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Inactivation of Pectin Methylesterase by Immobilized Trypsins From Cunner Fish and Bovine Pancreas

Inactivation of Pectin Methylesterase by Immobilized Trypsins From Cunner Fish and Bovine Pancreas

Dan Li, Madyu Matos, Benjamin K Simpson

Biotechnol Appl Biochem. Mar-Apr 2013;60(2):244-52.

PMID: 23600576

Abstract:

Immobilized cunner fish trypsin was used to inactivate pectin methylesterase (PME). The effects of different reaction conditions (e.g., incubation time, PME concentration, and temperature) on PME inactivation and kinetics of inactivation were investigated. Temperature, incubation time, and PME concentration significantly affected the extent of PME inactivation. Generally, higher temperature, longer incubation time, and low PME concentration caused more PME inactivation. The immobilized fish trypsin had higher capacity to inactivate PME than immobilized bovine trypsin. The inactivation efficiency of the immobilized fish trypsin was about 20% higher than that of its bovine counterpart. However, PME inactivated by both trypsins regained partial activity during storage at 4°C, with immobilized fish trypsin-treated PME regaining more of its original activity than the immobilized bovine trypsin-treated PME. Heat-denatured PME was hydrolyzed more extensively by immobilized fish trypsin than by its bovine counterpart. The rate constants increased, whereas the D-values decreased with temperature for both immobilized fish and bovine trypsins. The inactivation rate constants of immobilized fish trypsin at all the temperatures investigated (i.e., 15-35°C) were higher than those of immobilized bovine trypsin. Furthermore, the activation energy (Ea ) of PME inactivation by immobilized fish trypsin was lower than that of immobilized bovine trypsin.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001927-B	Protease from bovine pancreas		9001-92-7	Price
AP9002077	Trypsin from bovine pancreas		9002-07-7	Price

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