These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and characterization of a thermostable and highly specific beta-N-acetyl-D-glucosaminidase from Aspergillus niger 419.
    Author: Pera LM, Infante Majollí MV, Baigorí MD.
    Journal: Biotechnol Appl Biochem; 1997 Dec; 26(3):183-7. PubMed ID: 9428156.
    Abstract:
    After a 10.5-fold purification, beta-N-acetyl-D-glucosaminidase (EC 3.2.1.52) produced by Aspergillus niger 419, showed the following main characteristics: maximum activity at 65 degrees C, pH 4.5; K(m) and kcat using p-nitrophenyl-N-acetyl-beta-D-glucosaminide as substrate, 0.2 mM and 0.93 x 10(4) min-1, respectively; Ea, 30.5 kJ/mol; molecular mass, 131,000 Da; pI 4.4. The activity after heating for 15 min at 70, 75 and 80 degrees C was 70, 28 and 13% of that found at 65 degrees C, respectively. The enzyme was active in reaction mixtures containing glycerol, ethanol, methanol, propan-2-ol, acetone or dioxan. The presence of Sr2+ or Ca2+ enhanced the activity, while it was inhibited by Cu2+ and Fe3+. The enzyme was highly specific for p-nitrophenyl N-acetyl-beta-D-glucosaminide and no activity was found when p-nitrophenyl derivatives of N-acetyl-beta-D-galactosaminide, beta-D-galactopyranoside and beta-D-N,N'-diacetylchitobiose were tested as substrates. Due to its thermostability, specificity and resistance to different organic solvents, the enzyme might be a potentially useful tool for the analysis and production of oligosaccharides.
    [Abstract] [Full Text] [Related] [New Search]