Thermal Stabilization of Fungal Beta-Glucosidase Through Glutaraldehyde Crosslinking

J. O. Baker; K. K. Oh; K. Grohmann; M. E. Himmel

doi:10.1007/BF01026159

Thermal Stabilization of Fungal Beta-Glucosidase Through Glutaraldehyde Crosslinking

J. O. Baker, K. K. Oh, K. Grohmann, M. E. Himmel

BioEconomy and Sustainable Transportation

National Renewable Energy Laboratory

Research output: Contribution to journal › Article › peer-review

23 Scopus Citations

Abstract

The thermal stability of a purified Aspergillus niger β-glucosidase (EC 3.2.1.21) has been dramatically increased by intramolecular crosslinking with glutaraldehyde at pH 9.0, followed by borohydride reduction. The stabilization has been shown to be due to the formation of a distinct subpopulation of enzyme molecules, the activity of which has a half-life at 65°C of approximately 40 hours, which is some 80 times as long as that of the native enzyme at this temperature.

Original language	American English
Pages (from-to)	325-330
Number of pages	6
Journal	Biotechnology Letters
Volume	10
Issue number	5
DOIs	https://doi.org/10.1007/BF01026159 https://doi.org/10.1007/BF01026159
State	Published - May 1988

NREL Publication Number

ACNR/JA-232-10214

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AB - The thermal stability of a purified Aspergillus niger β-glucosidase (EC 3.2.1.21) has been dramatically increased by intramolecular crosslinking with glutaraldehyde at pH 9.0, followed by borohydride reduction. The stabilization has been shown to be due to the formation of a distinct subpopulation of enzyme molecules, the activity of which has a half-life at 65°C of approximately 40 hours, which is some 80 times as long as that of the native enzyme at this temperature.

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Thermal Stabilization of Fungal Beta-Glucosidase Through Glutaraldehyde Crosslinking

Abstract

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