• Food Science and Biotechnology
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• 제18권2호
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• pp.488-493
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• 2009

A protein isolate was prepared from black soybean (Glycine max L. Merrill) that possessed higher antioxidant activity than ordinary white soy protein isolates. The isolate was partially hydrolyzed by alcalase to reduce the allergenicity of black soybean. Alcalase remarkably reduced the molecular mass of the major soybean allergens that have molecular weights of 53, 38, and 24 kDa. Hydrolytic breakdown occurred more effectively in Gly m Bd 30K than in Gly m Bd 60K or Gly m Bd 28K. Alcalase hydrolysis increased the solubility and hydrophobicity of the black soybean protein isolate. The foaming activity and stability of black soybean proteins were highly increased by the partial hydrolysis.

• 한국축산식품학회지
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• 제40권6호
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• pp.1033-1043
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• 2020

This study investigated the impacts of gelatin hydrolysate addition on the technological properties and lipid oxidation stability of cooked sausage. Gelatin hydrolysate was prepared from pork and duck skin gelatin, through stepwise hydrolysis using collagenase and pepsin. The cooked sausages were formulated without gelatin (control) or with 1% pork skin gelatin, 1% duck skin gelatin, 1% pork skin gelatin hydrolysate, and 1% duck skin gelatin hydrolysate. The pH, color characteristics, protein solubility, cooking loss, and textural properties of cooked sausages were evaluated, and the 2-thiobarbituric acid reactive substances (TBARS) value was measured weekly to determine lipid oxidation stability during 4 wk of refrigerated storage. Enzymatic hydrolysis of gelatin decreased protein content and CIE L* but increased redness and yellowness (p<0.05). When 1% gelatin or gelatin hydrolysate was incorporated in cooked sausage, however, little to no impacts on pH value, moisture content, protein content, color characteristics, protein solubility, and cooking loss were found (p>0.05). The addition of 1% duck skin gelatin hydrolysate increased the cohesiveness and chewiness of cooked sausages. The inclusion of 1% duck skin gelatin accelerated lipid oxidation of cooked sausages during refrigerated storage (p<0.05), whereas duck skin gelatin hydrolysate caused a lower TBARS value in cooked sausage compared to duck skin gelatin. The results show comparable effects of gelatin and gelatin hydrolysate addition on the technological properties of cooked sausages; however, the oxidative stability of raw materials for gelatin extraction should be evaluated clearly in further studies.

• 한국식품영양과학회지
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• 제21권6호
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• pp.706-711
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• 1992

Papain과 pepsin에 의한 부분 가수분해가 번데기 농축단백질의 기능적 특성에 미치는 영향을 검토하였다. TCA 가용성 질소량을 측정하여 얻은 가수분해 정도는 papain으로 10분과 60분간 처리한 결과 각각 10.23%와 19.17% 였으며 pepsin으로 10분과 60분간 처리한 경우는 각각 15.41%와 21.41%로 나타났다. 효소처리한 번데기 농축단백질의 질소 용해도는 실험한 pH 전범위에서 증가하였으며 특히 papain과 pepsin 모두 60분 처리한것이 10분간 처리한것 보다 높게 나타났다. 0.03M $CaCl_2$를 첨가한 결과 전반적으로 질소 용해도가 증가하는 경향을 나타내었다. 번데기 농축단백질의 겉보기 밀도는 papain으로 처리시 차이가 나타나지 않았으며 pepsin의 겨우는 다소 증가하는 경향이었다. 수분 흡수력의 경우 pepsin으로 10분간처리한것 이외에는 큰차이를 나타내지 않았으나 지방흡수력은 papain과 pepsin으로 부분 가수분해한 결과 전반적으로 증가하였다.

• 생명과학회지
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• 제15권5호
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• pp.779-782
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• 2005

Coupled transcription/translation cocktail을 이용하여 R. glutinis EH 유전자를 in vitro에서 합성하고 활성을 평가하였다. SDS-PAGE 및 immunoblotting을 통하여 45 kDa 크기의 EH 단백질이 발현되었음을 확인하였고, NBP assay 및 chiral GC 분석을 통해 발현된 단백질이 (R)-styrene oxide에 대한 입체선택성이 있음을 확인하였다. 따라서 무세포 단백질 합성 시스템을 이용하여 입체선택성을 유지시킨 EH 유전자 발현이 가능하며, 이러한 방법은 putative EH 유전자 탐색 등에 효율적으로 응용될 것이다.

