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Updated: May 4, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Characteristics of a highly thermostable neutral protease produced fromBacillus stearothermophilus
1Department of Food Science and Technology, Faculty of Agriculture, Kyushu University, 6-10-1, Hakozaki, Higashi-ku, 812, Fukuoka, Japan.
Abstract:
A highly thermostable neutral protease was found in culture filtrates ofBacillus stearothermophilus. The optimum reaction pH and temperature of this protease were 6.0 and 60°C, respectively, and 90% activity remained even after heat treatment at 90°C for 30 min. The protease was markedly inactivated by diisopropyl fluorophosphate, but EDTA and iodoacetic acid hardly affected it. The neutral protease therefore could be defined as a highly thermostable, neutral(-serine) protease.
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