Propitious catalytic response of immobilized α-amylase from G. thermoleovorans in modified APTES-Fe < sub > 3 < /sub > O < sub > 4 < /sub > NPs for industrial bio-processing

Int J Biol Macromol. 2024 Apr 30:132021. doi: 10.1016/j.ijbiomac.2024.132021. Online ahead of print.ABSTRACTChallenges in enzyme and product recovery are currently intriguing in modern biotechnology. Coping enzyme stability, shelf life and efficiency, nanomaterials-based immobilization were epitomized of industrial practice. Herein, a α-amylase from Geobacillus thermoleovorans was purified and bound effectively on to a modified 3-Aminopropyltriethoxysilane (APTES)-Fe3O4 nanoparticle. It was revealed that the carrier-bound enzyme catalysis (pH 8 and 60 °C) was significant in contrast to the free enzyme (pH 7.5 and 55 °C). Furthermore, Zn2+ and Cu2+ were shown to cause inhibitory effects in both enzyme states. Unlike chloroform, toluene, benzene, and butanol, minimal effects were observed with ethanol, acetone, and hexane. The bound enzyme retained 27.4 % of its initial activity after being stored for 36 days. In addition, the reusability of the bound enzyme showed a gradual decline in activity after the first cycle; however, after 13 cycles, its residual activity at 53 % was observed. These data proved significant enough to use this enzyme for industrial starch and analogous substrate bio-processing.PMID:38697441 | DOI:10.1016/j.ijbiomac.2024.132021
Source: International Journal of Biological Macromolecules - Category: Biochemistry Authors: Source Type: research