Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/298382
Title: Identification and Characterization of Plant Bioactive Peptides as Potential Biopesticides
Researcher: Waghmare Supriya Balaji
Guide(s): Kamble L H
Keywords: Biotechnology and Applied Microbiology
Life Sciences
Microbiology
University: Swami Ramanand Teerth Marathwada University
Completed Date: 2019
Abstract: ABSTRACT newlineTotal 128 samples were screened for inhibitory activity in three concentrations i.e. equal, low and high (E:I ratio of 1:1; 1:2 and 2:1) and those which are capable of inhibiting even at lower concentrations were chosen for further studies. Three different concentrations were premixed with trypsin and loaded onto the gel, after few minutes of visual observation film was washed. X-ray film. Dot blot assay reveals Citrullus colocynthis, Ipomoea hederacea, Dryptes roxburghii, Cassia absus Showed inhibition in all three concentrations whereas Lepidium iberis, Piper nigrum, Pimpinella anisum showed inhibition at 1:3 concentrations. Spodoptera gut proteases (SGP) when pre-incubated with different inhibitors showed that Piper cubeba and Mucuna pruriens possess high inhibitory activity against the larval enzymes i.e. 56.84% and 56.59%. Pimpinella anisum, Citrullus colocynthis, Juniperus communis, Piper cubeba, Apium leptophyllum, Cassia absus Linn. Lowest activity was shown by Ipomoea hederacea Jacq. and Dryptes roxburghii. newlineCassia absus contain proteinacious-protease inhibitors showing inhibitions with SGP. Preliminary results suggest that the trypsin inhibitor was quite stable to heat for 30 minute. The optimum pH for the inhibitory activity is pH 7.7 indicates presence of Kunitz inhibitor type. The highest trypsin inhibitory activity was found at protein precipitated around 20% ammonium sulphate concentration. Gelatin embedded native PAGE of purified TI incubated independently with trypsin showed that the seeds contain multiple forms of TI. The molecular weights estimated of the three isoforms newlineof TI as determined by SDS-PAGE were ~30.3 kDa, ~19.6 kDA. and ~17.8kDa, 70 ug of partially purified protein causes 100% of trypsin inhibition. Thermal stability of C. absus inhibitor was assessed to check whether it can with stand high temperatures newline
Pagination: 100p
URI: http://hdl.handle.net/10603/298382
Appears in Departments:Department of Biotechnology

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01_title.pdfAttached File130.75 kBAdobe PDFView/Open
02_certificate.pdf183.94 kBAdobe PDFView/Open
03_abstract.pdf248.57 kBAdobe PDFView/Open
04_declaration.pdf264.08 kBAdobe PDFView/Open
05_contents.pdf64.65 kBAdobe PDFView/Open
06_list_of_tables.pdf322.85 kBAdobe PDFView/Open
07_list_of_figures.pdf330.83 kBAdobe PDFView/Open
08_abbreviations.pdf273.68 kBAdobe PDFView/Open
09_chapter 1.pdf411.38 kBAdobe PDFView/Open
10_chapter 2.pdf394.05 kBAdobe PDFView/Open
11_chapter 3.pdf527.84 kBAdobe PDFView/Open
12_chapter 4.pdf1.39 MBAdobe PDFView/Open
13_bibliography.pdf563.41 kBAdobe PDFView/Open
14_conclusion.pdf426.35 kBAdobe PDFView/Open
80_recommendation.pdf1.42 MBAdobe PDFView/Open


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