Genome Sequence of the Multiple-Protease-Producing Strain Geobacillus thermoleovorans N7
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            a Thermophilic Bacterium Isolated from Paniphala Hot Spring, West Bengal, India

Bose, Sucharita; Mukherjee, Trinetra; Sen, Urmimala; Roy, Chayan; Rameez, Moidu Jameela; Ghosh, Wriddhiman; Mukhopadhyay, Subhra Kanti

doi:10.1128/genomea.01202-16

Cited by 7 publications

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“…This difference may be explained by the potential stabilization of the enzyme with the used experimental set up such as buffer and their pH values. Besides, it was reported that the TPP is not only reflecting the temperature-dependent unfolding, but also an (Mohammadi et al, 2011) 99.66 65 60 QDY72590.1 Acetyl esterase GTNG_0744 (Bose et al, 2016) 90.08 60 59 irreversible thermal aggregation ( Jarzab et al, 2020;Seashore-Ludlow et al, 2020) and it may not be directly comparable with the biophysical methods. Collectively, it can be suggested that taking account of the plateau and R 2 values, the quality of the melting curve can give a useful prediction about the temperature at which the maximum enzyme activity would occur.…”

Section: T M Values Of Industrially Relevant Enzymesmentioning

confidence: 99%

Thermal Proteome Profiling and Meltome Analysis of a Thermophilic Bacterial Strain,Geobacillus thermoleovoransARTRW1: Toward Industrial Applications

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et al. 2020

OMICS: A Journal of Integrative Biology

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Thermophilic microorganisms that thrive in extreme environments are of great importance because they express heat-resistant enzymes with the potential to serve as biocatalysts in industrial applications. Thermal proteome profiling (TPP) is a multiplexed quantitative mass spectrometry method for analyses of structural information and melting behavior of thousands of proteins, simultaneously determining the thermal denaturation profiles of each protein. We report, in this study, TPP applied to a thermophilic bacterial proteome, a recently isolated strain of Geobacillus thermoleovorans named as ARTRW1. The proteome was investigated in terms of thermostable enzymes that are relevant to industrial applications. In this study, we present the thermostability profiles of its 868 proteins. The majority of G. thermoleovorans proteome was observed to melt between 62.5°C and 72°C, with melting point (T m) mean value of 68.1°C-6.6°C. Unfolding characteristics of several enzymes, including amylase, protease, and lipase, were demonstrated which are highly informative in terms of their applicability to specific industrial processes. A significant correlation was observed between protein melting temperature and the structural features such as molecular weight and abundance, whereas correlations were modest or weak in relation to the a-helix structure percentages. Taken together, we demonstrated a system-wide melting profile analysis of a thermal proteome and listed proteins with elevated T m values that are highly promising for applications in medicine, food engineering, and cosmetics in particular. The extracted T m values were found similar to those obtained by biophysical methods applied to purified proteins. TPP analysis has significant industrial and biomedical potentials to accelerate thermophilic enzyme research and innovation.

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Section: T M Values Of Industrially Relevant Enzymesmentioning

confidence: 99%