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  1. Article ; Online: The S-S bridge mutation between the A2 and A4 loops (T416C-I432C) of Cel7A of

    Dodda, Subba Reddy / Hossain, Musaddique / Mondal, Sudipa / Das, Shalini / Khator Jain, Sneha / Aikat, Kaustav / Mukhopadhyay, Sudit S

    Applied and environmental microbiology

    2024  Volume 90, Issue 4, Page(s) e0232923

    Abstract: Disulfide bonds are important for maintaining the structural conformation and stability of the protein. The introduction of the disulfide bond is a promising strategy to increase the thermostability of the protein. In this report, cysteine residues are ... ...

    Abstract Disulfide bonds are important for maintaining the structural conformation and stability of the protein. The introduction of the disulfide bond is a promising strategy to increase the thermostability of the protein. In this report, cysteine residues are introduced to form disulfide bonds in the Glycoside Hydrolase family GH 7 cellobiohydrolase (GH7 CBHs) or Cel7A of
    MeSH term(s) Aspergillus fumigatus/genetics ; Aspergillus fumigatus/metabolism ; Cellulose 1,4-beta-Cellobiosidase/genetics ; Cellulose 1,4-beta-Cellobiosidase/metabolism ; Cysteine ; Mutation ; Disulfides ; Enzyme Stability
    Chemical Substances Cellulose 1,4-beta-Cellobiosidase (EC 3.2.1.91) ; Cysteine (K848JZ4886) ; Disulfides
    Language English
    Publishing date 2024-03-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/aem.02329-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Computational approach for identification, characterization, three-dimensional structure modelling and machine learning-based thermostability prediction of xylanases from the genome of Aspergillus fumigatus.

    Dodda, Subba Reddy / Hossain, Musaddique / Kapoor, Bishwajit Singh / Dasgupta, Shreya / B, Venkata P Reddy / Aikat, Kaustav / Mukhopadhyay, Sudit S

    Computational biology and chemistry

    2021  Volume 91, Page(s) 107451

    Abstract: Identification of thermostable and alkaline xylanases from different fungal and bacterial species have gained an interest for the researchers because of its biotechnological relevance in many industries, such as pulp, paper, and bioethanol. In this study, ...

    Abstract Identification of thermostable and alkaline xylanases from different fungal and bacterial species have gained an interest for the researchers because of its biotechnological relevance in many industries, such as pulp, paper, and bioethanol. In this study, we have identified and characterized xylanases from the genome of the thermophilic fungus of Aspergillus fumigatus by in silico analysis. Genome data mining revealed that the A fumigatus genome has six xylanase genes that belong to GH10, GH11, GH43 glycoside hydrolase families. In general, most of the bacterial and fungal GH11 xylanases are alkaline, and GH10 xylanases are acidic; however, we found that one identified xylanase from A fumigatus that belongs to the GH10 family is alkaline while the rest are acidic. Moreover, physicochemical properties also stated that most of the xylanases identified have lower molecular weight except one that belongs to the GH43 family. Structure prediction by homology modelling gave optimized structures of the xylanases. It suggests that GH10 family structure models adapt (β∕α) 8 barrel type, GH11 homology models adapt β-jelly type, and the GH43 family has a fivefold β-propeller type structure. Molecular docking of identified xylanases with xylan revealed that GH11 xylanases have strong interaction (-9.6 kcal/mol) with xylan than the GH10 (-8.5 and -9.3 kcal/mol) and GH43 (-8.8 kcal/mol). We used the machine learning approach based TAXyl server to predict the thermostability of the xylanases. It revealed that two GH10 xylanases and one GH11 xylanase are thermo-active up to 75ᵒC. We have explored the physiochemical properties responsible for maintaining thermostability for bacterial and fungal GH10 and GH11 xylanases by comparing crystal structures. All the analyzed parameters specified that GH10 xylanases from both the fungi and bacteria are more thermostable due to higher hydrogen bonds, salt bridges, and helical content.
    Language English
    Publishing date 2021-02-06
    Publishing country England
    Document type Journal Article
    ISSN 1476-928X
    ISSN (online) 1476-928X
    DOI 10.1016/j.compbiolchem.2021.107451
    Database MEDical Literature Analysis and Retrieval System OnLINE

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