Authors
Trisha Tissopi, Santosh Prasad, Surabhi Gurjar, Pooja J Rao, Sarma Mutturi
Published in
Applied biochemistry and biotechnology. Jun 23, 2026. Epub Jun 23, 2026.
Abstract
In this study, divalent metal ions (Zn²⁺, Cu²⁺, and Mn²⁺) were employed for the in situ synthesis of highly stable hybrid nanoflowers (tAG-NFs) to immobilize transglycosylating α-glucosidase (tAG) for isomaltooligosaccharide (IMO) production. Characterization via SEM, FTIR, and XRD confirmed the successful formation of these distinct nanostructures and increased crystallinity. Optimization revealed that the Mn-tAG-NF system achieved the highest immobilization efficiency (~ 46%). This architecture demonstrated superior enzyme stability, retaining 41.61% activity at 64 °C and exhibiting high storage stability and reusability (~ 50% activity after five cycles), significantly outperforming the free enzyme. Kinetic analysis showed that immobilization generally enhanced substrate affinity (reduced Km). Crucially, HPLC studies confirmed that the Zn-tAG-NF and Mn-tAG-NF architectures successfully modulated the enzyme's catalytic specificity. These systems suppressed competing hydrolysis and favored the desired transglycosylation reaction, resulting in significantly higher IMO yields (Zn-tAG-NF: 0.52 ± 0.06 g/g maltose; Mn-tAG-NF: 0.47 ± 0.03 g/g maltose) and lower glucose byproduct compared to free tAG (0.37 ± 0.06 g/g maltose). This work demonstrates that the choice of divalent metal ion is critical for tailoring tAG nanoflower properties, providing a novel method to enhance enzyme stability and product selectivity for industrial biocatalysis.
PMID:
42334819
Bibliographic data and abstract were imported from PubMed on 23 Jun 2026.
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