• 한국식품영양학회지
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• 제10권1호
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• pp.87-91
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• 1997

식혜에 함유된 이소말토올리고당과 밥알에 30unit/ml의 $\alpha$-아밀라아제, 글루코아밀라아제, $\alpha$-글루코시다아제, $\beta$-아밀라아제를 가하여 작용시킨 결과 글루코아밀라아제 외에는 일부밖에 가수분해하지 못하였다. 그리고, 인체의 효소인 $\alpha$-아밀라아제와 $\alpha$-글루코시다아제를 함께 작용시켜도 25% 이상 가수분해하지 못하므로 비피두스균의 활성인자로 작용할 것으로 보인다. 밥알은 물에 녹지 않기 때문에 식이섬유로도 작용할 것으로 보인다.

• Preventive Nutrition and Food Science
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• 제20권3호
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• pp.176-182
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• 2015

Abalone protein was hydrolyzed by enzymatic hydrolysis and the optimal enzyme/substrate (E/S) ratios were determined. Abalone protein hydrolysates (APH) produced by Protamex at E/S ratio of 1:100 showed angiotensin I converting enzyme inhibitory activity with $IC_{50}$ of 0.46 mg/mL, and APH obtained by Flavourzyme at E/S ratio of 1:100 possessed the oxygen radical absorbance capacity value of $457.6{\mu}M$ trolox equivalent/mg sample. Flavourzyme abalone protein hydrolysates (FAPH) also exhibited $H_2O_2$ scavenging activity with $IC_{50}$ of 0.48 mg/mL and $Fe^{2+}$+ chelating activity with $IC_{50}$ of 2.26 mg/mL as well as high reducing power. FAPH significantly (P<0.05) protected $H_2O_2$-induced hepatic cell damage in cultured hepatocytes, and the cell viability was restored to 90.27% in the presence of FAPH. FAPH exhibited 46.20% intracellular ROS scavenging activity and 57.89% lipid peroxidation inhibition activity in cultured hepatocytes. Overall, APH may be useful as an ingredient for functional foods.

• Preventive Nutrition and Food Science
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• 제10권2호
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• pp.134-139
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• 2005

Seven brown algal species (Ecklonia cava, Ishige okamurae, Sargassum fulvellum, Sargassum horneri, Sargassum coreanum, Sargassum thunbergii and Scytosiphon lomentaria) were hydrolyzed using five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) and screened for angiotensin 1-converting enzyme (ACE) inhibitory activities. Most algal species examined showed good ACE inhibitory activities after the enzymatic hydrolysis. However, E. cava was the most potent ACE inhibitor of the seven species. Flavourzyme digest of E. cava exhibited an $IC_{50}$ of around $0.3\;{\mu}g/mL$ for ACE; captopril has an $IC_{50}$ of $\~0.05\;{\mu}g/mL$. The Flavourzyme digest was separated to three fractions by an ultrafiltration membrane (5, 10, 30 kDa MWCO) system according to the molecular weights. The active components were mainly concentrated in >30 kD fraction which are composed of the highest protein content $(27\%)$ and phenolic content (261 mg/100 mL) compared to the other two smaller molecular weight fractions. Therefore, the active compounds appear to be relatively high molecular weight complex molecules associated with protein (glycoprotein) and polyphenols. Therefore, E. cave is a potential source of antihypertensive compound.

• 한국식품과학회지
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• 제41권6호
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• pp.622-627
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• 2009

홍게 가공부산물을 고부가가치 식품소재로 이용하기 위하여 단백질 분해효소를 이용하여 가수분해하고 반응표면분석법으로 가수분해 조건을 최적화 하였다. 홍게 가공부산물을 단백질 분해 효소인 Flavourzyme으로 가수분해한 결과 효소반응곡선은 반응 초기 빠른 반응속도를 나타내다가 이 후에 느려지는 전형적인 형태를 나타내었다. 반응초기 90분까지 가수분해도는 30%까지 증가하다가, 이후 최종적으로 32-36%를 나타내었다. 최적화를 하기 위한 가수분해 요인변수로는 반응온도, 반응시간 및 홍게 가공부산물에 대한 Flavourzyme의 양을 선정하였고, 5개의 수준에서 부호화하여 이들을 중심합성설계법을 이용하여 반응표면분석을 실시하였다. 홍게 가공부산물을 Flavourzyme을 이용하여 반응표면 분석법으로 가수분해 조건을 최적화한 결과, 온도 $51.8^{\circ}C$, 반응시간 4시간 45분, 홍게 가공부산물에 대한 Flavourzyme의 양 3.8%로 나타났다. 홍게 가공부산물 효소분해물은 향미소재 및 반응향 제조의 전구물질로서 이용할 수 있을 것이다.

