Albuminated Glycoenzymes: Enzyme Stabilization through Orthogonal Attachment of a Single-Layered Protein Shell around a Central Glycoenzyme Core. Academic Article

abstract

• Here we demonstrate an approach to stabilize enzymes through the orthogonal covalent attachment of albumin on the single-enzyme level. Albuminated glycoenzymes (AGs) based upon glucose oxidase and catalase from Aspergillus niger were prepared in this manner. Gel filtration chromatography and dynamic light scattering support modification, with an increase in hydrodynamic radius of ca. 60% upon albumination. Both AGs demonstrate a marked resistance to aggregation during heating to 90 C, but this effect is more profound in albuminated catalase. The functional characteristics of albuminated glucose oxidase vary considerably with exposure type. The AG's thermal inactivation is reduced more than 25 times compared to native glucose oxidase, and moderate stabilization is observed with one month storage at 37 C. However, albumination has no effect on operational stability of glucose oxidase.

authors

• McShane, Michael

published proceedings

• Bioconjug Chem

altmetric score

• 0.75

author list (cited authors)

• Ritter, D. W., Newton, J. M., Roberts, J. R., & McShane, M. J.

citation count

• 1

complete list of authors

• Ritter, Dustin W||Newton, Jared M||Roberts, Jason R||McShane, Michael J

publication date

• May 2016

publisher

• American Chemical Society (ACS)  Publisher

published in

• Bioconjugate Chemistry  Journal

keywords

• Animals
• Aspergillus Niger
• Catalase
• Cattle
• Enzyme Stability
• Glucose Oxidase
• Serum Albumin, Bovine
• Temperature

PubMed Central ID

• 27111632

Digital Object Identifier (DOI)

• 10.1021/acs.bioconjchem.6b00103

start page

• 1285

end page

• 1292

volume

• 27

issue

• 5

URL

• http://dx.doi.org/10.1021/acs.bioconjchem.6b00103