Metal-induced stabilization of trypsin modified with alpha-oxoglutaric acid.
Alpha-oxoglutaric acid was attached to trypsin via reductive alkylation with NaBH4 thereby introducing metal-chelating groups at the protein surface. The thermostability of the modified enzyme was increased by 6.5-13 degrees C and its resistance to autolytic degradation was improved 2- to 4-fold in 5 mM ZnCl2, MnCl2 or MgCl2.
Villalonga
Maria L
ML
Enzyme Technology Group, Center for Biotechnological Studies, University of Matanzas, Matanzas, C.P. 44740, Cuba.
Reyes
Gretel
G
Villalonga
Reynaldo
R
D000478:Alkylation; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004789:Enzyme Activation; D004795:Enzyme Stability; D007656:Ketoglutaric Acids / Q000737:chemistry*; D008670:Metals / Q000737:chemistry*; D010084:Oxidation-Reduction; D010179:Pancreas / Q000201:enzymology*; D011485:Protein Binding; D011489:Protein Denaturation; D013329:Structure-Activity Relationship; D013696:Temperature; D014357:Trypsin / Q000737:chemistry*
D007656:Ketoglutaric Acids; D008670:Metals; D014357:Trypsin