Isolation, Specificity, and Application of β-N-Acetylhexosaminidases from Penicillium crustosum

β-N-acetylhexosaminidases have great potential in applied biocatalysis owing to their ability act on a wide range of natural and modified substrates. In this work, from four Penicillium crustosum strains (PcHex) were studied. The production showed the highest enzymatic activity culture medium after 11–14 days cultivation. specific isolated purified PcHex hydrolysis 4-nitrophenyl-N-acetyl-β-D-galactopyranoside was 15–20 U/mg protein. All similar pH–activity profiles, with optimum pH being 4.0–5.0 temperature 40 °C–50 °C. Apart standard substrates, two synthetic substrates (5-bromo-4-chloro-3-indolyl-N-acetyl-β-D-galactoside 2-chloro-4-nitrophenyl-β-D-galactopyranoside) tested successfully hydrolyzed using β-N-acetylhexosaminidase preparations. Maximum toward fluorogenic substrate 4-methylumbelliferyl-N-acetyl-β-D-galactopyranoside (4MU-β-GalNAc) observed for enzyme preparations PcHex1 (15.38 protein) swab samples books Slovak National Museum Martin (Slovak Republic) stored our laboratory. same preparation used selective β-anomer 4MU-GalNAc an anomeric mixture 4MU-α/β-GalNAc. Thus, pure α-anomer (with total yield 90%) separated mixture, which suggests application these enzymes.