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  1. Article ; Online: Production, characterization, and immobilization of partially purified surfactant-detergent and alkali-thermostable protease from newly isolated Aeromonas caviae.

    Datta, Sumitra / Menon, Gopalakrishnan / Varughese, Bincy

    Preparative biochemistry & biotechnology

    2017  Volume 47, Issue 4, Page(s) 349–356

    Abstract: Proteolytic Aeromonas caviae P-1-1 growing at wide-ranging pH (7.0-11.0) and moderate salinity (0-5% NaCl) was isolated from cattle shed of Thanjavur, India. It produced lipase, gelatinase, and polyhydroxybutyrate. Different culture conditions, ... ...

    Abstract Proteolytic Aeromonas caviae P-1-1 growing at wide-ranging pH (7.0-11.0) and moderate salinity (0-5% NaCl) was isolated from cattle shed of Thanjavur, India. It produced lipase, gelatinase, and polyhydroxybutyrate. Different culture conditions, incubation time, carbon and nitrogen sources, vitamins, amino acids, surfactants, and metal ions for optimal growth and protease production of P-1-1 were examined. Maximum protease (0.128 U/mL) production was achieved with 1% fructose, 1% yeast extract, 0.1% ammonium sulfate, 3% NaCl, 0.1% CaCl
    MeSH term(s) Aeromonas caviae/chemistry ; Aeromonas caviae/enzymology ; Aeromonas caviae/growth & development ; Aeromonas caviae/metabolism ; Alkalies/chemistry ; Animals ; Cattle/microbiology ; Cell Culture Techniques ; Enzyme Stability ; Enzymes, Immobilized/chemistry ; Enzymes, Immobilized/isolation & purification ; Enzymes, Immobilized/metabolism ; Hydrogen-Ion Concentration ; Industrial Microbiology ; Metals/chemistry ; Peptide Hydrolases/chemistry ; Peptide Hydrolases/isolation & purification ; Peptide Hydrolases/metabolism ; Salinity ; Sodium Chloride/chemistry ; Surface-Active Agents/chemistry
    Chemical Substances Alkalies ; Enzymes, Immobilized ; Metals ; Surface-Active Agents ; Sodium Chloride (451W47IQ8X) ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2017-04-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 1322522-4
    ISSN 1532-2297 ; 1082-6068
    ISSN (online) 1532-2297
    ISSN 1082-6068
    DOI 10.1080/10826068.2016.1244688
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Xenon-inhibition of the MscL mechano-sensitive channel and the CopB copper ATPase under different conditions suggests direct effects on these proteins.

    Petrov, Evgeny / Menon, Gopalakrishnan / Rohde, Paul R / Battle, Andrew R / Martinac, Boris / Solioz, Marc

    PloS one

    2018  Volume 13, Issue 6, Page(s) e0198110

    Abstract: Xenon is frequently used as a general anesthetic in humans, but the mechanism remains an issue of debate. While for some membrane proteins, a direct interaction of xenon with the protein has been shown to be the inhibitory mechanism, other membrane ... ...

    Abstract Xenon is frequently used as a general anesthetic in humans, but the mechanism remains an issue of debate. While for some membrane proteins, a direct interaction of xenon with the protein has been shown to be the inhibitory mechanism, other membrane protein functions could be affected by changes of membrane properties due to partitioning of the gas into the lipid bilayer. Here, the effect of xenon on a mechanosensitive ion channel and a copper ion-translocating ATPase was compared under different conditions. Xenon inhibited spontaneous gating of the Escherichia coli mechano-sensitive mutant channel MscL-G22E, as shown by patch-clamp recording techniques. Under high hydrostatic pressure, MscL-inhibition was reversed. Similarly, the activity of the Enterococcus hirae CopB copper ATPase, reconstituted into proteoliposomes, was inhibited by xenon. However, the CopB ATPase activity was also inhibited by xenon when CopB was in a solubilized state. These findings suggest that xenon acts by directly interacting with these proteins, rather than via indirect effects by altering membrane properties. Also, inhibition of copper transport may be a novel effect of xenon that contributes to anesthesia.
    MeSH term(s) Adenosine Triphosphatases/antagonists & inhibitors ; Cation Transport Proteins/antagonists & inhibitors ; Escherichia coli Proteins/antagonists & inhibitors ; Ion Channel Gating/drug effects ; Ion Channels/antagonists & inhibitors ; Ion Channels/drug effects ; Ion Channels/metabolism ; Mechanotransduction, Cellular/drug effects ; Patch-Clamp Techniques ; Xenon/pharmacology
    Chemical Substances Cation Transport Proteins ; Escherichia coli Proteins ; Ion Channels ; MscL protein, E coli ; Xenon (3H3U766W84) ; Adenosine Triphosphatases (EC 3.6.1.-) ; CopB ATPase, Enterococcus hirae (EC 3.6.1.-)
    Language English
    Publishing date 2018-06-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0198110
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Isolation, Purification, and Characterization of Haloalkaline Xylanase from a Marine Bacillus pumilus Strain, GESF-1

    Menon, Gopalakrishnan, Council of Scientific and Industrial Research (CSIR) Gijubhai Badheka Marg, Bhavnagar, India / Mody, Kalpana, Council of Scientific and Industrial Research (CSIR) Gijubhai Badheka Marg, Bhavnagar, India / Keshri, Jitendra, Council of Scientific and Industrial Research (CSIR) Gijubhai Badheka Marg, Bhavnagar, India / Jha, Bhavanath, Council of Scientific and Industrial Research (CSIR) Gijubhai Badheka Marg, Bhavnagar, India

    Biotechnology and Bioprocess Engineering

    (Nov 2010)  Volume v. 15, Issue (6), Page(s) p. 998–1005

    Abstract: A haloalkalitolerant xylanase-producing Bacillus pumilus strain, GESF1 was isolated from an experimental salt farm of CSMCRI. Birch wood xylan and xylose induced maximum xylanase production with considerable activity seen in wheat straw and no activity ... ...

    Abstract A haloalkalitolerant xylanase-producing Bacillus pumilus strain, GESF1 was isolated from an experimental salt farm of CSMCRI. Birch wood xylan and xylose induced maximum xylanase production with considerable activity seen in wheat straw and no activity at all with caboxymethyl cellulose (CMC). A three step purification yielded 21.21-fold purification with a specific activity of 112.42 U/mg protein (unit expressed as μmole of xylose released per min). Xylanase produced showed an optimum activity at pH 8.0, with approximately 50 and 30% relative activity at a pH 6.0 and 10.0, respectively. The temperature optimum was 40℃ and kinetic properties such as K∧m and V∧max were 5.3 mg/mL and 0.42 μmol/min/mL (6593.4 μmol/min/mg protein). Xylanase activity (160 ~ 120%) was considerably enhanced in 2.5 to 7.5% NaCl with 87 and 73% retention of activity in 10 and 15% of NaCl. Enzyme activity was enhanced by Ca²+, Mn²+, Mg²+, and Na+ but strongly inhibited by heavy metals such as Hg²+, Fe³+, Cu²+, Cd²+, and Zn²+. Organic reagents such as β-Mercaptoethanol enhanced xylanase activity whereas EDTA strongly inhibited its activity. Xylanase, purified from the Bacillus pumilus strain, GESF1 could have potential biotechnological applications.
    Keywords XYLOSE ; XYLOSE ; XILOSA
    Language English
    Document type Article
    ISSN 1226-8372
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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