• KSBB Journal
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• 제10권4호
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• pp.374-385
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• 1995

Gelatin 분해성 proteolytic enzyme 생성균인 B. subtilis 80021가 생산하는 세포외 단백칠 분해효소 생산을 위한 영양 요구성과 배양조건을 검토한 결과 는 다음과 같다. 영양요구성은 1.5%(w/v) glucose와 2.5% (w/v) yeast extract에서 효소활성도가 최고치를 나타내였고 metalion은 $Co^{2+}, Zn^{2+}$효소생성의 저해제로 작용한 반면 $Fe^{2+}와 Mn^{2+}$에서는 촉진제로 작용 하여 최고 3.5배 효소생산생이 증가하였다. 아미노산 첨가 영향에서는 대부분의 아미노산이 효소활생 을 촉진시키는 것으로 확인되였다. 배지의 최적초기 pH는 7.0 부근이며 배양온도는 $35^{\circ}C$에서 효소에 따 라 다소 차이는 였었으나 배양시간 30시간 정도에서 최고의 효소생산성을 나다내었고 30°C에서는 42시간째에 효소활성도가 최고치를 나타내였다. Tannic acid 첨가에 대한 만백질 분해효소 생산에서는 발효 애지에 tannic acid 첨가시 완전한 효소생산 저해제로 작용하였으며 salicin을 탄소원으로 한 salicinase assay에서는 온도 빛 배양시간에 관계없이 효소활성 을 보이지 않았고 복합탄소원 이용에 대한 amylase assay에서는 $35^{\circ}C$, 36시간째에 최대의 효소활성을 나타내였고 Invertase assay에서는 $35^{\circ}C$, 30시간째 에 최대 효소활성도 2.5unit/ml을 나타내였다. 또한 gelatin 가수분해능에서는 45% (w/v)의 gelatin 용 액의 점도가 발효조효소액에 의해 96% (mPas)의 정도저하를 가져오는 것으로 확인되었다.

• 한국식품영양과학회지
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• 제26권6호
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• pp.1116-1121
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• 1997

Effects of gamma irradiation onf the activity and the properties(amino acid compositions, in vitro digestibility and SDS-PAGE pattern) of proteolytic enzymes were investigated. The proteolytic activity of soluble human serine protease, enzyme in kiwi and pineapple decreased 10% and 30~65% by 5 kGy and 30 kGy, respectively. In dried pancreatin and lysozyme, the proteolytic and antimicrobial activities decreased 6~14% and 10~20% by 5kGy and 40kGy, respectively. The analysis of above 10kGy-irradiated soluble human serine protease by SDS-PAGE revealed radiolysis of the enzyme into protein or peptides of lower molecular weights. The irradiation of skim milk, hammastein casein, and lysozyme up to 40kGy had no deleterious effect on either the in vitro digestibility or amino acid compositions.

• 한국조리학회지
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• 제11권2호
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• pp.110-124
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• 2005

This study was conducted to investigate the proteolytic properties of Sarcodon aspratus on meat proteins. The analytical condition for the measurement of enzyme activity was determined and the effect of Sarcodon aspratus on beef protein and its fractions were determined by SDS-PAGE and the spectrophotometric method respectively. Optimum temperature and pH of Sarcodon aspratus were $73~78^{\circ}C$ and pH 8 respectively. However, enzyme tended to be denatured at $50^{\circ}C$ for 10 min incubation. Proteolytic activity of Sarcodon aspratus was higher than of kiwi and pear 66 and 990 times by dry weight respectively. It appeared that proteolytic activity of Sarcodon aspratus toward beef protein by SDS-PAGE was prominent when compared to that of kiwi and bromelain. Furthermore, Sarcodon aspratus showed the highest proteolytic activity toward all the beef protein fractions, which was followed by collagenase and bovine protease. Transmission electron microscopy showed the muscle fiber started to be degraded when treated with Sarcodon aspratus(1,000 unit) for 10min at $25^{\circ}C$. No distinct sarcomere, A-band, or z-line was observed when treated with Sarcodon aspratus for 60min at the same condition.

