• 한국식품과학회지
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• 제27권5호
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• pp.708-715
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• 1995

Pepsin, papain 및 trypsin 처리 참깨박 단백질의 기능성의 변화를 조사한 결과 용해도에 있어 pH 4에서 2%의 대조군에 비해 $53{\sim}94%$까지 뚜렷한 증가를 보였으며, trypsin에 의한 10%, 20% 가수분해도 처리군은 등전점에서 약 6배, papain에 의한 10% 가수분해도 처리군은 약 4.5배 가량의 유화능의 향상을 보였다. 기포 형성력은 각 효소 처리군의 30% 가수분해도 처리군의 알칼리 영역을 제외한 나머지 영역에서 전반적인 증가를 보였다. trypsin, papain 처리군의 겉보기 밀도와 수분 흡착력은 약 0.1 g/ml와 $0.3{\sim}0.7\;ml/g$ 정도 감소하였으나, 유지흡착력은 약 1 ml/g 정도의 증가를 보였다.

• 한국축산식품학회지
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• 제38권1호
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• pp.143-151
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• 2018

The effects of proteolytic enzymes (bromelain and bromelain+papain) and a ginger extract were assessed on collagen content and solubility, thermal shrinkage temperature of connective tissue, pH, cooking loss, drip loss, and Warner-Bratzler shear force (WBSF) of M. pectoralis profundus isolated from the beef brisket cut. Both proteolytic enzymes and ginger extract led to a significant increase in cooking loss and collagen solubility compared with untreated controls. On the other hand, the peak ($T_p$) thermal shrinkage temperature markedly decreased in all treatments compared with those in controls. Samples treated with bromelain, bromelain + papain, and ginger extract showed a significant decrease in WBSF by 36%, 40%, and 37%, respectively, compared with untreated controls. Our findings suggest that ginger extract are useful for post-mortem tenderization of meat containing high levels of collagen, compared to control even though, bromelain and bromelain + papain treatments have higher collagen solubility than ginger extract.

• Journal of Applied Biological Chemistry
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• 제43권4호
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• pp.246-249
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• 2000

We investigated the production of chitin oligosaccharides using food grade papain. A solution of commercial food grade papain (FGP) was dialyzed for 12 h before measuring its chitinolytic activity. The effects of enzyme concentration, reaction temperature, and pH on the endochitinase and $\beta$-N-acetylglucosaminidase activities and the thermostability of these enzymes were investigated. In adddition, the reaction products were analyzed with gel filtration on a Bio-Gel P2. The endochitinase activity was twentyfold higher than that of $\beta$-N-acetylglucosaminidase. The optimal endochitinase activity was at pH 3.0, while the maximal $\beta$-N-acetylglucosaminidase activity was at pH 6.0. The reaction product consisted mainly of the dimer of N -acetylglucosamine, with a small amount of its trimer. Under the experimental conditions, $120{\mu}g$ of chitin oligomers were obtained with 1 mg of FGP protein after an incubation of 2 h.

• 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.

• 한국식품과학회지
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• 제30권1호
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• pp.62-68
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• 1998

발효에 의한 향미특성과 저장성이 양호한 새로운 저염 오징어젓갈의 제조기술을 개발하고자 원료어육의 수분활성도와 염농도, papain과 glucose의 첨가농도 등 적정 제조조건에 대하여 조사하였다. 오징어육의 수분활성도를 0.94, 0.90과 0.88로 조절하고 3, 5와 7%의 식염을 첨가하여 제조한 오징어젓갈을 $10^{\circ}C$에서 6주간 숙성하였을 때 아미노태질소는 수분활성도가 높고 염도가 낮을수록 함량이 높았으며 수분활성도 0.90이고 식염농도가 5%인 경우 관능적 품질이 양호하였고 30일 이상 유통가능하였다. 수분활성도를 0.90으로 조절하고 5% 식염으로 염장한 오징어육을 papain의 첨가농도를 달리하여 $10^{\circ}C$에서 숙성하였을 때 papain의 첨가농도가 높을수록 단백질의 분해가 빨랐으며 관능적 품질은 papain 0.1%를 첨가한 처리구가 가장 양호하였다. 또한 수분활성도를 조절하여 5% 식염으로 염장한 오징어육은 1% glucose의 첨가로 유기산 발효를 촉진시켜 5주경에 pH 5.8로 저하하므로서 대조구의 최저 pH 6.13에 비하여 비교적 낮았으므로 저장성 연장효과가 기대되었다.

• Journal of Animal Science and Technology
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• 제62권6호
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• pp.933-947
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• 2020

This study was conducted to develop an effective heparin extraction method by using low-cost and highly effective enzymes from six pig by-products (liver, lung, heart, stomach, small intestine, and large intestine), and analyze their bioavailability. Low-cost and highly effective enzymes (alkaline-AK and papain) and a common enzyme (trypsin) were used for the heparin extraction. The angiotensin I- converting enzyme (ACE) inhibitory activity and the antimicrobial activity of extracted heparin were analyzed to verify their bioavailability. The average amount of heparin extracted per kilogram of pig by-products was 439 mg from the liver, 127 mg from the lung, 398 mg from the heart, 261 mg from the stomach, 197 mg from the small intestine, and 239 mg from the large intestine. Various enzymes were used to extract heparin, and the amount of extracted heparin was similar. Based on 1 g of pig by-product, the enzymes trypsin, papain, and alkaline-AK could extract 1,718 mg, 1,697 mg, and 1,905 mg of heparin, respectively. Heparin extracted from pig by-products showed antihypertensive activity and antimicrobial activity against Staphylococcus aureus at low populations. These results indicated that heparin can be obtained from pig by-products at a low cost.

