study on the Allergenicity of Milk Protein)

  • 정은자
    • 한국식품영양학회지
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    • 제8권2호
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    • pp.79-87
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    • 1995
  • It is generally known that the protein of talk has allergenicity and the allerenicity Induces allergic diseases. Finding methods to reduce the allergenicity of the food and develop methods to make low allergic food is the purpose of this study. For this study, 1 tried various experimental methods : heat treatment, irradation with ultraviolet and microwaves treatment with polyphosphate, enzyme hydrolysis and PCA inhibition test using guinea pigs and degrees of hydrolysis. The results obtained are as follows. Heat treatment reduced allergenicity of milk protein. The higher the heat, the better the effect. Irradiating with ultraviolet and microwave increased both the degree of protein hydrolysis and PCA inhibition reduced the allergenicity. Ultraviolet was more effective than microwaves on milk protein. Enzyme treatment increased the degree of hydrolysis and PCA inhibition, and reduced allergenicity considerably. Neutrase was more effective than alcalase on milk protein. Adding Polyphosphate did not induced protein hydrolysis, but increased PCA inhibition and reduced allergenicity.

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Process Development for the Enzymatic Hydrolysis of Food Protein: Effects of Pre-treatment and Post-treatments on Degree of Hydrolysis and Other Product Characteristics

  • Chae, Hee-Jeong;In, Man-Jin;Kim, Min-Hong
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제3권1호
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    • pp.35-39
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    • 1998
  • An enzymatic process was developed to produce protein hydrolysater form defatted soya protein. Various unit operations were tried, and the effects of pre- and post-treatments on the product characteristics such as degree of hydroylsis (DH), free amino acid content (%FAA) and average molecular weight (MW) were investigated. The use of acid washes showed no difference in %DH. Increasing pH during pre-cooking gave lower %DH. Alkaline cooking made too much insoluble protein, thus the protein yield was too small. A better hydrolysis with more acceptable taste was obtained when the combination of Neutrase/Alcalase/Flavourzyme was used in place of Alcalase/Flavourzyme combination; Untoasted defatted soya was more effective on the proteolysis than toasted one. The MW of the evaporated and spray dried product was higher than that of undried product, due to precipitation of low-solubility components. When ultrafiltration and the product concentration carried out the product separation by reverse osmosis, the solubility and the taste of the product were improved. The difference between enzyme hydrolysate and acid hydrolysate was significant in free amino acid composition, especially in tyrosine, phenylalanine, glutamine and asparagine.

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유채단백질의 단백효소에 의한 가수분해 조건 (The Hydrolysis Conditions of Rapeseed Protein by Pronase)

  • 김충희;김효선;정용현;강영주
    • 한국식품영양과학회지
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    • 제21권5호
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    • pp.513-518
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    • 1992
  • 탈지유채박(Brassica napus var. Youngsan)으로부터 추출, 정제하여 얻어진 유채단백질을 효소로 가수분해하기 위한 최적조건에 대하여 검토하였다. Pronase가 유채단백질에서 alcalase, neutrase보다 높은 활성을 나타내었고, 유채단백질의 가열처리는 pronase의 활성을 감소시켰다. 또한 유채단백질의 가수분해도는 완충액보다는 증류수에서 더 높은 결과를 얻었다. 시간별로는 1시간까지는 급속히 반응이 일어나나 그 이후는 완만해졌다. Pronase에 의한 유채단백질의 가수분해 최적조건은 $40^{\circ}C$와 pH 8.0이었고 효소 대 기질의 비와 기질 농도는 각각 1/100(w/w), 1%(w/v)이었다. 이와 같은 조건하에서 Km은 3.48%(w/v)를 얻었다.

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가수분해 식물성 단백질의 효소적 생산을 위한 효소 반응 시스템의 최적화 (Optimization of Enzymatic Treatment for the Production of Hydrolyzed Vegetable Protein)

  • 채희정;인만진;김민홍
    • 한국식품과학회지
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    • 제29권6호
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    • pp.1125-1130
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    • 1997
  • 효소 분해에 의해 HVP를 생산하는데 있어서 여러 가지 효소의 조합, 효소 첨가 순서, pH, 산세척 등이 가수분해에 미치는 효과를 검토하였다 Endoprotease으로서 Neutrase와 Alcalase를 혼합하여 사용하는 것이 Alcalase를 단독 사용하는 것 보다 가수분해도가 높았으며 exoprotease인 Flavourzyme을 이용하여 2차 가수분해함으로써 60%이상의 가수분해도를 얻을 수 있었다. 2차 가수분해 시 원심분리에 의해 미반응 불용 성분을 제거하는 것은 가수분해도에 큰 영향을 미치지 않았고, 1차 가수분해 후 2차 원심분리의 수세수를 원료 현탁에 재사용하였을 경우 가수분해도 및 단백질 회수율을 높일 수 있었다. Ca이온의 첨가에 의한 Neutrase의 안정화 효과는 가수분해도에 큰 영향을 미치지 않았다. 탄수화물 분해효소의 사용과 산세척의 반복에 의해 가수분해도와 생산물의 단백질 함량이 각각 증가함을 알 수 있었다. Endoprotease과 exoprotease을 별도로 각각 처리하기보다는 동시 처리하는 것이 가수분해에 효율적이었다.

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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.

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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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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효소 처리된 닭고기 부산물에서 헝성된 pyrazines의 비교 (Comparison of Pyrazines Formed in Chicken By-Products Hydrolyzed by Enzymes)

  • 손성희;조인희;김영석
    • 한국식품조리과학회지
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    • 제20권3호
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    • pp.265-270
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    • 2004
  • To investigate the formation of pyrazines, by-products of chicken were hydrolyzed by protease/peptidase for 4, 8 and 24 hours, after which the hydrolysates were heated with glucose, fructose and xylose, respectively, at l80$^{\circ}C$ for l00min. The formation of pyrazines showed a significant difference by quality and quantity according to the degree of protein hydrolysis. Especially, the formation of 2-methyl pyrazine and 2-ethyl-5-methyl pyrazine was considerably affected by, the degree of protein hydrolysis. Also, 3-ethyl-5-methyl pyrazine, 2-butyl-3-methyl pyrazine, 2-butyl-3,5-dimethyl pyrazine, methyl pyrazine, and 3-ethyl-5-methyl pyrazine were identified only in the hydrolysates for 24 hours.

Angiotensin I Converting Enzyme Inhibitory Activity of Krill (Euphausia superba) Hydrolysate

  • Kim Dong-Soo;Park Douck-Choun;Do Jeong-Ryong
    • Fisheries and Aquatic Sciences
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    • 제5권1호
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    • pp.21-27
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    • 2002
  • Angiotensin I converting enzyme inhibitory activities of shelled krill (Euphausia superba) hydrolysates by autolysis and by hydrolysis with commercial proteases were analyzed. Among the proteases, Alcalase was the most effective protease for the hydrolysis of krill considering the degree of hydrolysis $(87.5\%)$ and the ACE inhibitory activity $(60\%)$. Four hour hydrolysis suggested as the most suitable and economic. In order to establish the optimum hydrolysis condition of krill, degree of hydrolysis and ACE inhibitory activity as affected by Alcalase concentration and water amount added were statistically analyzed by response surface methodology (RSM). The optimum hydrolysis condition was $2.0\%$ Alcalase hydrolysis in 2 volumes (v/w) of water at $55\% for 4 hr. The hydrolysate prepared from the optimum hydrolysis condition was fractionated by molecular weight. The lower molecular weight fraction showed the higher ACE inhibitory activity. $IC_{50}$ of the fraction under 500 Da was 0.57mg protein/mL.