• 공업화학
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• 제10권5호
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• pp.635-638
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• 1999

구두용 나피(裸皮)의 물성에 가장 큰 영향을 주는 탈모 공정에 단백질 분해 효소가 미치는 영향을 연구하였다. 나피의 물성을 기존의 방법 대신 전자 현미경을 이용하여 측정하는 새로운 방법을 제시하였다. 단백질 분해 효소를 이용한 바이오-테크 처리가 화학적 처리보다 탈모율에서 약간 저하되나 나피의 물성과 환경 측면에서 우수한 것으로 나타났다. 특히, 화학적 처리시 발생하는 유해 가스인 $H_{2}S$가 전혀 발생치 않았으며, 탈모 공정의 폐수 처리시 COD 및 BOD 값이 각각 939 mg/L와 5268 mg/L로 상당량 감소하여 기존의 처리 방법들보다 환경 친화적인 방법임을 확인할 수 있었다. 따라서, 탈모 공정은 $29{\sim}30^{\circ}C$의 온도 범위에서 단백질 분해 효소인 0.4~0.5% Lupin LE-10을 첨가하여 20시간 처리하는 것이 적합하였다.

• 한국조리학회:학술대회논문집
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• 한국조리학회 2005년도 제33차 정기춘계학술세미나
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• pp.19-42
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• 2005

This study was conducted to investigate the proteolytic properties of Sarcodon aspratus on meat proteins. The analytical condition for the measurement of enzyme activity was determined and the effect of Sarcodon aspratus on beef protein and its fractions were determined by SDS-PAGE and spectrophotometric method, respectively. Optimum temperature and pH of Sarcodon aspratus was $73-78^{\circ}C$,pH 8, respectively. However, the enzyme tended to be denatured at $50^{\circ}C$ for 10min incubation. Proteolytic activity of Sarcodon aspratus was higher than those of kiwi and pear by 66 and 990 times by dry weight, respectively. It was appeared that proteolytic activity of Sarcodon aspratus toward beef protein by SDS-PAGE was prominent when compared to those of kiwi and bromelain. Furthermore, Sarcodon aspratus showed highest proteolytic activity toward all the beef protein fractions, which was followed by collagenase and bovine protease. Transmission electron microscopy showed the muscle fiber started to be degraded when treated with Sarcodon aspratus(1,000 unit) for 10min at $25^{\circ}C$. No distinct sarcomere, A-band, and z-line was observed when treated with Sarcodon aspratus for 60min at same condition.

• 한국미생물·생명공학회지
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• 제14권6호
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• pp.467-471
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• 1986

Fusarium moniliforme으로부터 순모세포벽 분해효소를 생산하고 분리, 정제하여 효소특성 및 protoplast 제조실험을 하였다. Ammonium nitrate를 0.2％ 첨가한 Baker's yeast 배지에서 7일간 진탕배양으로 효소를 생산한 후 Ammonium sulfate로 분획하고 Sephadex(G-100) column chromatography하여 세개의 peak를 얻었다 첫 번째 peak는 proteolytic, lytic activity 및 laminarin 분해력가를 보였으며, 두 번째 Peak는 lytic activity와 laminarin 분해력가를 동시에 가지고 있었으며, 세 번째 peak는 lytic activity만을 가지고 있었다. 분리된 세개의 peak를 혼합하였을때 개개의 peak보다 훨씬 높은 역가을 나타내어 상승효과를 보였고 또한 환원제에 의한 효소력가의 상승효과도 있었다. protoplast 수율은 99.2％정도였다

• Journal of Pharmaceutical Investigation
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• 제19권1호
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• pp.9-14
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• 1989

In order to study the protease from Agaricus bisporus (Lange), the crude protease preparation was separated by fractionation of mushroom extracts with ammonium sulfate. It was found that extracts from Agaricus bisporus (Lange) Sing. contained protease. The optimum pH of the enzyme was 6.0, and the pH range at which the enzyme was stable was 4.0 to 7.0. The optimum temperature at which the enzyme showed the highest proteolytic activity was $50^{\circ}C$, while the enzyme was instantly inactivated at about $60^{\circ}C$. The enzyme activity was inhibited by $Ag^+$, $Hg^{2+}$, $Cu^{2+}$, $Ba^{2+}$, $Fe^{3+}$, $Co^{2+}$, $Ca^{2+}$, $Pb^{2+}$, $Mg^{2+}$ and $Mn^{2+}$. The $K_m$ value was 0.32 mM with Hammarsten casein.

