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Poly(acrylamide/vinylsulfonic acid) hydrogel for invertase immobilization
Author(s) -
Öztop Hes.,
Akyildiz Furkan,
Saraydin Dursun
Publication year - 2020
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/jemt.23542
Subject(s) - invertase , acrylamide , self healing hydrogels , chemistry , swelling , nuclear chemistry , diffusion , polymer chemistry , immobilized enzyme , michaelis–menten kinetics , thermal stability , polymerization , polymer , enzyme , biochemistry , enzyme assay , chemical engineering , organic chemistry , physics , engineering , copolymer , thermodynamics
Poly (acrylamide/vinylsulfonic acid) PA/VSA and poly (acrylamide) PA hydrogels were prepared by free radical polymerization in the presence of a crosslinker, to be used as a support for the invertase enzyme. Spectrophotometric, thermal analysis methods, swelling, and diffusion experiments were used for the characterization of hydrogels. SEM images show that the hydrogels have a smooth, homogeneous, highly porous and spongy morphology. The swelling of PA/VSA was higher than that of PA in water. The diffusion of water within the hydrogel was found to be non‐Fickian. Invertase was immobilized onto PA and PA/VSA (immobilized invertases named PA‐I and PA/VSA‐I, respectively). The optimum pH values were found to be; 5.0, 3.0, and 3.0 for free invertase, PA‐I, and PA/VSA‐I, respectively. The optimum temperature values were 40°C, 50°C, and 60°C for free invertase, PA‐I and PA/VSA‐I respectively. Michaelis Constant, K m ; for free invertase and PA‐I and PA/VSA‐I were found to be 11.80, 21.40, and 18.42 mM, respectively. Maximum reaction rate; V max value for free invertase and PA‐I and PA/VSA‐I were found to be 7.46 μmol min −1 , 5.91 μmol min −1 , and 6.35 μmol min −1 , respectively. PA/VSA‐I showed excellent thermal, operational, storage, and pH stability.