• Food Science of Animal Resources
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• v.23 no.3
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• pp.193-199
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• 2003

In order to investigate the meat tenderizing effects of pear, pineapple and kiwifruit, crude protease was prepared from each fruit and treated with actomyosin in a single manner or mixed type in several combination. Actomyosin was incubated with various proteases for 24 hrs under three different pH condition, and its degrading performance was evaluated by the SDS-PAGE. Pear extract showed an active degrading activity for actomyosin at pH 5.3 and 7.0. But, little actomyosin degradation was observed at pH 8.0. Actomyosin was strongly degraded by the treatment of protease from pineapple at all different pHs(5.3, 7.0 and 8.0). Kiwifruit protease extract has shown actomyosin degradation activity 1hr after treatment at pH 5.3 and pH 7.0. Meanwhile, the mixture of pear and pineapple extracts(l:l, w/w) showed much more degradation than the results of singular manner treatment at pH 5.3 and 7.0. When the pear protease was mixed with kiwifruit protease(l:l, w/w), the performance of actomyosin degradation was similar to the results of each single protease treatment. When the mixture was made of pineapple and kiwifruit extracts, actomyosin degradation was almost the same as the result of treatment of pineapple protease only. When those three proteases were mixed together(l:l:l, w/w/w), actomyosin degrading activities was in time dependent manner at pH 5.3. In summary, pear protease can be used potentially as a meat tenderizer when it was mixed with pineapple or kiwifruit rendering proper tenderization of the meat.

• Proceedings of the Plant Resources Society of Korea Conference
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• 2003.04a
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• pp.142-142
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• 2003

본 연구에서는 kiwifruit 과육 속에 들어 있는 단백질분해효소의 gelatin분해활성을 조사하고 그 산업적 방안을 검토하였다. Kiwifruit 과육에서 3개의 단백질분해효소의 활성 밴드(PI, PII, PIII)가 관찰되었다. 단백질분해효소 PI은 220 kD, PII는 51 kD, PIII는 26 kD에 해당하는 것으로 추정할 수 있었다. 이들 단백질분해효소 PI, PII, PIII는 모두 pH 2.0~5.0 범위에서 높은 활성을 보였으며 pH 4.0에서 가장 높게 나타났다. 이들 단백질분해효소 PI, PII, PIII는 모두 cysteine proteinase 저해제인 E-64와 iodoacetate에 의해서 저해되었으며, cysteine proteinase를 촉진하는 DTT, cysteine 및 $\beta$-mercaptoethanol에 의해서 활성이 증가하였다. 그 중 단백질분해효소 PIII는 분자량과 효소의 특성으로 보아 actinidin (EC 3.4.22.14)과 동일한 것으로 판단되었다. 단백질분해효소 PI, PII, PIII는 모두 $Ca^{2+}$, $Mg^{2+}$과 $Mn^{2+}$에 의해 촉진되었으며, $Zn^{2+}$과 Hg$^{2+}$에 의해 완전히 저해되는 것으로 나타났다. 하지만, Co$^{2+}$, Cu$^{2+}$, $Al^{3+}$ , Fe$^{3+}$ 등 금속이온의 영향은 다소 다르게 나타났다. Kiwifruit 과육의 단백질분해효소 PI, PII, PIII 중에서 PI과 PII는 온도가 증가함에 따라 활성이 점차 낮아졌으나 PIII는 비교적 안정한 것으로 조사되었다. 특히, PIII는 5$0^{\circ}C$ 이내의 범위에서 48시간 경과시에도 75% 이상의 활성을 보여 이 범위의 온도에서는 상당 시간 동안 안정한 것으로 나타났다. 단백질분해효소의 산업적 가치를 고려해 볼 때 우선적으로 넓은 기질특이성과 열안정성이 높아야 한다. Kiwifruit에서 추출한 단백질분해효소는 4$0^{\circ}C$ 전후에서 최대의 활성을 보이고, 고온에서도 상당 시간 비교적 안정한 특성을 보여 식품제조, 식육연화 등 식품산업 분야에서의 활용가능성이 높을 것으로 보이며, 나아가 단백질이 갖는 식품학적 기능성을 높이는 데에도 사용할 수 있을 것으로 판단된다.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.12 no.1
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• pp.276-280
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• 2011

