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Title: Stabilization of Bovine Intestine Alkaline Phosphatase by Sugars
Authors: SEKIGUCHI, Satoshi
HASHIDA, Yasuhiko
YASUKAWA, Kiyoshi  kyouindb  KAKEN_id
INOUYE, Kuniyo
Author's alias: 井上, 國世
Keywords: bovine intestine alkaline phosphatase
enzyme
stability
sugar
trehalose
Issue Date: Jan-2012
Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
Journal title: Bioscience, Biotechnology, and Biochemistry
Volume: 76
Issue: 1
Start page: 95
End page: 100
Abstract: Bovine intestine alkaline phosphatase (BIALP) is widely used as a signaling enzyme in sensitive assays such as enzyme immunoassay. In this study, we evaluated the effects of sugars on the kinetic stability of BIALP in the hydrolysis of p-nitrophenylphosphate (pNPP). The temperatures reducing initial activity by 50% in a 30-min incubation, T50, of BIALP with 1.0 M disaccharide (sucrose and trehalose) or 2.0 M monosaccharide (glucose and fructose) were 55.0–55.5 °C, 4.7–5.2 °C higher than without sugar (50.3±0.1 °C). The T50 of BIALP increased to 58.4±0.3 °C when the trehalose concentration was from 1.0 to 1.5 M, but did not change when the glucose concentration was from 2.0 to 3.0 M. Thermodynamic analysis revealed that the stabilization of BIALP by sugars was driven by the increase in the enthalpy change of activation for thermal inactivation of BIALP. No sugars affected the kcat of BIALP in the hydrolysis of pNPP. These results suggest that not only trehalose, which is considered the most effective stabilizer of enzymes, but also sucrose, glucose, and fructose can be used as stabilizers of BIALP.
Rights: © 2012 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
URI: http://hdl.handle.net/2433/176990
DOI(Published Version): 10.1271/bbb.110553
Appears in Collections:Journal Articles

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