Characterization of Immobilized β-N-Acetylhexosaminidase1


Journal Article

The properties of β -N -acetylhexosaminidase chemically bound to Sepharose 4B were determined and compared to those of the soluble enzyme. External diffusion effects on the kinetics of the immobilized enzyme were eliminated by assaying in a recirculation reactor with rapid flow rates. The immobilized β-N-acetylhexosaminidase exhibited a broad pH optimum quite similar to that of the soluble enzyme. Compared to the soluble enzyme the immobilized enzyme demonstrated a markedly enhanced stability at each pH and temperature investigated. Immobilization caused an increase in both the apparent Km and Ki, with. © 1977, Taylor & Francis Group, LLC. All rights reserved.

Full Text

Duke Authors

Cited Authors

  • Nunley, JA; Baricos, WH; Chambers, RP

Published Date

  • January 1, 1977

Published In

Volume / Issue

  • 10 / 6

Start / End Page

  • 501 - 514

Electronic International Standard Serial Number (EISSN)

  • 1532-236X

International Standard Serial Number (ISSN)

  • 0003-2719

Digital Object Identifier (DOI)

  • 10.1080/00032717708079394

Citation Source

  • Scopus