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  1. AU="Sharmili Jagtap"
  2. AU="Colín-Martínez, Tania"

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  1. Artikel: Scale-up and inhibitory studies on productivity of lipase from Acinetobacter radioresistens PR8

    Gupta, Krishna Kant / Anshul Nigam / Ramadas Krishna / Sharmili Jagtap

    The Society for Biotechnology, Japan Journal of bioscience and bioengineering. 2017 Aug., v. 124, no. 2

    2017  

    Abstract: Acinetobacter radioresistens PR8 produces extracellular lipase depending upon growth media. In present work we not only screened the nutrient sources but also investigated the causes for variation in productivity. The nutrient sources investigated are, ... ...

    Abstract Acinetobacter radioresistens PR8 produces extracellular lipase depending upon growth media. In present work we not only screened the nutrient sources but also investigated the causes for variation in productivity. The nutrient sources investigated are, groundnut oil, groundnut cake and fresh groundnut. Lower lipase productivity was observed on fresh ground nut in contrast to groundnut oil and groundnut cake. The lipase productivity was examined in the batch and parameters monitored were bacterial growth, enzyme activity, pH, lipids and protein concentration. The aflatoxin B1 and oxalic acid present in fresh groundnut were found to be responsible for lower lipase productivity. The interaction studies of oxalic acid and purified lipase was confirmed with CD spectra analysis, isothermal titration calorimetry studies and fluorescence quenching. Therefore, the importance of economical cheap groundnut cake with no aflatoxin B1 and oxalates are proposed to be used for optimum lipase production.
    Schlagwörter Acinetobacter radioresistens ; aflatoxin B1 ; carboxylic ester hydrolases ; culture media ; enzyme activity ; fluorescence ; lipids ; microbial growth ; oxalates ; oxalic acid ; peanut cake ; peanut oil ; peanuts ; pH
    Sprache Englisch
    Erscheinungsverlauf 2017-08
    Umfang p. 150-155.
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    ZDB-ID 1465387-4
    ISSN 1347-4421 ; 1389-1723
    ISSN (online) 1347-4421
    ISSN 1389-1723
    DOI 10.1016/j.jbiosc.2017.03.005
    Datenquelle NAL Katalog (AGRICOLA)

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  2. Artikel: Purification, biochemical characterization and structural modelling of alkali-stable β-1,4-xylan xylanohydrolase from Aspergillus fumigatus R1 isolated from soil

    Deshmukh, Rehan Ahmed / Madan Kumar Mandal / Sharmili Jagtap / Suraj Kumar Mandal

    BMC biotechnology. 2016 Dec., v. 16, no. 1

    2016  

    Abstract: BACKGROUND: Aspergillus fumigatus R1 produced xylanase under submerged fermentation which degrades the complex hemicelluloses contained in agricultural substrates. Xylanases have gained considerable attention because of their tremendous applications in ... ...

    Abstract BACKGROUND: Aspergillus fumigatus R1 produced xylanase under submerged fermentation which degrades the complex hemicelluloses contained in agricultural substrates. Xylanases have gained considerable attention because of their tremendous applications in industries. The purpose of our study was to purify xylanase and study its biochemical properties. We have predicted the secondary structure of purified xylanase and evaluated its active site residues and substrate binding sites based on the global and local structural similarity. RESULTS: Various microorganisms were isolated from Puducherry soil and screened by Congo-red test. The best isolate was identified to be Aspergillus fumigatus R1. The production kinetics showed the highest xylanase production (208 IU/ml) by this organism in 96 h using 1 % rice bran as the only carbon source. The purification of extracellular xylanase was carried out by fractional ammonium sulphate precipitation (30–55 %), followed by extensive dialysis and Bio-Gel P-60 Gel-filtration chromatography. The enzyme was purified 58.10 folds with a specific activity of 38196.22 IU/mg. The biochemical characterization of the pure enzyme was carried out for its optimum pH and temperature (5.0 and 500C), pH and temperature stability, molecular mass (Mr) (24.5 kDa) and pI (6.29). The complete sequence of protein was obtained by mass spectrometry analysis. Apparent Km and Vmax values of the xylanase for birchwood xylan were 11.66 mg/ml and 87.6 μmol min−1 mg−1 respectively. CONCLUSION: Purified xylanase was analyzed by mass-spectrometry which revealed 2 unique peptides. Xylanase under current study showed significant production using agricultural residues and a broad range of pH stability in the alkaline region. Xylanase produced by Aspergillus fumigatus R1 could serve as the enzyme of choice in industries.
    Schlagwörter active sites ; agricultural wastes ; ammonium sulfate ; Aspergillus fumigatus ; binding sites ; carbon ; dialysis ; gel chromatography ; industry ; mass spectrometry ; microorganisms ; models ; molecular weight ; peptides ; pH ; rice bran ; soil ; submerged fermentation ; temperature ; xylan ; xylanases
    Sprache Englisch
    Erscheinungsverlauf 2016-12
    Umfang p. 11.
    Erscheinungsort BioMed Central
    Dokumenttyp Artikel
    ISSN 1472-6750
    DOI 10.1186/s12896-016-0242-4
    Datenquelle NAL Katalog (AGRICOLA)

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