In this study, an enzymatic procedure for the determination of glycine (Gly) was developed by using a column containing immobilized glutamate dehydrogenase (GDH) on glyoxal agarose beads. Ammonia is produced from the enzymatic reactions between Gly and GDH with NAD(+) in phosphate buffer medium. The indophenol blue method was used for ammonia detection based on the spectrophotometric measurements of blue-colored product absorbing at 640 nm. The calibration graph is linear in the range of 0.1-10 mM of Gly concentrations. The effect of pH, temperature, and time interval was studied to find column stability, and also the interference effects of other amino acids was investigated. The interaction between GDH and glyoxal agarose beads was analyzed by Fourier transform infrared (FTIR) spectroscopy. The morphology of the immobilized and non-immobilized agarose beads were characterized by atomic force microscopy (AFM).
We Report Herein Results of an Investigation of the Assembly of Silver Nanoparticles Mediated by Glutathione (GSH) and Cysteine (Cys) Interaction in the Presence of Metal Ions: Ag+, Cd2+, Co2+, Cu2+, Fe3+, Hg2+, Ni2+, Pb2+, Zn2+. The Silver Nanoparticles Produce Well-Ordered Structures upon Interaction with Glutathione in Variable Acidic Ph Condition and Exhibit Pronounced Changes in their Optical Properties Arising due to Electromagnetic Interaction. The Effect of Selected Metal Ions on the Nature of Complexation as Well as the Variation in the Optical Response due to Variable Degree of Complex Formation Amongst the Particles Have Been Investigated. The Changes in Optical Properties of the Silver Nanoparticles Have Been Accounted for the Complex Formation among the Aggsh, Cys and Metal Ions. The Complexes Have Been Characterized by UV-Vis Spectroscopy, FTIR, and AFM Studies. It Has Been Observed that the New Absorption Peaks Appear and Intensifies Depending on the Cys and Metal Ion Interaction. The Aggsh Nanoparticles Provided a Simple and Rapid Strategy to Detect Cys with the Aid of Metal Ions in Aqueous Solution. Different Metal Ions Give Different UV-Vis Spectra Profile and Show Different Sensitivity. This New Material Allows a Quantitative Assay of Cys down to the Concentration of 1× 10−5 M in Co2+ Ion Complexation. The Mechanism by which Metal Ions Can Bind with both the GSH Modified Ag Nanoparticles and Cys Molecule through Cooperative Metal–ligand Interactions Is Discussed.
İnvertaz enzimi (β-fruktofuranosidaz, EC 3.2.1.26) sükrozun fruktoz ve glukoza hidrolizini katalizleyen, endüstriyel alanda geniş uygulama alanına sahip, hidrolaz sınıfı enzimlerdendir. Günümüzde birçok enzim saflaştırma tekniği bulunmaktadır. Fakat bu yöntemler genellikle uzun ve çok sayıda işlem basamakları içermektedir. TPP (three-phase partitioning) yöntemi ise tek adımda, kısa işlem sonrası diğer tekniklere yakın oranda saflaştırma gerçekleştirebilmektedir. Endüstriyel proseslerde kullanılan enzim preparatlarının tercih edilmesinde önemli kriterlerden birisi bu preparatların kararlılığıdır. Enzim aktivitesinin zamana bağlı olarak korunmasında termik, mikrobiyal yıkım, pH, kimyasal inaktivasyon gibi faktörler etkilidir. Bu çalışmada kokulu kara üzümden (Vitis labrusca) izole edilen invertaz enziminin TPP yöntemiyle saflaştırılması sonrası termal kararlılığı incelendi. Saflaştırılan enzim 4-50 °C sıcaklık aralığında stabilitesini korudu.
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