This study investigated the activation conditions of pancreatic enzymes from porcine pancreas. Duodenum induced the activation of pancreatic protease and lipase in pancreas. When 10% duodenum was added to pancreatic juice and the mixture was incubated at $30^{\circ}C$ for 90 min or at $25^{\circ}C$ for 4 hrs, the activities of pancreatic protese and lipase reached the peak. When the pancreatin was prepared by sequential process of enzymatic activation at $25^{\circ}C$ for 4 hrs, centrifugation, acetone precipitation and freeze-drying, the specific activities of pancreatic protease, lipase and amylase were 136, 116 and 400 U/mg-protein, respectively. The protease, lipase and amylase activities of the prepared pancreatin were 5.4, 58.0 and 16.0 times higher than those of USP standard, respectively.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.29 no.3
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• pp.309-319
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• 1996

Properties as related to the utilization of the crude proteases extracted from the muscle and viscera of fish (2 dark fleshed lish; anchovy, Engraulis japonica, and gizzard-shad, Clupanoda punctatus; 2 white fleshed fish; seabass, Lateolabrax japonicus, and sole, Pleuronichthys cornutus) were studied. Proteolytic activity of the muscle protease was slightly inhibited with the increase of sodium chloride concentration and it was apparent against the yellowtail myofibrillar protein than casein substrate. Proteolytic activities of the seabass and sole visceral crude protease were inhibited to 50 to $60\%\;by\;25\%$ of sodium chloride, but those of anchovy and gizzard-shad viscera crude enzymes were not influenced by sodium chloride. The vacuum freeze-dried crude protease and glycerol-mixed crude pretense of gizzard-shad and seabass muscles were almost lost their activities on the 16th week of storage, while those from the viscera of the fish were relatively stable. Degradation of the yellowtail myofibrillar protein by the anchovy muscle and viscera crude pretenses rapidly proceeded in the beginning of the reaction and the degraded products were mainly distributed in the range of 6 to 15 kDa electrophoretically.

• Parasites, Hosts and Diseases
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• v.35 no.1
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• pp.39-46
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• 1997

The present study was undertaken to determine whether live T. uaginnlis degrades human secretory IgA, serum If and IgG molecules. Human immunoglobulins were exposed to live trophozoites, parasite Iysate, and excretory-secretory product (ESP) of T ucginnlis. To determine the fragmentation of immunoglobulins, the reaction sample was subjected to SDS-PAGE and EITB, and peroxidase conjugated antihuman IgA and IgG were used as probes. Live trophozoites degraded secretory IgA, serum IgA and IgG, and degradation were pressed forward by the prolongation of the incubation time and by increasing the number of trichomonads respectively. Also the Iysates and ESP of trichomonads degraded IgA and IgG. The cysteine and serine proteinase inhibitors such as I-64, antipain, iodoacetic acid, iodoacetamide, TLCK reduced the ability of cleaving immunoglobulins. The proteinase activity and cytotoxicity of T. uaginnlis to HeLa cells were decreased when live T. vusinalis was treated with metallo-proteinase inhibitor as well as cysteine and serine proteinase inhibitors. These results suggest that proteinase secreted from live T ucginclis may play a part role in host pathogenesis by T. uosinnlis, and the cleaving ability of host immunoglobulins by the proteinase may contribute as a one of immune evasion mechanism for parasite survival in the host.

