• Fisheries and Aquatic Sciences
• /
• v.14 no.3
• /
• pp.174-178
• /
• 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.

• Food Science of Animal Resources
• /
• v.31 no.4
• /
• pp.491-496
• /
• 2011

The purpose of this study was to examine the effect of a crude protease from Bacillus polyfermenticus on tenderizing pork meat. A B. polyfermenticus protease was characterized, and pork loin samples were treated in solutions containing different enzymes (papain and proteases from Aspergillus oryzae and B. polyfermenticus) and stored for 24, 72, or 168 h at $4^{\circ}C$. Each treated sample was subjected to a quality assessment. B. polyfermenticus protease activity was lower than that for other enzymes tested, although it easily hydrolyzed the meat protein. The optimum temperature and pH for the activity of this protease were $50^{\circ}C$ and pH 7.0. The meat tenderizing activity of the protease from A. oryzae was higher than that of papain and the B. polyfermenticus protease. The fragmentation index of the enzyme-treated with the B. polyfermenticus protease was higher than that of the control. A sensory evaluation was not different between meat treated with proteases, but the overall tenderness of enzyme-treated meats was higher than that of the controls. Therefore, the B. polyfermenticus protease, papain, and the A. oryzae protease appear to be suitable for use as meat tenderizers.

• Korean Journal of Food Science and Technology
• /
• v.24 no.1
• /
• pp.101-106
• /
• 1992

Vie investigated the clarification effects of foxtail millet wine, a traditional wine in Cheju island, by centrifugation, protease treatment and ultrafiltration(UF). It was difficult to remove completely cloudy substances in foxtail millet wine only by centrifugation. With protease concentration of $5{\times}10^{-4}%(w/v)\;at\;35^{\circ}C$, for 2 hrs, foxtail millet wine was clarified effectively. Papain and bromelain appeared similar effects to the clarification of wine, but ficin was inferior to those. Ultrafiltration with pore size $100K\;and\;0.22{\mu}m$ membranes had appeared better clarification effects than the best result of enzyme treatment, and then was considered as a simple and economic method.

• Journal of Society of Preventive Korean Medicine
• /
• v.27 no.2
• /
• pp.23-33
• /
• 2023

Objectives : Sojadodamgangki-tang and its main components are traditional korean medicinal methods for treatment of cough, sputum and dyspnea. Using a respiratory inflammatory model, we intend to reveal the anti-inflammatory effect and its immune mechanism of Sojadodamgangki-tang. Methods : We used a papain-induced respiratory inflammatory mouse model. 8-week-old female BALB/C mice were divided into 3 groups as follows: the following groups: saline control group, papain treated group (vehicle), papain and Sojadodamgangki-tang(200 mg/kg) treated group (n=4). To evaluate the anti-inflammatory effect of Sojadodamgangki-tang extracts, inflammatory cell infiltration was measured in bronchoalveolar lavage fluid (BALF) and nasal lavage fluid (NALF). In addition, the effects of Sojadodamgangki-tang extracts on Th2 cell population in lung were determined by using flow cytometry. Results : Sojadodamgangki-tang extracts administration reduced inflammatory cell infiltration in BALF and NALF, especially of eosinophils. Furthermore, total immunogloblin (Ig)-E levels was reduced in BALF and serum by drug administration. Interestingly, Sojadodamgangki-tang extracts treatment also decreased the Th2 cell (CD4⁺GATA3⁺) population in lung. Conclusions : Our findings indicate Sojadodamgangki-tang extracts have anti-inflammatory effects by mediating Th2 cell and B cell activation.

• Journal of Korean Ophthalmic Optics Society
• /
• v.19 no.1
• /
• pp.51-57
• /
• 2014

Purpose: The present study was conducted to establish the experimental condition for the proper evaluation of protein removal efficacy when developing protein removal agents. Its protein removal efficacy was further analyzed and compared with the result from protein removal efficacy against protein deposition on contact lens to suggest the evaluation method for efficacy of protein removal agents. Methods: Protein digestibility assay presented in the Korean pharmacopoeia was selected to establish the evaluation method for efficacy of papain, pancreatin, subtilisin A and protease itself as a ingredient and protein removal tablets or solution containing those enzymes and find a suitable test conditions. Furthermore, the cleaning efficacy of commercially available protein removal tablets and solution on balafilcon A lens deposited with protein artificially was measured and the correlation between two evaluation methods was further analyzed. Results: When pancreatin itself and the product containing pancreatin was evaluated by protein digestibility assay, both reached 28 IU/mg, the standard value of protein digestibility suggested by the Korean pharmacopoeia. In case of protease and subtilisin A tested with trichloroacetic acid B solution, both of them met the enzyme activity level proposed by the manufacturers when they were evaluated by protein digestibility assay however, papain and subtilisin A tested with trichloroacetic acid A solution were not reached the enzyme activity level. Among protein removal agents, three products except a product containing pancreatin did not meet the enzyme activity value specified by the manufacturer when they were evaluated by protein digestibility assay. However, actual protein removal efficacy of three products except a papain-containing product on the lens was greater than 90% protein removal. In the case of papain-containing protein removal product, its effect was not measured by protein digestibility assay however, its actual protein removal efficacy on the lens reached 73.72%. Conclusions: From the results, it was confirmed that the efficacy of protein removal agents for contact lens should be evaluated by different method according to the type of proteolytic enzyme contained. That is, the protein removal agents containing pancreatin, protease and subtilisin A can be evaluated by protein digestibility assay and protein removal efficiency evaluation and the products containing papain can be effectively evaluated by only the evaluation method for protein removal efficiency employing the lens.

