Ticona Alonso R Poma, da Silva Neto Mário, de Marco Janice Lisboa, Cabrera Roberto Castellanos, Hamann Pedro R Vieira, Polikarpov Igor, Noronha Eliane Ferreira
Enzyme Biotechnology Research Laboratory, Science Faculty, Universidad Nacional Jorge Basadre Grohmann, 23003, Tacna, Peru.
Department of Cell Biology, Institute of Biological Sciences, University of Brasilia, Brasilia, D.F, 70910-900, Brazil.
Biotechnol Lett. 2025 Jul 30;47(4):83. doi: 10.1007/s10529-025-03624-1.
Currently, the shift to a greener economy requires the prospection of new industrial processes to reduce greenhouse-gas emissions. Enzymatic catalysis is considered a green alternative to traditional industrial processes. Among enzymes of industrial relevance, starch-degrading enzymes, such as α-amylases, have received attention because of their enormous potential to hydrolyze starch-based materials, generating smaller sugars that can be used for the biosynthesis of chemicals of industrial relevance, such as ethanol. In the present study, a new isolate of Paenibacillus barengoltzii was obtained from cow rumen and its potential to produce amylases was evaluated. Additionally, a recombinant amylase, AmyPb, was produced and biochemically characterized. AmyPb displays high activity at elevated temperatures (55 °C) and can withstand elevated temperatures. The experimentally calculated melting temperature showed that AmyPb is more stable in alkaline environments, with a Tm of 59 °C at pH 9. AmyPb hydrolyzed potato and cassava starches with hydrolysis efficiencies of 28 and 55%, respectively. The results of this study are relevant for the development of industrial processes that employ thermostable amylases.
目前，向绿色经济转型需要探寻新的工业流程以减少温室气体排放。酶催化被认为是传统工业流程的绿色替代方案。在具有工业相关性的酶中，淀粉降解酶，如α-淀粉酶，因其具有水解淀粉基材料的巨大潜力而受到关注，可生成较小的糖类，这些糖类可用于生物合成具有工业相关性的化学品，如乙醇。在本研究中，从奶牛瘤胃中获得了一种新的巴伦戈尔茨类芽孢杆菌分离株，并评估了其产生淀粉酶的潜力。此外，还生产了一种重组淀粉酶AmyPb，并对其进行了生化特性表征。AmyPb在高温（55°C）下表现出高活性，并且能够耐受高温。实验计算得出的解链温度表明，AmyPb在碱性环境中更稳定，在pH 9时的解链温度为59°C。AmyPb分别以28%和55%的水解效率水解马铃薯淀粉和木薯淀粉。本研究结果对于采用耐热淀粉酶的工业流程开发具有重要意义。
