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Title
Cellulose-gold nanohybrid as an effective support to enhance the catalytic efficiency and stability of α-amylase from Bacillus aquimaris
Type Article
Keywords
α-amylase Hybrid nanoparticles Immobilization Stability Reusability
Abstract
Cellulose nanocrystals/gold nanoparticle hybrids were synthesized under extreme conditions using hydrothermal treatment without utilizing toxic chemicals. The synthesis of the designed nanohybrid and enzyme immobilization process were confirmed by FT-IR, DLS, intrinsic fluorescence, UV–Vis spectroscopy, FESEM, and EDX techniques. The enzyme, in its free form, exhibited maximum activity at a pH of 10 and a temperature of 70 ◦C. However, when the enzyme was immobilized, its optimal temperature increased to 80 ◦C while its optimal pH remained constant. This catalytic platform significantly improved the thermal and chemical stability, along with enzyme stability at significant pH levels. Following a storage period of four weeks, it was observed that immobilized α-amylase retained 67.5 % of its initial activity, while free α-amylase retained only 17 % of its initial activity. The immobilized α-amylase exhibited a catalytic efficiency of 0.488 mM􀀀 1 s􀀀 1, which was found to be twice as high as that of the free form, which had a catalytic efficiency of 0.254 mM􀀀 1 s􀀀 1. The immobilized enzyme retained its initial activity up to 75 % after 11 consecutive uses. On the basis of the obtained results, it appears that the manufactured immobilized enzyme represents an appropriate choice for industrial use under harsh conditions.
Researchers Roohullah Hemmati (Third researcher) , Dariush Saberi (Fourth researcher) , Soudabeh Kavousipour (Fifth researcher)