Biochemical and thermodynamic characterization of de novo synthesized β-amylase from fenugreek

Agrawal, Dinesh Chand; Dwevedi, Alka; Kayastha, Arvind M.

doi:10.1016/j.ijbiomac.2019.02.162

Cited by 11 publications

(1 citation statement)

References 51 publications

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“…Extremozymes possess useful native metabolic functions with potential for application in industrial and biotechnological processes. These include: cellulases (Ueda et al 2010;Li et al 2018), and other carbohydrate-degrading enzymes such as esterases (Charavgi et al 2013), amylases (Agrawal, Dwevedi, and Kayastha 2019;Wu et al 2018), xylanases (Basit et al 2018;Sunna and Bergquist 2003), proteases (Jayakumar et al 2012;Barzkar et al 2018), pectinases (Kaur and Satyanarayana 2004), keratinases (Wu et al 2017;Korniłłowicz-Kowalska and Bohacz 2011), lipases (Schreck and Grunden 2014), peroxidases (Merlino et al 2010) and phytases (Jatuwong et al 2020;Berka et al 1998).…”

Section: Mesophilic Vs Extremophilic Enzymesmentioning

confidence: 99%

Thermophilic Enzymes

Viegas

Ramos

Fernandes

2021

UPjeng

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Substantial improvements in the industrial production of goods led to a widespread feeling of unlimited access to food, commodities, and energy. As greener alternatives for industrial processes are in demand, scientists have turned to enzymes, looking for apt biocatalysts. Focusing on extremophiles, this mini review draws a comparison between thermophiles and their mesophilic counterparts, exploring what features are instrumental to their thermostability. A higher number of ion-pairs, hydrophobicity of buried side chains, compact tertiary structure cores, and a complex network of hydrogen bonds are the four main characteristics responsible for the robustness of thermophilic enzymes.

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