Mechanisms of Thermal Stability Adopted by Thermophilic Proteins and Their Use in White Biotechnology

Littlechild, Jennifer A.; Novak, Halina R.; James, Paul; Sayer, C.

doi:10.1007/978-94-007-5899-5_19

Cited by 13 publications

(11 citation statements)

References 129 publications

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“…This property makes it quite attractive for applications at elevated temperatures. Among the lipases which have their temperature optimum at 50°C, Aspergillus terreus lipase is stable at 60°C for more than 12 h [20].…”

Section: Enzymatic Propertiesmentioning

confidence: 99%

Purification and Characterization of Active Aggregates of an Organic Solvent Tolerant Lipase from Marinobacter sp. EMB5

Hemamalini¹,

Sk²

2018

Insights Enzyme Res

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Background: Marinobacter is a halophilic bacterial genus and a bio-geochemically important group in sea water, is generally associated with the bioremediation of hydrocarbon-rich effluents released into the salt-rich environment by various anthropogenic activities. It is a well-known lipase producer-the NCBI Protein database shows nearly 520 Marinobacter lipases. In this context, its lipase and esterase are considered important. However, their enzymatic properties in purified form have been scantily studied. Since hydrocarbons are acted upon on solvent water interface, the stability and catalytic behavior of Marinobacter lipase in non-aqueous media needs to be more specifically investigated.Aim: Marinobacter sp. EMB5 was isolated from Kozhikode, Kerala, India. It was found to be potent lipase producer. The aim of the present work was to obtain a purified preparation and undertake its detailed characterization with respect to above aspects. Work:The crude Marinobacter sp. lipase was purified by Sephacryl S200 gel filtration chromatography. The lipase eluted as a single activity peak in void volume and had a very high molecular mass. Aggregation has not been reported in case of Marinobacter lipase, so far, although it is known in other lipases. The aggregated lipase was mixed with 2-propanol (70%, v/v) and disaggregated lipase was obtained as a single activity peak in Sephacryl S200 gel filtration chromatography corresponding to 82 kDa molecular mass. This monomeric species was less active than aggregated purified preparation. Hence, further characterization and studies were carried out on purified active aggregate lipase. It was stable in a wide range of organic solvents at high concentration up to 24 h. The organic solvent stability was further investigated by Far UV CD spectroscopy and fluorescence spectroscopy. Conclusion:Due to the fact that Marinobacter sp. EMB5 lipase remained stable in organic solvents for prolonged incubation periods, it has potential to be used in industrial organic synthesis.

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Section: Enzymatic Propertiesmentioning

confidence: 99%

Purification and Characterization of Active Aggregates of an Organic Solvent Tolerant Lipase from Marinobacter sp. EMB5

Hemamalini¹,

Sk²

2018

Insights Enzyme Res

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“…Many thermophilic enzymes can be cloned and overexpressed in a soluble form using a mesophilic host ( Escherichia coli ) and can be easily purified from the cell extract by a straight forward heat treatment which precipitates most of the mesophilic proteins. The features responsible for the increased thermophilicity can be identified by studying the biochemical and structural features of a range of purified thermophilic proteins [ 10 ]. These include an increase in ionic interactions and often large ionic networks are observed within the protein and at the subunit interfaces.…”

Section: Introductionmentioning

confidence: 99%

Archaeal Enzymes and Applications in Industrial Biocatalysts

Littlechild¹

2015

Archaea

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Archaeal enzymes are playing an important role in industrial biotechnology. Many representatives of organisms living in “extreme” conditions, the so-called Extremophiles, belong to the archaeal kingdom of life. This paper will review studies carried by the Exeter group and others regarding archaeal enzymes that have important applications in commercial biocatalysis. Some of these biocatalysts are already being used in large scale industrial processes for the production of optically pure drug intermediates and amino acids and their analogues. Other enzymes have been characterised at laboratory scale regarding their substrate specificity and properties for potential industrial application. The increasing availability of DNA sequences from new archaeal species and metagenomes will provide a continuing resource to identify new enzymes of commercial interest using both bioinformatics and screening approaches.

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“…A number of adaptations have been observed experimentally and reported to contribute towards the increased thermal stability of major proteins from thermophilic and hyperthermophilic organisms. These adaptations primarily include an increase in ionic interactions; increased hydrophobicity; increased packing of additional secondary structure and C‐terminal extensions to fill internal cavities; introduction of disulfide bonds into cytoplasmic proteins; capping of the ends of α‐helices; shortening of surface loops; increases or decreases of some amino acids; and the stabilization of loops via interaction with metal ions . Usually a combination of these adaptations is used to achieve resistance to thermal denaturation.…”

Section: Resultsmentioning

confidence: 99%

Characterization of a thermostable glycoside hydrolase (CMbg0408) from the hyperthermophilic archaeon Caldivirga maquilingensisIC‐167

et al. 2016

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Mechanisms of Thermal Stability Adopted by Thermophilic Proteins and Their Use in White Biotechnology

Cited by 13 publications

References 129 publications

Purification and Characterization of Active Aggregates of an Organic Solvent Tolerant Lipase from Marinobacter sp. EMB5

Purification and Characterization of Active Aggregates of an Organic Solvent Tolerant Lipase from Marinobacter sp. EMB5

Archaeal Enzymes and Applications in Industrial Biocatalysts

Characterization of a thermostable glycoside hydrolase (CMbg0408) from the hyperthermophilic archaeon Caldivirga maquilingensisIC‐167

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