• Journal of the Korean Applied Science and Technology
• /
• v.36 no.3
• /
• pp.1018-1027
• /
• 2019

Natural-derived protein-derived low molecular weight peptides have been known to have physiological activities such as antioxidant, hypertension relief, immunomodulation, pain relief and antimicrobial activity. In this study, the low-molecular peptides were produced using commercial proteases (alcalase, bromelain, flavourzyme, neutrase, papain, protamex), and the antioxidant activity (DPPH scavenging activity, superoxide radical scavenging activity, hydroxy radical scavenging activity, and metals chelation capacity), constituent amino acid and molecular weight of the peptide were analyzed. Enzyme reaction was performed by adding 50 g of chopped Ogae meat slurry and 2%(w/v) protein enzyme into the enzyme reactor for 2 h at a pH of 6 and a temperature of $60^{\circ}C$. The degree of hydrolysis(%) after the reaction ranged from $36.65{\pm}4.10%$ to $70.75{\pm}5.29%$. The highest degree of hydrolysis of protamex was 46.3%, and the highest value of papain hydrolysate was $70.75{\pm}5.29%$. On the other hand, alcalase hydrolysate showed the lowest value of $36.65{\pm}4.10%$. Bromelain-treated low molecular weight peptides showed the highest DPPH radical scavenging activity and the lowest scavenging activity of alcalase-treated peptides. Superoxide radical scavenging activity showed that bromelain treated low molecular peptide showed the highest radical scavenging activity of 50% or more. Hydroxyl radical scavenging activity ranged from about 16.73 to 69.16%, the highest among bromelain-treated low molecular peptides. $Fe^{2+}$ chelation abilities showed a distribution between about 17.85 to 47.84%. The chelation capacity of the hydrolysates was not significantly different without any difference to the enzymes used. The results of amino acid analysis showed differences between hydrolysates of alcalase, bromelain, flavourzyme, neutrase, papain, and protamex enzymes. The most amino acid was glutamic acid. The molecular weight distribution of the enzyme hydrolyzates was in the range of 300-2,000 Da, although the molecular weight distribution differed according to the treated enzymes.

• Proceedings of the Korean Society for Applied Microbiology Conference
• /
• 1975.07a
• /
• pp.111.4-111
• /
• 1975

1l들이 mass cylinder에 200ml의 맥주를 넣고 질소가스로써 발포시킨 다음 거품이 사라지는 현상을 시간적으로 측정하는 방법을 이용하며 생산공정의 각 단계에서 채취한 맥주를 검사해 본 결과 chillproofing 공정 이후의 맥주에 foaming이 현저히 손상되고 있다는 것을 알았다.

• Proceedings of the Korean Society for Applied Microbiology Conference
• /
• 1976.10a
• /
• pp.190.1-190
• /
• 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.

• Proceedings of the Korean Society for Applied Microbiology Conference
• /
• 1977.10a
• /
• pp.195.4-196
• /
• 1977

Trypsin에 대해서 비해물질을 생성하는 Streptomyces속 균주 AS 707을 선별하고 이 균주가 생성하는 물질의 작용성 및 제성질을 조사한 결과 본 저해물질은 열에 대해서 비교적 강하고 pH 처리에 대해서는 산성에서 중성에 걸쳐서는 안정하나 alkali성에서는 불안정했고 $\alpha-chymotrypsin과$ papain에 대해서도 저해작용을 하였으며 trypsin에 대한 저해양상은 mixed type이었다.(중략)

• Proceedings of the Korean Society of Applied Pharmacology
• /
• 1993.04a
• /
• pp.57-57
• /
• 1993

단백질 분해효소는 염증주변에 축적된 파괴조직이나 변성단백질등을 분해하여 염증, 특히 만성염증의 순환을 정상화함으로써 소염제로서 사용되어 왔으며 현재, Chymotrypsin, Trypsin, Promelain, Papain, Serrathiopeptidase, Pronase 등이 소염효소제로써 사용되고 있다. 이들은 주로 미생물 배양액에서 통상적인 방법으로 정제하여 사용하며, 유전자 재조합기술을 사용하여 재조합 균주에서 생산할 경우 그 생산성을 증대시킬수 있을 것이라 기대된다.