Abstract

AbstractIt has been shown with the aid of chemical analysis, gel permeation chromatographic analysis of malto‐oligosaccharide mixtures produced by the action of α‐amylase (1, 4,‐α‐D‐glucan glucanohydrolase, E. C. 3. 2. 1. 1.) and photomicroscopy, that dyed amylosic fragments, produced by the conventional action of α‐amylase on Cibacron® Blue 3G‐A dyed amylose substrates, can become adsorbed by microcrystalline cellulose. The adsorption occurs between the aromatic residues of the dye molecule and the surface of microcrystalline cellulose, and only when the amount of solubilisation of the dyed amylose substrate is high. Thus, under these circumstances erroneously low values for α‐amylase activity will be obtained when using such a chromogenic substrate due to adsorption of soluble dyed fragments onto the surface of microcrystalline cellulose, thereby escaping detection. When α‐amylase levels are low, thereby causing little solubilisation of the dyed substrate, as is frequently the case in clinical chemistry, the amount of absorption cannot be detected and therefore the use of microcrystalline cellulose as a tablet binder to facilitate the routine use of these dyed amylose chromogenic substrates is permissible.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.