• Fisheries and Aquatic Sciences
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• 제2권1호
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• pp.36-43
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• 1999

A study on the hydrolysis of anchovy using proteolytic bacteria isolated from anchovy jeotkal (a salt-fermented fish) was carried out to develop a rapid process of liquefied anchovy jeotkal. Five kinds of proteolytic bacteria, such as Staphylococcus sp.-l, Photobacterium sp., Volcaniella sp., Staphylococcus sp.-2 and Bacillus sp., were isolated from the anchovy jeotka1 that fermented with $20\%$ NaCl at room temperature for 2 months. Those grew well at $40^{\circ}C$, pH 7.0 on TPY broth with $2.0\%$ NaCl. The optimal hydrolysis temperature, pH, time and proteolytic bacteria densities for hydrolysis of minced anchovy were$40^{\circ}C$, 7.0, 6 hours and $1.8\times10^8$ cells/g raw anchovy, respectively.

• 한국식품과학회지
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• 제24권3호
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• pp.294-299
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• 1992

본 연구에서는 분리대두단백질에 단백질 가수분해효소를 처리하여 대두단백질에 가수분해적 변성을 야기하여 그 기능성을 변화 고찰하고 실제 식품에의 이용방법으로 효소처리된 두유로 두부를 만들어 물성실험과 관능평가를 실시하였다. 장엽에서 SPI를 제조한 후 15분간 bromelain으로 처리하여 2.7% 가수분해된 MSPI를 만들어 기능특성을 측정 비교하였다. MSPI는 전 pH범위에서 용해도가 증가하였고, 특히 등전점에서 15% 정도 증가하였다. 유화형성력과 기포팽창력은 증가하였으나 이들의 안정성은 감소하였는데, 특히 기포안정성은 알칼리쪽에서 급격히 감소하였고, 등전점에서는 가장 큰 것으로 나타났다. 표준두유와 변형두유를 혼합하여 제조한 두부로 물성실험과 관능평가를 실시하였을 때 압착실험에서는 변형두부I이 연하고 탄력성 있는 두부를 형성하는 것으로 나타났다. 각 두부의 물성모형은 spring 한개와 Maxwell 모형 세개를 가진 7요소모형으로 동일한 물성모형을 나타내었다. 관능평가에서는 표준두유와 변형두유를 3 : 1의 비율로 혼합하여 제조한 두부의 품질이 가장 우수한 것으로 평가되었다.

• 한국식품과학회지
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• 제22권3호
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• pp.234-240
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• 1990

본 실험에서는 상품화된 단백질 분해효소를 이용한 굴 및 홍합에 대한 최적 가수분해 조건에 대하여 조사하였다. 가수분해도, 유리아미노태 질소, 핵산관련물질, 유리아미노산 및 관능검사로 가수분해물들의 특성을 조사한 결과 굴의 경우 MKC-HT proteolytic, alcalase 0.6L 및 thermoase가, 홍합의 경우 acid-fungal protease와 thermoase가 각 가수분해물 제조시 가장 효과적인 단백질 분해효소임을 확인하였다.

• 유기물자원화
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• 제6권1호
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• pp.1-12
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• 1998

피혁제조시 발생되는 크롬을 함유한 피혁 고형폐기물인 shaving scrap의 단백질 자원화 가능성을 검토하기 위하여 MgO를 기본으로 하여 alkaline inducing agents 및 alkaline proteolytic enzymes을 혼용처리하여 shaving scrap으로 부터 회수한 가수분해 단백질의 용해도, 무기성분 함량, 분자량분포 등을 비교 검토함으로서 최적 가수분해 조건 및 액체비료의 원료로 활용하기 위한 저분자 단백질의 회수방안을 조사한 결과는 다음과 같다. Alkaline inducing agents의 혼용처리에 의한 shaving scrap의 가수분해 실험결과 7% MgO를 기본으로 하여 alkaline inducing agents 종류에 따라 65~85% 범위로 용해도 차이가 뚜렷하였으며, 가수분해되는 정도는 NaOH>$Ca(OH)_2$>KOH순으로 나타났으며, 획득된 hydrolyzed protein의 평균분자량은 NaOH처리시 약 10 KD, $Ca(OH)_2$ 처리시 약 40 KD, KOH처리시 약 80 KD이었으며, 크롬함유량은 약 15 ppm이었다. Alkaline proteolytic enzymes의 혼용처리에 의한 shaving scrap의 가수분해 실험결과 alkaline proteolytic enzymes 종류에 따라 Alcalase>Esperase>Savinase순으로 용해도 차이를 보였으며, 0.5% Alcalase의 처리에 의해 용해도 85%수준, 평균분자량 1 KD 미만, 크롬 함유량 10ppm 이하인 저분자 형태의 hydrolyzed protein을 획득할 수 있었다.