• Nutrition Research and Practice
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• 제7권1호
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• pp.3-8
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• 2013

Buckwheat is known as a health food but is one of the major food allergens triggering potentially fatal anaphylaxis in Asia, especially in Japan and Korea. This study was conducted to investigate the characteristic of enzymatic resistance of buckwheat protein and allergenic potential. Enzymatic resistance of buckwheat protein was performed with in vitro digestibility test in simulated gastric fluid (SGF), pH 1.2, using pepsin and simulated intestinal fluid (SIF) using chymotrypsin. Reactivity of buckwheat proteins to human IgE was performed using six allergic patients sensitized to buckwheat. Buckwheat's IgE levels were measured using the Phadia UniCAP-system. Buckwheat protein, 16 kDa, still remained after 30 min treatment of pepsin on SDS-PAGE. Even though 16 kDa almost disappeared after 60 min treatment, two out of the six buckwheat patients' sera showed reactivity to hydrolysate after 60 min treatment, indicating that allergenicity still remained. In simulated intestinal fluid (SIF) using chymotrypsin, buckwheat protein, 24 kDa, showed resistance to hydrolysis with chymotrypsin on SDS-PAGE, and still had allergenicity based on the result of ELISA. Our results suggest that buckwheat proteins have strong resistance to enzyme degradation. This may be attributed in part to the allergenic potential of buckwheat. Further study should be continued regarding buckwheat allergy.

• 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.

• Membrane and Water Treatment
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• 제7권5호
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• pp.451-462
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• 2016

The molecular weight of proteins and protein hydrolysis products (PHP) in the fractionated post-production marinating brines left after herring marination process was determined by the HPLC. The proteins and PHP retention was evaluated in the three-stage purification process with the usage of polypropylene bag ($25{\mu}m$) and ceramic membranes with the cut-off of 150 and 1 kDa. It was found that the process of marination contributes to high participation of compounds in the post-production marinating brines. Those are characterised by low molecular weight, formed as a result of protein hydrolysis. Each stage of the scavenging process was reducing the content of proteins and PHP. The lowest retention was observed in the stage at which a PP bag was used, while the highest in the UF process, with the usage of 150 kDa membrane. The total retention of proteins and PHP differed according to the type of post-production marinating brines and reached the level of 16-22%.

• Food Science and Biotechnology
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• 제17권4호
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• pp.873-877
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• 2008

Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.

• Applied Biological Chemistry
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• 제40권5호
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• pp.404-408
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• 1997

단백질 분해효소를 이용하여 대두 단백질 가수분해물을 제조하여 물리화학적인 특성과 응용 가능성을 조사하였다. 단백질 함량이 60%이고, 가수분해도가 50%인 탈지대두박 분해물은 조미 소재의 기본 베이스로 사용하기에 적합하였고 이를 마일러드 반응시키고 조미하여 풍미를 향상시킨 가수분해물은 효소분해 간장 및 복합조미료의 원료로 사용 가능하였다. 대두분리단백의 가수분해물은 단백질 함량이 85%이며 평균 분자량이 250내외로서 환자식, 유아식, 스포츠 영양 등의 저엘러지 단백질원으로 적합하였다. 효소분해HVP의 염 함량은 2%이내로서 다른 원료와의 배합 사용량에 제한을 주지 않으면서 고 단백 제품의 개발을 용이하게 하였다. 대두박 분해의 부산물로 30%의 단백질 함량과 21%의 섬유소를 갖는 부산물이 생성되었으며 이는 식이섬유원, 보습제 또는 중량제로서의 응용 가능성이 있었다.

• 한국식품저장유통학회지
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• 제23권3호
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• pp.413-421
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• 2016

본 연구는 폐기되는 돈혈을 식품소재로 활용하고자 단백질 가수분해효소 5종을 처리하여 품질특성 변화를 조사하였다. 그 결과 KMFP-15(E)로 가수분해할 때 pH 7.3, 총 고형분 함량 $24.3^{\circ}Brix$ 및 유리아미노산 함량 4,944 mg%로 가장 높은 고형분 함량 및 유리아미노산 함량을 나타내었다. KMFP-15(E) 농도에 따른 영향을 조사한 결과 처리농도가 증가함에 따라 총 고형분 함량 및 유리아미노산이 증가하였으며, 유리아미노산은 KMFP-15(E) 0.2% (w/v)첨가구에서 7,224 mg%로 0.3% (w/v)첨가구와 유의적인 차이를 나타내지 않아 0.2% (w/v)로 설정하였다. KMFP-15(E)의 가수분해 시간에 따라 유리아미노산 함량은 4시간에서 7,404 mg%로 가장 높게 나타났으며, 시간이 경과할수록 감소하는 경향을 보여 최적 가수분해시간은 4시간으로 설정하였다. 상기 설정된 가수분해 조건을 통해 제조된 돈혈 분말(PBHP)에는 조단백질 및 아미노산과 철분, 칼륨, 아연 등 다량의 무기질이 함유되어 있는 것으로 나타났으며 특히, 철분의 함량은 1,983 mg%로 높게 나타나 식품소재로 활용 가능한 것으로 나타났다. 이상의 결과 폐기되는 돈혈의 활용방안으로 다양한 가수분해조건중 효소 KMFP-15(E) 0.2% (w/v)를 첨가하여, 4시간에서 가수분해 하였을 때 전반적 품질 특성이 가장 우수하여 향후 돈혈을 이용해 단백질 보충, 아미노산소재 및 철분강화제 등의 식품 및 의약품 소재로의 고부가가치 창출이 가능할 것으로 판단되었다.