title: Biochemical and kinetic study of laccase from Ganoderma cupreum AG-1 in hydrogels.
abstract: In the present study, three different types of hydrogels i.e., (poly (-acrylamide)/alginate (P (AAm)/Alg), poly (acrylamide-N-isopropylacrylamide) (P (AAm-NIPA)), and poly (acrylamide-N-isopropylacrylamide)/alginate (P (AAm-NIPA)/Alg)) were synthesized by acrylamide, alginate, and N-isopropylacrylamide for the entrapment of laccase. The hydrogel-entrapped and free laccase showed optimum temperature of 50 °C for the oxidation of ABTS, but the entrapped laccase showed high temperature, pH, and storage stability as compared to the free enzyme. The K m values of free laccase, (P (AAm)/Alg)-L, (P (AAm-NIPA))-L, and (P (AAm-NIPA)/Alg)-L were found to be 0.13, 0.28, 0.33, and 0.50 mM, respectively. The V max values of free laccase, (P (AAm)/Alg)-L, (P (AAm-NIPA))-L, and (P (AAm-NIPA)/Alg)-L were found to be 22.22 × 10(2), 5.55 × 10(2), 5.0 × 10(2), and 4.54 × 10(2) mM/min, respectively. The entrapped laccase hydrogels were used for the decolorization of Reactive Violet 1 dye, with 39 to 45 % decolorization efficiency till the 10th cycle.
authors.affiliation: Department of Microbiology, Natubhai V. Patel College of Pure and Applied Sciences, Vallabh Vidyanagar, Gujarat, 388 120, India.
authors.forename: Mayur
authors.initials: M
authors.lastname: Gahlout
authors.forename: Shilpa
authors.initials: S
authors.lastname: Gupte
authors.forename: Akshaya
authors.initials: A
authors.lastname: Gupte
mesh_terms: D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry*; D032902:Ganoderma / Q000737:chemistry / Q000201:enzymology*; D006358:Hot Temperature; D020100:Hydrogels / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D042845:Laccase / Q000737:chemistry*
chemical_list: D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D020100:Hydrogels; D042845:Laccase