• Journal of Microbiology and Biotechnology
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• 제21권6호
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• pp.617-626
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• 2011

Transglutaminase from Streptomyces mobaraensis is an enzyme of unknown function that cross-links proteins to high molecular weight aggregates. Previously, we characterized two intrinsic transglutaminase substrates with inactivating activities against subtilisin and dispase. This report now describes a novel substrate that inhibits papain, bromelain, and trypsin. Papain was the most sensitive protease; thus, the protein was designated Streptomyces papain inhibitor (SPI). To avoid transglutaminase-mediated glutamine deamidation during culture, SPI was produced by Streptomyces mobaraensis at various growth temperatures. The best results were achieved by culturing for 30-50 h at $42^{\circ}C$, which yielded high SPI concentrations and negligibly small amounts of mature transglutaminase. Transglutaminasespecific biotinylation displayed largely unmodified glutamine and lysine residues. In contrast, purified SPI from the $28^{\circ}C$ culture lost the potential to be cross-linked, but exhibited higher inhibitory activity as indicated by a significantly lower $K_i$ (60 nM vs. 140 nM). Despite similarities in molecular mass (12 kDa) and high thermostability, SPI exhibits clear differences in comparison with all members of the wellknown family of Streptomyces subtilisin inhibitors. The neutral protein (pI of 7.3) shares sequence homology with a putative protein from Streptomyces lavendulae, whose conformation is most likely stabilized by two disulfide bridges. However, cysteine residues are not localized in the typical regions of subtilisin inhibitors. SPI and the formerly characterized dispase-inactivating substrate are unique proteins of distinct Streptomycetes such as Streptomyces mobaraensis. Along with the subtilisin inhibitory protein, they could play a crucial role in the defense of vulnerable protein layers that are solidified by transglutaminase.

• Journal of Ginseng Research
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• 제14권1호
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• pp.21-26
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• 1990

The chemical composition and stabilities of the purified ginseng invertase were investigated. The purified enzyme was found to be a glycoprotein composed of 80.2% protein and 19.7% total sugar. The protein component of the enzyme was composed of acidic amino acid (9.3%), basic amino acid (48.9%), nonpolar amino acid (21.4%), polar amino acid (20.4%) and 6.1% S-containing amino acid. It showed especially high contents of histidine and serine. The enzyme was inactivated almost completely by the treatment with some proteases (papain, pepsin. trypsin, pancreatin and microbial alkaline pretense) and protein denatllrants (8M urea and 6M guanidine-HC1), bolt not with glyrosidase (${\alpha}$-amylase, ${\beta}$-amylase. glcoamylese and cellullase). btonosaccharides sllch as glilrose, fructose, galactose and mannose did not exert any influence on the enzyme activity. The activity of the enzyme was inhibited by Ag+, Mn2+, Hg2+, Zn2+ and Al3+, whereas Ca2+, Mg2+, Ba2+ and Fe3+ gave rather activating effects on the enzyme activity. The enzyme was relatively stable in the VH range of VH 6 and 8, and at the temperatures below 35$^{\circ}C$.

• Journal of Animal Science and Technology
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• 제44권6호
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• pp.801-808
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• 2002

상업적 단백질 분해 효소에 0.02% $CaCl_2$를 첨가하여 응유 활성화를 시킨 탈지유에 대한 분해 작용의 결과를 요약하면 다음과 같다. 다양한 효소별 가수분해 시간에 따른 가수분해도는 미생물 유래 효소와 trypsin은 pepsin과 papain W-40보다 높은 분해도를 나타냈다. 12% TCA 용액에 가용성인 NPN의 양은 trypsin이 가장 높은 분해도를 나타내었고 rennet과 pepsin이 가장 낮은 분해도를 보였다. 전기영동에 있어서 trypsin과 protease S는 $\alpha$- lactalbumin을 분해하였고 papain w-40은 $\beta$- lactoglobulin을 미약하게 분해하였으며 neutrase 1.5는 90분 이후부터 $\alpha$-lactalbumin과 $\beta$-lactoglobulin을 분해하였다. Rennet과 비교한 전기영동상에서는 rennet에 의해 분해 되지 않은 ${\alpha}_s$- casein과 $\beta$-casein을 trypsin과 protease S가 다량 분해하였고 $\kappa$-casein은 rennet에 비해 papain W-40이 상당 수준의 분해상을 나타내었다. 이상의 결과 가수분해도 및 NPN 양은 trypsin, neutrase 1.5 및 protease S가 다른 효소에 비해 높게 나타났으며, 전기영동상에서는 pepsin과 neutrase 1.5가 rennet과 유사한 경향을 나타내었다.

• 한국미생물생명공학회:학술대회논문집
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• 한국미생물생명공학회 1976년도 제8회 학술발표회
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• pp.190.1-190
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• 1976

맥주의 한sod 혼탁방지용으로 널리 사용되고 있는 papain을 미생물 효소로써 대치할 목적으로 토양에서 분리한 148주의 균주가운데서 Bacillus 속이라고 추정되는 한 균주를 선택하여 효소를 생산하였다. 이 효소는 제탁 능력에 있어서 시판의 protesal에 비등하며 저장시에는 pH7-8, 온도 $35^{\circ}C$ 이하에서 안정성이 확인되어 충분히 실용가치가 있는 것으로 본다.