Solvent tolerant enzymes in extremophiles: Adaptations and applications

Kikani, Bhavtosh A.; Patel, Rajesh; Thumar, Jignasha T.; Bhatt, Hitarth B.; Rathore, Dalip Singh; Koladiya, Gopi A.; Singh, Satya Prakash

doi:10.1016/j.ijbiomac.2023.124051

Cited by 20 publications

(8 citation statements)

References 186 publications

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“…Extensively developed techniques based on artificial intelligence adopting machine learning are expected to help in the de novo design of enzymes potentially applied in therapy. , Nonaqueous enzymology seems to be of high interest in the context of the presented model, where the environment is treated as an important component conditioning the enzyme activity …”

Section: Discussionmentioning

confidence: 99%

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Hydrophobicity-Based Force Field In Enzymes

Roterman,

Konieczny,

Stapor

et al. 2024

ACS Omega

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The biocatalysis process takes place with the participation of enzymes, which, depending on the reaction carried out, require, apart from the appropriate arrangement of catalytic residues, an appropriate external force field. It is generated by the protein body. The relatively small size of the part directly involved in the process itself is supported by the presence of an often complex structure of the protein body, the purpose of which is to provide an appropriate local force field, eliminating the influence of water. Very often, the large size of the enzyme is an expression of the complex form of this field. In this paper, a comparative analysis of arbitrarily selected enzymes, representatives of different enzyme classes, was carried out, focusing on the measurement of the diversity of the force field provided by a given protein. This analysis was based on the fuzzy oil drop model (FOD) and its modified version (FOD-M), which takes into account the participation of nonaqueous external factors in shaping the structure and thus the force field within the protein. The degree and type of ordering of the hydrophobicity distribution in the protein molecule is the result of the influence of the environment but also the supplier of the local environment for a given process, including the catalysis process in particular. Determining the share of a nonaqueous environment is important due to the ubiquity of polar water, whose participation in processes with high specificity requires control. It can be assumed that some enzymes in their composition have a permanently built-in part, the role of which is reduced to that of a permanent chaperone. It provides a specific external force field needed for the process. The proposed model, generalized to other types of proteins, may also provide a form of recording the environment model for the simulation of the in silico protein folding process, taking into account the impact of its differentiation.

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Section: Discussionmentioning

confidence: 99%

“… 81 , 82 Nonaqueous enzymology seems to be of high interest in the context of the presented model, where the environment is treated as an important component conditioning the enzyme activity. 83 …”

Section: Discussionmentioning

confidence: 99%

Hydrophobicity-Based Force Field In Enzymes

Roterman,

Konieczny,

Stapor

et al. 2024

ACS Omega

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“…Peptide and ester synthesis reactions take place in the co-solvent system but at higher solvent concentration enzyme activity reduces it is due to the interplay of the solvents at the interface between enzymes and water molecules. Recently it has been observed that greener solvents like ionic liquid can also replace as reaction media for enzymatic bio-catalysis [ [6] , [7] , [8] ]. As a novel strategy, deep eutectic solvents (DESs) are emerging as viable substitutes for traditional organic solvents [ 9 ].…”

Section: Introductionmentioning

confidence: 99%

Production and characterization of an organic solvent activated protease from haloalkaliphilic bacterium Halobiforma sp. strain BNMIITR

Gupta,

Choudhury,

Navani

2024

Heliyon

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“…This is because catalysis in non-aqueous media offers several advantages, such as increased solubility of hydrophobic substrates in the reaction media, better substrate and product stability, and favoring synthesis over hydrolysis (Cao and Matsuda, 2016 ; Ramos-Martín et al, 2020 ). However, exposure to organic solvents and/or elevated temperature could pose challenges to enzyme activity and stability (Kumar et al, 2016 ; Kikani et al, 2023 ). Therefore, the use of organic solvent-tolerant thermostable lipases to catalyze reactions in non-aqueous media offers several biotechnological advantages (Ismail et al, 2021 ; Haryati et al, 2022 ; Kikani et al, 2023 ).…”

Section: Introductionmentioning

confidence: 99%

A thermostable organic solvent-tolerant lipase from Brevibacillus sp.: production and integrated downstream processing using an alcohol-salt-based aqueous two-phase system

Leykun,

Johansson,

Vetukuri

et al. 2023

Front. Microbiol.

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Lipases are used for the synthesis of different compounds in the chemical, pharmaceutical, and food industries. Most of the reactions are carried out in non-aqueous media and often at elevated temperature, requiring the use of organic solvent-tolerant thermostable lipases. However, most known lipases are not stable in the presence of organic solvents and at elevated temperature. In this study, an organic solvent-tolerant thermostable lipase was obtained from Brevibacillus sp. SHI-160, a moderate thermophile isolated from a hot spring in the East African Rift Valley. The enzyme was optimally active at 65°C and retained over 90% of its activity after 1 h of incubation at 70°C. High lipase activity was measured in the pH range of 6.5 to 9.0 with an optimum pH of 8.5. The enzyme was stable in the presence of both polar and non-polar organic solvents. The stability of the enzyme in the presence of polar organic solvents allowed the development of an efficient downstream processing using an alcohol-salt-based aqueous two-phase system (ATPS). Thus, in the presence of 2% salt, over 98% of the enzyme partitioned to the alcohol phase. The ATPS-recovered enzyme was directly immobilized on a solid support through adsorption and successfully used to catalyze a transesterification reaction between paranitrophenyl palmitate and short-chain alcohols in non-aqueous media. This shows the potential of lipase SHI-160 to catalyze reactions in non-aqueous media for the synthesis of valuable compounds. The integrated approach developed for enzyme production and cheap and efficient downstream processing using ATPS could allow a significant reduction in enzyme production costs. The results also show the potential of extreme environments in the East African Rift Valley as sources of valuable microbial genetic resources for the isolation of novel lipases and other industrially important enzymes.

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Solvent tolerant enzymes in extremophiles: Adaptations and applications

Cited by 20 publications

References 186 publications

Hydrophobicity-Based Force Field In Enzymes

Hydrophobicity-Based Force Field In Enzymes

Production and characterization of an organic solvent activated protease from haloalkaliphilic bacterium Halobiforma sp. strain BNMIITR

A thermostable organic solvent-tolerant lipase from Brevibacillus sp.: production and integrated downstream processing using an alcohol-salt-based aqueous two-phase system

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