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- W4309396807 abstract "Enzyme immobilization on adequate carriers is a challenging strategy. Understanding the enzyme-carrier interactions and their effects on enzyme conformation and bioactivity is critical. In this study, a meso-macropores silica (MMS) was used to immobilize β-galactosidase from the yeast Kluyveromyces lactis (β-gal-KL) by physical adsorption. The bioactivity of the immobilized β-gal-KL was altered, evidenced by the increased Km , decreased Vmax and kcat , and increased activity at alkaline values. By performing infrared spectroscopy analysis and subsequent secondary structure assessment from the amide I band, the immobilized β-gal-KL suffered a β-sheet (∼31-35 %) to α-helix (∼15-19 %) transition with increased turns (∼21-22 %) with respect to the free β-gal-KL having ∼12 % α-helix, ∼42 % β-sheet, and ∼17 % turns. These findings led us to correlate the observed bioactivity performance to structural alterations to a non-native conformation. The presented line of thought can lead to a better understanding of the reasons causing bioactivity alterations upon enzyme immobilization." @default.
- W4309396807 created "2022-11-26" @default.
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- W4309396807 date "2022-12-01" @default.
- W4309396807 modified "2023-09-25" @default.
- W4309396807 title "Immobilization of <i>Kluyveromyces lactis</i> β‐Galactosidase on Meso‐macroporous Silica: Use of Infrared Spectroscopy to Rationalize the Catalytic Efficiency" @default.
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- W4309396807 doi "https://doi.org/10.1002/cplu.202200340" @default.
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