• Preventive Nutrition and Food Science
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• 제14권4호
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• pp.323-328
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• 2009

Cryotin F could be used for hydrolyzing shrimp byproducts into bioactive ingredients, which could be used as value-added products. The objective of this study was to investigate the optimum condition for antioxidative activities of the enzymatic hydrolysate produced with Cryotin F using response surface methodology with central composite rotatable design. Shrimp byproducts (shells and heads) were hydrolyzed with Cryotin F. The experimental ranges of the independent variables for 20 experimental runs were 28.2-61.8${^{\circ}C}$ reaction temperature, pH 6-10 and 0.5-5.5% enzyme concentration. The degree of hydrolysis for the reaction products was measured. Their antioxidative activities were measured using 1,1-diphenyl-2-picryl-hydrazyl (DPPH) scavenging activity and Fe-chelating activity. The experimental method with central composite rotatable design was well designed to investigate the optimum condition for biofunctional ingredients with antioxidative activities using Cryotin F because of their high R2 values of 0.97 and 0.95 for DPPH-scavenging activity and Fe-chelating activity, respectively. Change in enzyme concentration did not significantly affect their antioxidative activities (p<0.05). Both DPPH scavenging activity and chelating activity against Fe for the enzyme hydrolysates were more affected by the pH of enzyme hydrolysis than by their action temperature. DPPH-scavenging activity was higher at acidic pH than alkali pH, while chelating activity against Few was inversely affected. Hydrolysate of shrimp byproducts showed high antioxidative activities depending on the treatment condition, so the optimum treatment of enzymatic hydrolysate with Cryotin F and other proteases can be applied to shrimp byproducts (shells) and other protein sources for biofunctional ingredients.

• Nutrition Research and Practice
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• 제8권3호
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• pp.278-283
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• 2014

BACKGROUND/OBJECTIVES: Due to its beneficial health effects, use of buckwheat has shown a continuous increase, and concerns regarding the allergic property of buckwheat have also increased. This study was conducted for evaluation of the hydrolytic effects of seven commercial proteases on buckwheat allergens and its allergenicity. MATERIALS/METHODS: Extracted buckwheat protein was hydrolyzed by seven proteolytic enzymes at individual optimum temperature and pH for four hours. Analysis was then performed using SDS-PAGE, immunoblotting, and competitive inhibition ELISA (ciELISA) with rabbit antiserum to buckwheat protein, and direct ELISA with pooled serum of 21 buckwheat-sensitive patients. RESULTS: Alkaline protease, classified as serine peptidase, was most effective in reducing allergenicity of buckwheat protein. It caused decomposition of the whole buckwheat protein, as shown on SDS-PAGE, and results of immunoblotting showed that the rabbit antiserum to buckwheat protein no longer recognized it as an antigen. Allergenicity showed a decrease of more than 50% when pooled serum of patients was used in ELISA. Two proteolytic enzymes from Aspergillus sp. could not hydrolyze buckwheat allergens effectively, and the allergenicity even appeared to increase. CONCLUSIONS: Serine-type peptidases appeared to show a relatively effective reduction of buckwheat allergenicity. However, the antigenicity measured using rabbit antiserum did not correspond to the allergenicity measured using sera from human patients. Production of less allergenic buckwheat protein may be possible using enzymatic hydrolysis.

• 한국수산과학회지
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• 제53권3호
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• pp.297-307
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• 2020

This study investigated the cosmetic effects of enzymatic hydrolytes of an aquatic by-product, fish skin. The skins of olive flounder Paralichthys olivaceus (PO) and Alaska pollock Gadus chalcogrammus (AP) were hydrolyzed using pepsin, Alcalase, and Protemax. Three enzymatic hydrolytes were obtained and the inhibitory effects of these hydrolytes on the aging-related enzymes tyrosinase, elastase, and collagenase were determined. The results indicated that the pepsin hydrolytes of PO and PA had stronger activities than the other hydrolytes. PO and PA also significantly reduced the intracellular reactive oxygen species levels in and improved the viability of H₂O₂-treated Vero cells; decreased nitric oxide production by and increased the cell viability of lipopolysaccharide-treated RAW 264.7 cells; and reduced intracellular reactive oxygen species levels and improved the viability of ultraviolet B irradiated HaCaT cells and human dermal fibroblasts. Furthermore, PO and PA remarkably reduced the intra- and extracellular melanin contents of alpha-melanocyte-stimulating hormone-stimulated B16F10 cells. These results demonstrate that PO and PA have potential for use in the cosmetic industry.

