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Isolation, Specificity, and Application of β-IN/I-Acetylhexosaminidases from IPenicillium crustosum/I

Applied sciences, 2023-03, Vol.13 (6) [Peer Reviewed Journal]

COPYRIGHT 2023 MDPI AG ;ISSN: 2076-3417 ;EISSN: 2076-3417 ;DOI: 10.3390/app13063399

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  • Title:
    Isolation, Specificity, and Application of β-IN/I-Acetylhexosaminidases from IPenicillium crustosum/I
  • Author: Ondrejková, Ema ; Hronská, Helena ; Štefuca, Vladimír ; Bláhová, Mária ; Rosenberg, Michal
  • Subjects: Enzymes ; Hydrolysis
  • Is Part Of: Applied sciences, 2023-03, Vol.13 (6)
  • Description: β-N-acetylhexosaminidases have great potential in applied biocatalysis owing to their ability to act on a wide range of natural and modified substrates. In this work, β-N-acetylhexosaminidases from four Penicillium crustosum strains (PcHex) were studied. The production strains showed the highest enzymatic activity in the culture medium after 11-14 days of cultivation. The specific activity of the isolated and purified PcHex of hydrolysis of 4-nitrophenyl-N-acetyl-β-D-galactopyranoside was 15-20 U/mg protein. All isolated β-N-acetylhexosaminidases showed similar pH-activity profiles, with the optimum pH being 4.0-5.0 and the optimum temperature being 40 °C-50 °C. Apart from standard substrates, two synthetic substrates (5-bromo-4-chloro-3-indolyl-N-acetyl-β-D-galactoside and 2-chloro-4-nitrophenyl-β-D-galactopyranoside) were tested and successfully hydrolyzed using β-N-acetylhexosaminidase preparations. Maximum activity toward the fluorogenic substrate 4-methylumbelliferyl-N-acetyl-β-D-galactopyranoside (4MU-β-GalNAc) was observed for enzyme preparations from PcHex1 (15.38 U/mg protein) isolated from swab samples of books in the Slovak National Museum in Martin (Slovak Republic) and stored in our laboratory. The same enzyme preparation was used for the selective hydrolysis of β-anomer of 4MU-GalNAc from an anomeric mixture of 4MU-α/β-GalNAc. Thus, pure α-anomer (with the total yield being 90%) was separated from the mixture, which suggests the application potential of these enzymes.
  • Publisher: MDPI AG
  • Language: English
  • Identifier: ISSN: 2076-3417
    EISSN: 2076-3417
    DOI: 10.3390/app13063399
  • Source: ROAD: Directory of Open Access Scholarly Resources
    ProQuest Central
    DOAJ Directory of Open Access Journals
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