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A novel alkaliphilic Nocardiopsissp., strain TOA-1, was isolated from a tile-joint of a bathroom. Strain TOA-1 produced a variety of alkaline hydrolytic enzymes. An alkaline protease, designated NAPase, was purified and characterized. NAPase had a very high keratinolytic activity and high stability under acidic conditions.

The egIgene, encoding a major endoglucanase (EGI) of Scopulariopsis brevicaulisTOF-1212, was cloned and sequenced. The egIgene consisted of 868 bp with one intron and encoded a protein of 229 amino acids with a calculated molecular mass of 22,392 daltons. The EGI was assigned to a family 45 of glycosyl hydrolases and showed high similarity with other fungal endoglucanases, especially with those of Humicola griseaand Fusarium oxysporum, on the basis of hydrophobic cluster analysis. The egIgene was expressed under the promoter of the phosphoglycerate kinase gene (PGK) in Saccharomyces cerevisiae. The transformed cells were able to secrete the enzyme efficiently in an active form.

A keratinolytic alkaline proteae (NAPase) from Nocardiopsissp. TOA-1 degraded a scrapie prion without any chemical or physical treatment. Optimal temperature and pH were 60 °C and above pH 10.0. The scrapie prion was completely degraded within 3 min under optimal conditions.