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Seasonal Dynamics of Bacterial and Fungal Lineages in Extreme Environments
Published in Suhaib A. Bandh, Javid A. Parray, Nowsheen Shameem, Climate Change and Microbial Diversity, 2023
Nafeesa Farooq Khan, Uzma Zehra, Zafar A. Reshi, Manzoor Ahmad Shah, Tawseef Rehman Baba
The genetic basis to highlight adaptive responses to high temperatures is researched more intensively among all hostile environments. Among biomolecules (DNA, proteins, and lipids), the most deliberate aspect of adaptation for thermophiles is found in proteins. Proteins lose their activity (denature) at high temperatures and eventually lead to a considerable rise in the membrane fluidity and thus alter the metabolic activities. Thermophiles display a range of cellular alterations to avoid diminishing properties, in view of essential metabolic proteins and in them, the frequency of (double and single) esters are more (Schulze-Makuch and Guinan, 2016); thus enhancing the membrane mobility to a full extent. Unlike other organisms, heat stable proteins apropos of thermophiles are very small and alkaline (Bell et al., 2015). The thermostability is possibly a result of the following interactions: (1) hydrogen bonds; (2) reduced loop lengths of proteins; (3) increased secondary bonding propensity; (4) core hydrophobicity; (5) week interactions (van der Waals force); and (6) enhanced ionicity and protein packaging (Brininger et al., 2018). The enzyme’s rigidity and noncompliance to remove complex packaging, predominated by rising temperature correspond by and large to escalated bi-sulfide bonding, joining two Cysteines (Reed et al., 2013; Siliakus et al., 2017).
Proteases from Thermophiles and Their Industrial Importance
Published in Devarajan Thangadurai, Jeyabalan Sangeetha, Industrial Biotechnology, 2017
D. R. Majumder, Pradnya P. Kanekar
The general advantages of enzymes from thermophiles are as follows (Rakshit et al., 2003): (1) Lesser stringency in the maintenance of sterile conditions as contamination is lower due to the increased temperature; (2) Fermentation allows a higher operational temperature which has a significant influence on the bioavailability and solubility of organic compounds; (3) Elevated process temperatures leads to higher reaction rates due to a decrease in viscosity and an increase in diffusion coefficient of substrates and higher process yield due to increased solubility of substrates and products and favorable equilibrium displacement in endothermic reactions; and (4) Volatile products can be easily recovered. Stability of bioactive molecules against temperature, denaturing agents like detergents and organic solvents, extreme pH conditions enhances their industrial and biotechnological applications. The fermentation is cost effective as elaborate cooling conditions are not required. Thermostable enzymes can also be used as models for the understanding of thermostability and thermoactivity, which is useful for protein engineering.
Recent Advances in Enzyme Immobilization Using Nanomaterials and its Applications for the Production of Biofuels
Published in Madan L. Verma, Nanobiotechnology for Sustainable Bioenergy and Biofuel Production, 2020
Sujit Sadashiv Jagtap, Ashwini Ashok Bedekar
The thermal stability of the enzyme includes three different types including thermodynamic, process stability and kinetic stability (Kumar et al. 2000). Multiple factors including hydrophobic interactions and hydrogen bonds affect the thermostability of enzymes. Several methods have been used to improve the thermal stability of the enzyme, including the introduction of disulfide bonds, salt bridges, hydrogen bonds, optimizing surface charge of the protein, optimizing the free energy of protein unfolding and chemical cross-links (Verma et al. 2012, Yang et al. 2015). The single or few point mutations also largely changed its thermal stability (Packer and Liu 2015).
Characterization and application of a crude bacterial protease to produce antioxidant hydrolysates from whey protein
Published in Preparative Biochemistry & Biotechnology, 2023
Andréia Monique Lermen, Naiara Jacinta Clerici, Dienefer Borchartt Maciel, Daniel Joner Daroit
In addition to thermoactivity, the thermostability of enzymes plays a crucial role for its applications. Although a higher optimal temperature was detected for the crude protease in the presence of Ca2+ (65 °C; Figure 2A), the thermal stability results (Figure 2B) indicate that temperatures equal to or higher than 60 °C might not be suitable for biocatalytic processes.
Kinetic and thermodynamic investigations of cell-wall degrading enzymes produced by Aureobasidium pullulans via induction with orange peels: application in lycopene extraction
Published in Preparative Biochemistry and Biotechnology, 2019
Adedeji Nelson Ademakinwa, Femi Kayode Agboola
Enzymes for industrial applications must display some measure of thermostability. Enzyme thermostability involves both kinetic and thermodynamic properties. Kinetically, the thermal denaturation of enzymes is described by first-order kinetics using the following equation:
Synthesis of high strength agar and its water plugging application in enhanced oil recovery
Published in Petroleum Science and Technology, 2023
Kaiping Tian, Wanfen Pu, Shuai Zhao
Thermostability analysis was performed by using TG 209 (NETZSCH, Germany) and DSC 214 (NETZSCH, Germany). TG test conditions: The test temperature range was 30–600 °C at the heating rate of 10 °C/min. DSC test conditions: The test temperature range was 40–550 °Cat a heating rate of 10 °C/min.