• 한국식품영양학회지
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• 제6권1호
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• pp.1-7
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• 1993

19 Samples of koji-starters using in brewing were collected from Korea and Japan, and then 31 strains of koji-molds were isolated from them. After Identification of the Isolate, rice koji was made with each strains, and its saccharogenic activity, dextrogenic activity, proteolytic activity, acid Producing ability, browning reaction and flavor were tested. Among 31 strains of isolates, 10 strains were Identified as Asp nwamori var. kawachii, 18 strains as Asp. oryzae, 3 strains as Asp. usamii mkt. shirousamii. The koji-starters made in Korea were composed of single species of koji-mold with same strain, but those made in Japan were composed of the mixture of different two species or the mixture of different 2 ∼4 strains in same species. Judging from amylolytic and proteolytic ability by species, Asp. awamori var. kawachii H1, I1 and 11, Asp. owsae J2, L2, M2, P3 and P4, and Asp. usamii writ. shirousamii S1 were better than the others. Mold strains isolated from Korean koji-starters were much lower in amylolytic or proteolytic activity than those from Japanese koji-starters. The typical characteristics for the 3 species of koji-molds were that Asp. awamori var. kawachii was strong in acid producing ability, but week in amylolytic and proteolytic ability, that Asp. owzae had strong amylolytic activity and good aroma, but produced little amount of acid, and that Asp. usamii mut. shirousamii had strong Proteolytic activity but some off-flavor.

• 한국수산과학회지
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• 제32권4호
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• pp.458-465
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• 1999

Distribution of the proteolytic activities of crude pretense extracted from the viscera of ten kinds of fish was examined. Their proteolytic activities on proteinous substrates (azocasein, hemoglobin, and casein) from the viscera of anchovy, bastard flatfish, mackerel and red sea bream were higher than those of other fishes, and the crude pretenses were further fractoinated with acetone or ammonium sulfate. Optimum concentrations for pretenses fractionation were $0\~55\%$ for acetone and $30\~70\%$ for ammonium sulfate. The fractionated viscera pretense of mackerel showed the highest proteolytic activity among four kinds of fishes. Activities of cathepsin D- and pepsin-like enzymes at pH 3.0, cathepsin L-, B-, H- and G-like enzyme at pH 6,0, and Hypsin- and chymotrypsin- like enzymes (pH 8.0) were detected in the fractionated viscera pretense, whereas activities of cathepsin L- and chymoeypsin-like enzyme were observed in commercial pretenses. Proteolytic activities of Alcalase, Protamex, and Aroase AP-10 for azocasein were slightly higher than the fractionated viscera pretenses, but their amidolytic activities at pH 6.0 and 8.0 toward synthetic substrates were lower than counterpart. The fractionated pretenses from fish viscera would be utilized as commercial pretenses.

• 한국수산과학회지
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• 제31권5호
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• pp.631-636
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• 1998

1. C. lipolytica FM5로부터 단백분해 효소를 생산하기 위한 배지로는 Bacto-tryptone $0.5\%$, proteose peptone $0.5\%$, yeast extract $0.25\%$, NaCl $0.5\%$, 그리고 $CaCl_2\;0.2\%$인 TPPY broth가 가장 효과적이었다. 2. 단백분해효소의 생성은 C. lipolytica FM5의 증식과 거의 일치하는 증식관련형으로서 균의 생육이 최대에 도달한 배양 48시간째에 효소의 생성량도 최대치를 나타내었다. 3. 효소반응의 최적온도는 $35^{\circ}C$였으며, pH 6.5$\~$9.0의 범위에서 효소활성은 거의 변화가 없었다. 4. $Ca^{2+},\;Cu^{2+},\;Fe^{2+}\;Mg^{2+}$등의 금속이온은 효소활성에 큰 영향을 미치지 않았으나 $Zn^{2+},\;Mn^{2+}\;K^+$ 등은 효소활성을 다소 저해하였다.