Biocatalysis Through Thermostable Lipases: Adding Flavor to Chemistry

Sharma, Rohit K.; Thakur, Vishal; Sharma, Monika; Birkeland, Nils-Kåre

doi:10.1007/978-94-007-5899-5_34

Cited by 10 publications

(5 citation statements)

References 140 publications

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“…Hot springs have been recognized as an important source of beneficial thermophiles belonging to the Bacteria and Archaea domains, which can produce valuable biomolecules and thermozymes. Owing to their thermostability and ability to withstand the high-temperature conditions often utilized in industrial practices, thermozymes have several industrial applications [ 26 , 27 ]. The use of thermophiles and their products in harsh industrial conditions at elevated temperatures has several advantages, including reduced risk of microbial contamination, lower viscosity of the reaction medium and increased mass transfer, diffusion coefficient, and solubility of substrates [ 2 , 4 , 5 ].…”

Section: Introductionmentioning

confidence: 99%

Microbial Diversity of Terrestrial Geothermal Springs in Armenia and Nagorno-Karabakh: A Review

et al. 2021

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The microbial diversity of high-altitude geothermal springs has been recently assessed to explore their biotechnological potential. However, little is known regarding the microbiota of similar ecosystems located on the Armenian Highland. This review summarizes the known information on the microbiota of nine high-altitude mineralized geothermal springs (temperature range 25.8–70 °C and pH range 6.0–7.5) in Armenia and Nagorno-Karabakh. All these geothermal springs are at altitudes ranging from 960–2090 m above sea level and are located on the Alpide (Alpine–Himalayan) orogenic belt, a seismically active region. A mixed-cation mixed-anion composition, with total mineralization of 0.5 mg/L, has been identified for these thermal springs. The taxonomic diversity of hot spring microbiomes has been examined using culture-independent approaches, including denaturing gradient gel electrophoresis (DGGE), 16S rRNA gene library construction, 454 pyrosequencing, and Illumina HiSeq. The bacterial phyla Proteobacteria, Bacteroidetes, Cyanobacteria, and Firmicutes are the predominant life forms in the studied springs. Archaea mainly include the phyla Euryarchaeota, Crenarchaeota, and Thaumarchaeota, and comprise less than 1% of the prokaryotic community. Comparison of microbial diversity in springs from Karvachar with that described for other terrestrial hot springs revealed that Proteobacteria, Bacteroidetes, Actinobacteria, and Deinococcus–Thermus are the common bacterial groups in terrestrial hot springs. Contemporaneously, specific bacterial and archaeal taxa were observed in different springs. Evaluation of the carbon, sulfur, and nitrogen metabolism in these hot spring communities has revealed diversity in terms of metabolic activity. Temperature seems to be an important factor in shaping the microbial communities of these springs. Overall, the diversity and richness of the microbiota are negatively affected by increasing temperature. Other abiotic factors, including pH, mineralization, and geological history, also impact the structure and function of the microbial community. More than 130 bacterial and archaeal strains (Bacillus, Geobacillus, Parageobacillus, Anoxybacillus, Paenibacillus, Brevibacillus Aeribacillus, Ureibacillus, Thermoactinomyces, Sporosarcina, Thermus, Rhodobacter, Thiospirillum, Thiocapsa, Rhodopseudomonas, Methylocaldum, Desulfomicrobium, Desulfovibrio, Treponema, Arcobacter, Nitropspira, and Methanoculleus) have been reported, some of which may be representative of novel species (sharing 91–97% sequence identity with their closest matches in GenBank) and producers of thermozymes and biomolecules with potential biotechnological applications. Whole-genome shotgun sequencing of T. scotoductus K1, as well as of the potentially new Treponema sp. J25 and Anoxybacillus sp. K1, were performed. Most of the phyla identified by 16S rRNA were also identified using metagenomic approaches. Detailed characterization of thermophilic isolates indicate the potential of the studied springs as a source of biotechnologically valuable microbes and biomolecules.

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Section: Introductionmentioning

confidence: 99%

Microbial Diversity of Terrestrial Geothermal Springs in Armenia and Nagorno-Karabakh: A Review

et al. 2021

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“…Bacteria are considered as their most reliable source that can express them even in coal mines (Ali et al 2015) or geothermal springs (Shahinyan et al 2017). Several isoforms of lipases have been isolated from bacterial cultures (Verma and Sharma 2014) and found applications in food, dairy, and detergent industries (Gupta et al 2004;Sharma et al 2013). Lipases largely differ by biochemical parameters.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a novel lipase from Pseudomonas aeruginosa

Berdiev¹,

Ziyavitdinov²,

Asrorov³

et al. 2019

Nova Biotechnologica Et Chimica

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Lipases cleaving oils into fatty acids and glycerol are of great interest for the use in increasing the efficiency of fuels. In this work, a novel lipase from Pseudomonas aeruginosa, P. aeruginosa A12, was isolated by ion-exchange and hydrophobic chromatography. The purity of lipase was shown by electrophoresis and its molecular weight was estimated to be ~ 31.6 kDa. The whole amino acid sequence was analyzed by an LC-MS/MS method. Temperature- and pH-dependent optimum of the enzyme compiled 30 °C and 7.5, respectively. The obtained enzyme exhibited 79 % similarity of amino acid sequence to a lipase isolated from the same strain of P. aeruginosa. Thus, the novel lipase was determined to belong to I.1 subfamily of bacterial true lipases. Three dimensional structure of the isolated lipase isoform was modeled based on obtained sequences. Amino acids forming the catalytic domain were shown in the model. Lid domain is suggested to be in the open conformation. These results provide a potential alternative for enzymatic digestion of fuel oils and serve for the development of fundamental knowledge of lipase activity.

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“…Many hydrolase enzymes including proteases, lipases, esterases and cellulases are already used commercially in industrial biocatalysis as documented in recent review chapters [ 56 , 63 , 66 ]. However, there is still an increasing need for the new enzymes to compliment the existing ‘Tool Box’ and to make these commercially available.…”

Section: Introductionmentioning

confidence: 99%

Improving the ‘tool box’ for robust industrial enzymes

Littlechild

2017

Journal of Industrial Microbiology and Biotechnology

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The speed of sequencing of microbial genomes and metagenomes is providing an ever increasing resource for the identification of new robust biocatalysts with industrial applications for many different aspects of industrial biotechnology. Using ‘natures catalysts’ provides a sustainable approach to chemical synthesis of fine chemicals, general chemicals such as surfactants and new consumer-based materials such as biodegradable plastics. This provides a sustainable and ‘green chemistry’ route to chemical synthesis which generates no toxic waste and is environmentally friendly. In addition, enzymes can play important roles in other applications such as carbon dioxide capture, breakdown of food and other waste streams to provide a route to the concept of a ‘circular economy’ where nothing is wasted. The use of improved bioinformatic approaches and the development of new rapid enzyme activity screening methodology can provide an endless resource for new robust industrial biocatalysts.This mini-review will discuss several recent case studies where industrial enzymes of ‘high priority’ have been identified and characterised. It will highlight specific hydrolase enzymes and recent case studies which have been carried out within our group in Exeter.

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Biocatalysis Through Thermostable Lipases: Adding Flavor to Chemistry

Cited by 10 publications

References 140 publications

Microbial Diversity of Terrestrial Geothermal Springs in Armenia and Nagorno-Karabakh: A Review

Microbial Diversity of Terrestrial Geothermal Springs in Armenia and Nagorno-Karabakh: A Review

Characterization of a novel lipase from Pseudomonas aeruginosa

Improving the ‘tool box’ for robust industrial enzymes

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