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Immobilization of α-amylase in ultrafine polyvinyl alcohol (PVA) fibers via electrospinning and their stability on different substrates
- Porto, Mariana Dias Antunes, dos Santos, Jaqueline Pozzada, Hackbart, Helen, Bruni, Graziella Pinheiro, Fonseca, Laura Martins, da Rosa Zavareze, Elessandra, Dias, Alvaro Renato Guerra
- International journal of biological macromolecules 2019 v.126 pp. 834-841
- Fourier transform infrared spectroscopy, alpha-amylase, corn starch, electrolysis, enzyme activity, hydrolysis, pH, polyvinyl alcohol, scanning electron microscopy, starch, temperature, wheat starch
- The objective of this study was to immobilize α-amylase in ultrafine polyvinyl alcohol (PVA) fibers by electrolysis and to evaluate its stability at different temperatures and pHs using various starch substrates such as corn starch and germinated and ungerminated wheat starches. The α-amylase-loaded ultrafine fibers were characterized by scanning electron microscopy (SEM), Fourier transform infrared spectroscopy (FT-IR), and loadability and enzymatic activity evaluations. Incorporation of the enzyme resulted in a slight change in fiber morphology; the fibers became flatter and thicker with increasing enzyme concentration. The mean diameters ranged from 187 to 282 nm. FT-IR spectra indicated that the enzyme was incorporated into the fibers. PVA showed a high loading capacity for α-amylase at all concentrations tested (1.0, 1.5, and 2.0% w/v), indicating that PVA is an excellent support. The enzymatic activity of α-amylase was tested on the different starch substrates; the activity was higher in the immobilized form than in the free form. Enzymatic immobilization improved the stability of α-amylase over a wide range of temperatures and pHs. Enzymatic activity was highest when germinated wheat starch was used as the substrate at different temperatures and pHs, indicating great potential for its application in hydrolysis with α-amylase.