• Journal of Pharmaceutical Investigation
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• 제19권4호
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• pp.203-212
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• 1989

A proteolytic enzyme was extracted from Sarcodon aspratus (Berk) S. Ito by percolation method. Proteolytic activity of the extracted proteolytic enzyme (SAP) was compared with several digestives containing proteolytic enzymes. Potency of SAP was higher than that of the other digestives except for protease. The optimum pH ranse of SAP was similar to that of pancveatin and protease. SAP was more stable than pancreatin and protease under various temperature, alkaline pH, and metal ions. Bovine serum albumin hydrolysing activity of SAP was equivalent to that of pancreatin and protease in small intestine of rats. SAP demonstrated lower adsorption to antacids than pancreatin and protease. Among the mixtures of SAP and several antacids, magnesium oxide-SAP showed the highest proteolytic activity.

• 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.

• 농업과학연구
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• 제39권4호
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• pp.561-568
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• 2012

The aim of this study was to introduce a simple method for isolation of ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin from cow's milk, and peptides produced by enzymatic hydrolysis of ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin with alcalase. Whey protein were precipitated from whey by ammonium sulfate and, ${\alpha}$-lactalbumin and ${\beta}$-lactoglobulin were isolated using Hi Prep 26/60 Sephacryl S-100 column gel filtration chromatography. Bovine serum albumin and ${\beta}$-lactoglobulin were isolated by Mono-Q 5/50 GL column anion exchange chromatography of the 50% Ammonium Sulfate-supernatant. Isolated whey proteins were hydrolyzed by proteolytic alcalase. Tricine SDS-PAGE and reverse-phase HPLC analyses revealed that almost hydrolyzed all the ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin and bovine serum albumin with alcalase. Molecular weight of various peptides derived from alcalase hydrolysate were small molecular weight than 3.5 kDa.

• 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.

• Fisheries and Aquatic Sciences
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• 제14권3호
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• pp.174-178
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• 2011

This study aimed to determine the degree of hydrolysis and angiotensin-I-converting enzyme (ACE)-inhibitory activity of Giant Jellyfish Nemopilema nomurai (jellyfish) hydrolysates. The degree of hydrolysis using six proteolytic enzymes (Alcalase, Flavozyme, Neutrase, papain, Protamex, and trypsin) ranged from 13.1-36.8% and the inhibitory activities from 20.46-79.58%. Using papain hydrolysate, we newly isolated and characterized ACE-inhibitory peptides with a molecular weight of 3,000-5,000 Da that originated from jellyfish collagen. The purified peptide (FII-b) was predicted to be produced from an alpha-2 fragment of the type IV collagen of jellyfish. The N-terminal sequence of FII-b was Asp-Pro-Gly-Leu-Glu-Gly-Ala-His-Gly- and showed 87% identity to the collagen type IV alpha-2 fragment of Rattus norvegicus and a predicted protein from Nematostella vectensis, indicating that the ACE-inhibitory peptide originated from the collagen hydrolysate and had an $IC_{50}$ value of 3.8 ${\mu}g$/mL. The primary structure of the fragment is now being studied; this peptide represents an interesting new type of ACE inhibitor and will provide knowledge of the potential applications of jellyfish components as therapies for hypertension.

• 한국수산과학회지
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• 제28권5호
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• pp.557-568
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• 1995

어류의 사후 초기의 변화를 육 및 장기조직중에 분포하는 단백질분해효소의 작용과 관련하여 검토할 목적으로 멸치의 육 및 장기에서 분리한 cathepsin L과 chymotrypsin 및 trypsin의 단백질 기질에 대한 특성과 근원섬유단백질에 대한 분해능을 전기영동적으로 분석하여 다음의 결론을 얻었다. 이들 세 효소의 casein에 대한 친화도는 유사하였고, 근원섬유단백질에 대한 친화도는 casein에 대한 친화도보다 높았다. 멸치와 방어의 근원섬유단백질에 대한 cathepsin L과 chymotrypsin의 활성은 trypsin보다 훨씬 높게 나타났다. $0-25\%$까지의 식염농도에서 세 효소의 단백질분해활성은 식염의 농도에 반비례하였으며, 식염의 공존상태에서 세 효소는 casein 보다 근원섬유단백질에 대하여 높은 활성을 나타내었다. 관원섬유단백질의 효소 분해시에 cathepsin L은 chymotrypsin과 trypsin에 비하여 염농도와 온도에 의한 영향이 적었다. 따라서, 멸치의 사후변화와 젓갈 숙성 중의 자가소화는 trypsin보다는 cathepsin L과 chymotrypsin의 단백질분해활성이 더욱 깊이 관여할 것으로 판단된다.