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Immobilization of the serine protease from thermomonospora fusca yx



Immobilization of the serine protease from thermomonospora fusca yx



Journal of Agricultural & Food Chemistry 38(3): 918-922



The heat-stable serine protease from Thermomonospora fusca strain YX was immobilized by cyanogen bromide coupling to Sepharose-4B. The immobilized portease hydrolyzed low molecular weight substrates in accordance with Michaelis-Menton kinetics at 25.degree. C, while at 65.degree. C diffusion appeared to be rate-limiting. Immobilization of the protease increased its half-life at 85.degree. 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 .beta.-lactoglobulin. Hydrolysis was monitored by an acid precipitation method as well as colorimetric analysis of terminal amino groups.

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Accession: 007425035

Download citation: RISBibTeXText

PMID: 18595095

DOI: 10.1021/jf00093a070



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