• Asian-Australasian Journal of Animal Sciences
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• 제17권5호
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• pp.712-718
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• 2004

This study was carried out to separate the calcium-binding protein derived from enzymatic hydrolysates of cheese whey protein. CWPs (cheese whey protein) heated for 10 min at $100^{\circ}C$ were hydrolyzed by trypsin, papain W-40, protease S, neutrase 1.5 and pepsin, and then properties of hydrolysates, separation of calcium-binding protein and analysis of calcium-binding ability were investigated. The DH (degree of hydrolysis) and NPN (non protein nitrogen) of heated-CWP hydrolysates by commercial enzymes were higher in trypsin than those of other commercial enzymes. In the result of SDS-PAGE (sodium dodecyl sulphate polyacrylamide gel electrophoresis), $\beta$-LG and $\alpha$-LA in trypsin hydrolysates were almost eliminated and the molecular weight of peptides derived from trypsin hydrolysates were smaller than 7 kDa. In the RP-HPLC (reverse phase HPLC) analysis, $\alpha$-LA was mostly eliminated, but $\beta$-LG was not affected by heat treatment and the RP-HPLC patterns of trypsin hydrolysates were similar to those of SDS-PAGE. In ion exchange chromatography, trypsin hydrolysates were shown to peak from 0.25 M NaCl and 0.5 M NaCl, and calcium-binding ability is associated with the large peak, which was eluted at a 0.25 M NaCl gradient concentration. Based on the results of this experiment, heated-CWP hydrolysates by trypsin were shown to have calcium-binding ability.

• 대한화장품학회지
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• 제35권2호
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• pp.135-141
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• 2009

본 연구는 열수추출법에 의하여 추출한 세리신을 이용하여 단독 또는 2종의 효소를 이용하여 가수분해하고 그 가수분해물의 항산화 및 미백효과를 살펴본 것이다. 여러 산업용효소 중 세리신에 대한 분해효과가 우수한 alcalase, flavourzyme 및 protamex를 이용하여 분해한 결과 세리신의 분자량은 20 ${\sim}$ 30 kDa의 범위로 감소하였으며 사용한 효소별로 특이적 가수분해물이 나타났다. 세리신 가수분해물의 항산화능을 살펴본 결과 원래 세리신에 비하여 DPPH 소거율이 높게 나타났으며 flavourzyme과 protamex를 같이 사용한 경우 약 85 %의 소거율을 나타냈다. 티로시나아제의 활성억제 효과를 살펴본 경우에는 세리신 가수분해물이 오히려 더 낮은 억제효과를 나타내었으나 세리신 가수분해물의 분획을 실시하고 활성억제 효과를 살펴본 결과 F2와 P3의 분획이 상대적으로 우수한 억제 효과를 나타내었다.

• 한국의류학회지
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• 제32권9호
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• pp.1461-1466
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• 2008

This study provides effects of mixed activators on enzymatic activation and determines optimum mixture ratio for enzymatic treatment. Wool 80% and polyester 20% blend fabric and papain from carica papaya are used in this experiment. L-cysteine and sodium sulfite are used as activators for papain treatment process. The treatment condition is pH 7.5, $70^{\circ}$, papain concentration 10%(o.w.f), 60 minutes. L-cysteine and sodium sulfite are added in enzyme solution with various concentrations($0{\sim}50mM$). The optimum treatment condition is determined by measuring weight loss, tensile strength, whiteness, water contact angle(WCA), dyeability and surface micrographs. The results are as follow; The optimum mixture ratio of activators is L-cysteine 2mM and sodium sulfite 10mM. Mixed activators assists in improving the activation of papain. WCA of papain treated fabrics is decreased since papain treatment with activator mixture makes wool polyester blend fabrics more hydrophilic. Dyeing property of papain-treated fabrics more improves by the treatment with mixed activators than with single activator. It means that this method can save time and lower cost. After papain treatment in the presence of mixed activator, the surface of fabrics is modified. The surface of wool fiber shows to be descaled and hydrolyzed, and that of polyester fiber shows to be cracked.