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  1. Article: pCold-assisted expression of a thermostable xylanase from

    Patel, Dharti Keyur / Dave, Gayatri

    3 Biotech

    2022  Volume 12, Issue 10, Page(s) 245

    Abstract: The biotechnological application of bacterial xylanases requires a high thermostability, a catalytically active state for a broad pH range. The : Supplementary information: The online version contains supplementary material available at 10.1007/s13205- ...

    Abstract The biotechnological application of bacterial xylanases requires a high thermostability, a catalytically active state for a broad pH range. The
    Supplementary information: The online version contains supplementary material available at 10.1007/s13205-022-03315-y.
    Language English
    Publishing date 2022-08-25
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2600522-0
    ISSN 2190-5738 ; 2190-572X
    ISSN (online) 2190-5738
    ISSN 2190-572X
    DOI 10.1007/s13205-022-03315-y
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  2. Article: pCold-assisted expression of a thermostable xylanase from Bacillus amyloliquefaciens: cloning, expression and characterization

    Patel, Dharti Keyur / Dave, Gayatri

    3 Biotech. 2022 Oct., v. 12, no. 10

    2022  

    Abstract: The biotechnological application of bacterial xylanases requires a high thermostability, a catalytically active state for a broad pH range. The Bacillus amyloliquefaciens (MTCC 1270) xynA gene was amplified and cloned into the pCold vector and was ... ...

    Abstract The biotechnological application of bacterial xylanases requires a high thermostability, a catalytically active state for a broad pH range. The Bacillus amyloliquefaciens (MTCC 1270) xynA gene was amplified and cloned into the pCold vector and was expressed in Escherichia coli to evaluate the expressed proteins’ thermostability. The pCold, compared to other similar vectors, has unique properties—including pH and temperature tolerance due to the presence of the cspA promoter. The recombinant xynA-pCold (rxynApC) showed the expression of xynA gene with a molecular weight of ~ 27 kDa, confirmed on SDS-PAGE. The rxynApC exhibits optimal activity at 70 °C and pH 8.0. The residual activity of the recombinant enzyme was 90% at pH 8.0. The thermal decomposition temperature (Td) value for the rxynApC enzyme was 93.33 °C obtained from the thermogravimetric analysis, indicating the potent stability of the cloned enzyme. The specific activity of native xylanase and rxynApC under optimal conditions was 32.35 and 105.5 U/mg, respectively. The structural model of the xynA gene was predicted using the in silico tool along with the active site (containing four important Tyr-166, Gly-7, Try-69 and Arg-112 amino acids). The predicted biophysical parameters of the in silico model were similar to the experimental results. The unique feature of the cspA promoter is that it gave a high expression of rxynApC enzyme having alkali and thermostable properties with high yield in surrogate host E. coli. Thus, the recombinant xynA gene can potentially be applied to different industrial needs by looking at its thermostability and enhanced enzyme activity.
    Keywords Bacillus amyloliquefaciens ; Escherichia coli ; active sites ; computer simulation ; enzyme activity ; genes ; models ; molecular weight ; pH ; polyacrylamide gel electrophoresis ; temperature ; thermal degradation ; thermal stability ; thermogravimetry ; xylanases
    Language English
    Dates of publication 2022-10
    Size p. 245.
    Publishing place Springer International Publishing
    Document type Article
    ZDB-ID 2600522-0
    ISSN 2190-5738 ; 2190-572X
    ISSN (online) 2190-5738
    ISSN 2190-572X
    DOI 10.1007/s13205-022-03315-y
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Linkers: A synergistic way for the synthesis of chimeric proteins.

    Patel, Dharti Keyur / Menon, Dhanya V / Patel, Darshan H / Dave, Gayatri

    Protein expression and purification

    2021  Volume 191, Page(s) 106012

    Abstract: In the cell, the protein domains are attached with the short oligopeptide, commonly known as linker peptide. Besides bridging, the linker assists in the domain-domain interaction and protein folding into the peculiar conformations. Linkers allow or ... ...

    Abstract In the cell, the protein domains are attached with the short oligopeptide, commonly known as linker peptide. Besides bridging, the linker assists in the domain-domain interaction and protein folding into the peculiar conformations. Linkers allow or control the movement of protein domains in the dynamic cellular environment. The recent advances in the recombinant DNA technology enable the construction of multiple gene constructs in an open reading frame. The express sequences can work in a cascade to cater for myriad functions. This trend has given momentum to incorporating bridge sequences (linker) that essentially separates the independent domains. According to the cellular need, the bridging partner can be spaced at a secure gap or requires attaching or interacting physically. The flexible or rigid linker can help to achieve such conformations in chimeric fusion proteins. The linker can improve solubility, proteolytic resistance and stability of such fusion proteins. Recently, linker aided protein switches and antibody-drug conjugates are gaining the attention of researchers worldwide. Here, we thoroughly reviewed the types of the linker, strategies for linker engineering and the composition of a linker.
    MeSH term(s) Protein Domains ; Protein Engineering ; Protein Folding ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics
    Chemical Substances Recombinant Fusion Proteins
    Language English
    Publishing date 2021-11-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1055455-5
    ISSN 1096-0279 ; 1046-5928
    ISSN (online) 1096-0279
    ISSN 1046-5928
    DOI 10.1016/j.pep.2021.106012
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