ArticleHeliyon2020
Contributions of protein microenvironment in tannase industrial applicability: An in-silico comparative study of pathogenic and non-pathogenic bacterial tannase.
Article in Heliyon, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 21 citations in OpenAlex.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tannase is an inducible industrially important enzyme, produced by several microorganisms. A large number of bacteria have reported as tannase producers; however, some of them are pathogenic in nature. Therefore, it is quite uncertain whether the application of these tannase enzymes from such pathogenic bacteria is suitable for industries and human welfare. Till date, there is no clear evidence regarding which group of bacteria (non-pathogenic or pathogenic) is better suited for their application in the edge of industries with particular reference to the food industry. The present study is following the findings of the above queries. In this study, a large number of tannase protein sequences have been retrieved from the databases, including both non-pathogenic and pathogenic bacterial species. Physiochemical and evolutionary properties of those sequences have been evaluated. Results have shown that non-pathogenic bacterial tannase possesses a high number of acidic and basic amino acid residues as compared to their pathogenic counterparts. The acidic and basic amino acid residues of tannase provide unique microenvironment to it. In the other hand, the numbers of disorder forming residues are higher in tannase sequences of pathogenic bacteria. The study of tannase microenvironment leads in the formation of salt bridges, which finally favoring the stability and proper functioning of tannase. This is the first report of such observation on tannase enzyme using
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