Importance of isoleucine residue in ion channel formation ability of 11-residue peptaibols.

Peptaibols are a class of short peptides, typically 7 to 20 amino acids long, characterized by noncanonical amino acid residues such as aminoisobutyric acid (Aib). Although the helix length is shorter than the membrane thickness, the 11-residue peptaibol trichorovin-XII (TV-XII) can form ion channels in membranes. Assuming that a higher proportion of isoleucine (Ile) relative to leucine (Leu) residues is crucial for maintaining the ion channel activity of TV-XII, peptide analogs of TV-XII with varying Ile content were designed, synthesized, and evaluated.

Characterization of a novel exo-chitosanase, an exo-chitobiohydrolase, from Gongronella butleri.

An exo-chitosanase was purified from the culture filtrate of Gongronella butleri NBRC105989 to homogeneity by ammonium sulfate precipitation, followed by column chromatography using CM-Sephadex C-50 and Sephadex G-100. The enzyme comprised a monomeric protein with a molecular weight of approximately 47,000 according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme exhibited optimum activity at pH 4.

Classification of chitosanases by hydrolytic specificity toward N¹,N⁴-diacetylchitohexaose.

The hydrolytic specificities of chitosanases were determined using N¹,N⁴-diacetylchitohexaose [(GlcN)₂-GlcNAc-(GlcN)₂-GlcNAc]. The results for the hydrolytic specificities of chitosanases belonging to subclasses I, II, and III toward chitohexaose and N¹,N⁴-diacetylchitohexaose agreed with previous results obtained by analysis of the hydrolysis products of partially N-acetylated chitosan. N¹,N⁴-Diacetylchitohexaose is a useful substrate to determine the hydrolytic specificity of chitosanase.

Characterization of a chitosanase from Aspergillus fumigatus ATCC13073.

Chitosanase II was purified from the culture filtrate of Aspergillus fumigatus ATCC13073. The purified enzyme had a molecular mass of 23.5 kDa.