• Journal of Applied Biological Chemistry
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• v.63 no.4
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• pp.291-295
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• 2020

In order to increase the utilization of defatted sesame meal (DSM), a by-product of sesame oil production, the conditions of extraction of insoluble proteins from DSM by enzyme treatment were investigated. As a result of comparing the treatment results of proteolytic enzymes Alcalase, Flavorzyme, Neutrase, and Protamex with control, Protamex was effective in increasing the total solid and protein content. At the reaction conditions of Protamex (50 ℃, pH 6.0), the dosage of enzymes was appropriate for 1% of DSM and 3 h of enzyme reaction time. To improve the efficiency of enzymatic treatment, the protein content extracted increased as the heat treatment temperature increased, and slightly increased above 110 ℃. As a result of investigating the effect of the combination treatment of cell lytic enzyme (Tunicase) and protease (Protamex) on protein solubilization, it was most effective to treat the cell lytic enzyme after processing the protease. After heat treatment (110 ℃, 10 min), sequential treatment of Protamex and Tunicase increased the protein content by about 3.5 times (9.85→35.58 mg/mL) of the non-heated control and 2.2 times (15.83→35.58 mg/mL) of the heat treated control.

• Food Science and Preservation
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• v.24 no.5
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• pp.697-706
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• 2017

The purpose of this study was to investigate the physiochemical properties of Doenjang was fermented by added with fungi and protease. The moisture content and pH of Doenjang added with protease (WP) were lower than those of control w/o protease while the contents of titratable acidity, reducing sugar, and amino-type nitrogen in WP were higher than control. The ${\alpha}$-amylase activities of Doenjang added with single and mixed Protease B were the highest at 4 weeks of fermentation period and protease activity of WP was about 4 times higher than that of control. The 4-9 kinds of free amino acids (proline, isoleucine, leucine, and phenylalanine etc.) in WP was increased in comparison with control. The DPPH radical scavenging activity and total polyphenol content were higher in WP than control. Total aerobic bacterial and fungal numbers were decreased depending on fermentation time regardless of addition of protease. In conclusion, the protease can be used as additives improving the quality and taste of fermented Doenjang.

• Journal of Korean Society of Environmental Engineers
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• v.36 no.4
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• pp.265-270
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• 2014

Protease producing microorganisms were isolated from many kinds of food waste and fermented foods, which contains high amount and variable kinds of degraded substances. Several microorganisms were identified by 16S rRNA full sequencing analysis methods. The activity of protease was analyzed and identified in variable conditions for the application. For industrial use for biowaste treatment some proteases were isolated, identified and selected from microbial cells. And the tests were carried for the further use. The protein degrading activity at low temperature is useful for the treatment of organic waste, which contains much proteins. By the protein degradation process the organic waste can be utilized in variable fields, for example from feedstuff supplement to fertilizer for agriculture. Bacterial cells with protease activity at low temperature were isolated and identified. The optimal conditions for microbial cultivation and protease production were studied.

• The Korean Journal of Zoology
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• v.30 no.4
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• pp.401-409
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• 1987

단백질 분해효소와 ovoinhibitor가 계배근세포 융합에 미치는 영향을 알아보기 위하여 세포 운합지수의 측정, Western blot 분석법에 의한 ovoinhibitor의 세포 내농도 측정 및 단백질 분해효소의 활성도를 조사하였다. 세포 배양 30시간과 72시간에 처리된 ovoinhibitor는 상당히 근세포 융합 억제시켰다. 근세포 내 ovoinhibitor의 농도는 배 양 48시간에서 가장 높았고, 배양이 진행됨에 따라 계속 떨어져서 대체로 융합지수가 올라갈수록 그 농도가 낮아지는 경향을 보였다. 근세포 분화가 진행됨에 따라 총 단백질 분해효소의 환성도는 계속 증가하였는데 특히 배양 48시간에서 72시간 사이의 급격한 증가를 나타내는 시기는 세포 융합이 가장 활발히 일어나는 시기와 일치했다. 이상의 결과는 단백질 분해효소 저해제가 근세포 분화에 상당한 영향을 끼침을 보여 주며, 단백질 분해효소와 단백질 분해효소 저해제는 하나의 조절단위로써 근세포 분화에 어떤 작용을 할 것으로 사료된다.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 1998.06a
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• pp.175.2-176
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• 1998