• 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.

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

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.516-519
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• 2000

Generally pancreas consist of lipid, water and protein, digestion enzyme complex (pro-tease, lipase, amylase). The sample used in this work was frozen dry and treated by a semi-batch flow type. In order to develop a supercritical fluid extraction process to rem-ove lipid from the pancreas, experiments were conducted at various operating conditions(pressure range $1500{\sim}2800psi$, temperature range $25{\sim}40^{cdot}C$, particle size$(0.25{\sim}1.0mm$, flow rate $20{\sim}80m{\ell}/min)$. Also cholesterol in the pancreas was removed. The highest extraction efficiency was 2500psi, $35^{\cdot}C$, 0.25mm of pancreas size. The enzyme activity of the pancreas produced from this work showed high value compared with imported pancreas.

• Journal of Pharmaceutical Investigation
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• v.33 no.4
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• pp.273-279
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• 2003

Pancreatin is a enzyme mixture breaking down carbohydrates, proteins and lipids. Most pancreatin used in Korea is imported from foreign countries. However, guideline of each country for pancreatin produced from each country is different. Therefore, guideline for pancreatin imported from several countries, such as Europe, Japan and America, it is standardized to control its quality. Assay of enzyme activity for pancreatin in KP is similar to tat in JP, but it is significantly different from those in FP ad in USP. We measured pancreatin digestive activities of 17 commercial products. Activity assay of digestive enzymes, starch- and lipid-digestive enzymes, for pancreatin by KP method (including JP) was difficult compared to those by FIP ad USP methods. Particularly, activity assays of starch- and lipid-digestive enzymes by KP method were mistakable, ad varied in diluted samples than those by FIP. However, activity assay of protein-digestive enzyme by KP method was similar to that by FIP. Starch-digestive enzyme activities of 17 commercial pancreatins by KP method were lower 0.079-fold compared to those by FIP method. Their protein-digestive enzyme activities by KP method were higher 75.7-fold than those by FIP method. Their lipid-digestive enzyme activities by KP method were lower 0.234-fold compared to those by FIP method.

• KSBB Journal
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• v.18 no.4
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• pp.301-305
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• 2003

The study of pancreatin extraction was investigated by supercritical fluid process. Using supercritical carbon dioxide extraction with entrainer the purification of pancreatin was possible to remove lipids from Hog pancreas. To observe the optimum conditions different experimental variables were changed as pressure, temperature, flow rate of solvent and 0.25 mm of sample size were evaluated for effective removal of lipids. Ethanol and n-hexane were used as an entrainer with 5 mL/min. Increasing pressure at constant temperature the efficiency of the lipid removal in Hog pancreas was improved and the protein was concentrated without denaturalization, compared that of the control Hog pancreas. The most efficient conditions of lipid elimination were 17 MPa of pressure and 35$^{\circ}C$ of temperature and 0.25 mm of sample size.