Scientific Reports (Aug 2023)

Immobilization of α-transglucosidase on silica-coated magnetic nanoparticles and its application for production of isomaltooligosaccharide from the potato peel

  • Rohit Maurya,
  • Usman Ali,
  • Sunaina Kaul,
  • Raja Bhaiyya,
  • Ravindra Pal Singh,
  • Koushik Mazumder

DOI
https://doi.org/10.1038/s41598-023-38266-8
Journal volume & issue
Vol. 13, no. 1
pp. 1 – 16

Abstract

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Abstract In this study, the production of isomaltooligosaccharide from potato peel starch was carried out in three steps: liquefaction, saccharification, and transglucosylation. Further, cloning α-transglucosidase gene from Aspergillus niger (GH31 family), transforming into E. coli BL21 (DE3), overexpressing and purifying the resulting protein for the production of α-transglucosidase. The generated α-transglucosidase was then bound with magnetic nanoparticles, which improved reusability up to 5 cycles with more than 60% activity. All the modifications were characterized using the following methods: Fourier transform infra-red analysis, Transmission Electron Microscopy, Field Emission Scanning Electron Microscopy, Energy Dispersive X-ray spectroscopy, X-Ray Diffraction Spectroscopy, Thermogravimetric Analysis, and Dynamic Light Scattering (DLS) analysis. Further, the optimum conditions for transglucosylation were determined by RSM as follows: enzyme-to-substrate ratio 6.9 U g−1, reaction time 9 h, temperature 45 °C, and pH 5.5 with a yield of 70 g l−1 (± 2.1). MALDI-TOF–MS analysis showed DP of the IMOs in ranges of 2–10. The detailed structural characterization of isomaltooligosaccharide by GC–MS and NMR suggested the α-(1 → 4) and α-(1 → 6)-D-Glcp residues as major constituents along with minor α-(1 → 2) and α-(1 → 3) -D-Glcp residues.