Assay for glucose oxidase from Aspergillus niger and Penicillium amagasakiense by Fourier transform infrared spectroscopy

Purification, biochemical characterization and antifungal activity of a novel Aspergillus tubingensis glucose oxidase steady on broad range of pH and temperatures

“…In fact, FTIR spectra analysis of the hydrolysis products of the purified enzyme revealed functional characteristics including a broad-stretching C-O and C=O groups at 1209 and 1732.16 cm -1 , respectively, suggesting the formation of D-glucono-1,5-lactone in the enzymatic reaction. These results are in agreement with the studies of Karmali et al [43] and Anas et al [31] who used the FT-IR technique to assay for GOD activity and to investigate its kinetic behavior. The purified enzyme showed a high affinity for b-D-glucose.…”

Micro-biofuel cell powered by glucose/O2 based on electro-deposition of enzyme, conducting polymer and redox mediators: Preparation, characterization and performance in human serum

“…or O-H str.) are characteristics of either d-glucono-1,5-lactone or d-gluconic acid (Tajmir-Riahi, 1989;Karmali et al, 2004). The two weak transmission peaks situated at 3334 and 1682 cm −1 in Fig.…”

Modification of carbon nanotubes with redox hydrogel: Improvement of amperometric sensing sensitivity for redox enzymes

“…Most of the assays for enzyme activity and for kinetic studies of enzyme reactions involve the use of auxiliary enzymes to generate easily detectable species such as NAD(P) + or chromophores which absorb strongly either in ultraviolet or visible regions of spectrophotometers (Karmali et al, 2004;Bergmeyer, 1974). These linked enzyme assays present some disadvantages since the presence of other substances and enzymes in the reaction mixture may affect the kinetic behavior of the enzyme that is being investigated (Karmali et al, 2004).…”

“…These linked enzyme assays present some disadvantages since the presence of other substances and enzymes in the reaction mixture may affect the kinetic behavior of the enzyme that is being investigated (Karmali et al, 2004). On the other hand, the assay conditions (i.e., temperature, pH, and ionic strength) may not be the same for different enzymes involved in the assay system (Schindler and Lendl, 1999).…”

“…Therefore, it is of great interests to devise novel enzyme assays that are specific and fast and do not require auxiliary enzymes. Recently, Karmali et al reported the use of Fourier transform infrared (FTIR) spectroscopy as a simple and direct assay method for the activity of GOD (Karmali et al, 2004). However, this method can only be applied to the enzymes for which the substrate and the product have quite distinguishable frequencies of IR absorbing.…”