Glucose oxidase stabilization against thermal inactivation using high hydrostatic pressure and hydrophobic modification.

Abstract:

:High hydrostatic pressure (HHP) stabilized glucose oxidase (GOx) against thermal inactivation. The apparent first-order kinetics of inactivation of GOx were investigated at 0.1-300 MPa and 58.8-80.0°C. At 240 MPa and 74.5°C, GOx inactivated at a rate 50 times slower than at atmospheric pressure at the same temperature. The apparent activation energy of inactivation at 300 MPa was 281.0 ± 17.4 kJ mol-1 or 1.3-fold smaller than for the inactivation at atmospheric pressure (378.1 ± 25.6 kJ mol-1 ). The stabilizing effect of HHP was greatest at 74.5°C, where the activation volume of 57.0 ± 12.0 cm3  mol-1 was highest compared to all other studied temperatures. Positive apparent activation volumes for all the treatment temperatures confirmed that HHP favors GOx stabilization. A second approach to increase GOx stability involved crosslinking with N-(3-dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (EDC) and either aniline or benzoate. The modified enzyme remained fully active with only slight increases in KM (1.3-1.9-fold increases for aniline and benzoate modification, respectively). The thermal stability of GOx increased by 8°C with aniline modification, while it decreased by 0.9°C upon modification with benzoate. Biotechnol. Bioeng. 2017;114: 516-525. © 2016 Wiley Periodicals, Inc.

journal_name

Biotechnol Bioeng

authors

Halalipour A,Duff MR Jr,Howell EE,Reyes-De-Corcuera JI

doi

10.1002/bit.26185

subject

Has Abstract

pub_date

2017-03-01 00:00:00

pages

516-525

issue

3

eissn

0006-3592

issn

1097-0290

journal_volume

114

pub_type

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