DOI QR코드

DOI QR Code

A Study on the Activation Conditions of Pancreatic Enzymes

판크레아틴 소화효소의 활성화 조건 연구

  • Kim, Dong-Chung (Department of Human Nutrition and Food Science, Chungwoon University)
  • Received : 2010.10.30
  • Accepted : 2011.01.13
  • Published : 2011.01.31

Abstract

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.

돼지 췌장에서 추출한 판크레아틴 효소들의 활성화 조건에 대해 조사하였다. 십이지장의 첨가는 췌장의 단백질분해효소와 지방분해효소의 활성화를 유도하였다. 췌장액에 10% 십이지장을 첨가하여 $30^{\circ}C$에서 90분간 반응시키거나 $25^{\circ}C$에서 4시간 반응시켰을때 췌장의 단백질분해효소와 지방분해효소의 활성화는 정점에 도달하였고, 전분분해효소의 활성에는 거의 영향을 주지 않았다. 2$5^{\circ}C$에서 4시간의 효소활성화, 원심분리, 아세톤침전 및 동결건조의 연속 공정으로 제조한 판크레아틴 효소들의 비활성도는 단백질분해효소 136 U/mg, 지방분해효소 170 U/mg 및 전분분해효소 400 U/mg으로 나타났다. 확립된 공정에 의해 제조된 판크레아틴은 USP 기준의 5.4배의 단백질분해효소, 58배의 지방분해효소 및 16배의 전분분해효소 활성을 보유한 고활성의 제품이었다.

Keywords

References

  1. 김동현, 윤혜경, 신지은, "판크레아틴 규격 표준화 연구", 약제학회지, 제33권 제4호, pp. 273-279, 1월, 2003. https://doi.org/10.4333/KPS.2003.33.4.273
  2. J. E. Clain, et al., "In vitro enzyme activity of commercially available pancreatic enzyme extracts", South African Medical Journal, 53(15), pp. 582-583, 1978.
  3. I. Jung, 이득식, 김동청, "돼지 췌장으로부터 판크레아틴 회수 공정 연구", 산학기술연구, 제4권, 제2호, pp. 98-102, 12월, 2009.
  4. T. Wieloch, "Trypsin activation of porcine procolipase", FEBS, 185(1), pp. 63-66, 1985. https://doi.org/10.1016/0014-5793(85)80741-9
  5. A. Larsson and C. Erlanson-Albertsson, "The effect of pancreatic procolipase and colipase on pancreatic lipase activation", Biochimica et Biophysica Acta-Lipids and Lipid Metabolism, 1083(3), pp. 283-288, 1991. https://doi.org/10.1016/0005-2760(91)90084-U
  6. M. H. Kang and J. Lee, "An improved procedure for the recovery of pancreatic enzymes with enhanced activity", Biotechnology Techniques, 10(6), pp. 419-424, 1996.
  7. H. Kimura, et al., "Activation of human pancreatic lipase activity by calcium and bile salts", The Journal of Biochemistry, 92(1), pp. 243-251, 1982. https://doi.org/10.1093/oxfordjournals.jbchem.a133920
  8. S. H. Lewis, "Preparing pancreatin", U. S. Patent 3956483, 1976.
  9. M. Abboudi, et al., "Method for producing pancreatin which contains low amounts of residual organic solvent and product thereof", U. S. Patent 5861291, 1999.
  10. USFDA, "Pancreatin", The United State Pharmacopeia, 1995.
  11. C. M. Stoscheck, "Quantitation of protein", Methods in Enzymology, 182, pp. 50-68, 1990. https://doi.org/10.1016/0076-6879(90)82008-P
  12. D. A. Grant and J. Hermon-Taylor, "Purification of porcine enterokinase by affinity chromatography", Biochemical Journal, 147(2), pp. 363-366, 1975. https://doi.org/10.1042/bj1470363
  13. D. H. De Souza, "The stability of pancreatic lipase", Biochemical Journal, 10(1), pp. 108-114, 1916. https://doi.org/10.1042/bj0100108
  14. B. Borgstrom, "The temperature-dependent interfacial inactivation of porcine pancreatic lipase effect of colipase and bile salts", Biochimica et Biophysica Acta-Lipids and Lipid Metabolism, 712(3), pp. 490-497, 1982. https://doi.org/10.1016/0005-2760(82)90276-4
  15. H. Hans, et al., "Continuous process of producing pancreatin and product thereof", U. S. Patent 4019958, 1977.