Published March 1990
| public
Journal Article
Immobilization of the serine protease from Thermomonospora fusca YX
Chicago
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Abstract
The heat-stable serine protease from Thermomonospora fusca strain YX was immobilized by cyanogen bromide coupling to Sepharose-4B. The immobilized protease hydrolyzed low molecular weight substrates in accordance with Michaelis-Menton kinetics at 25 °C, while at 65 °C diffusion appeared to be rate-limiting. Immobilization of the protease increased its half-life at 85 °C, by a factor of 3 at pH 6.25 and by a factor of 5 at pH 8.50. A packed column of the immobilized protease efficiently hydrolyzed both bovine serum albumin and β-lactoglobulin. Hydrolysis was monitored by an acid precipitation method as well as colorimetric analysis of terminal amino groups.
Additional Information
© 1990 American Chemical Society. Received for review March 6, 1989. Accepted November 13, 1989. We thank J. B. Hunter for her advice and I. J. Brockman for assistance in preparation of protease. This study was supported in part by a grant to T.W.G. from the Cornell Biotechnology Program.Additional details
- Eprint ID
- 86132
- Resolver ID
- CaltechAUTHORS:20180430-145300353
- Cornell Biotechnology Program
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