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Biochemical Characterization of Novel Bioactive Protein from Silkworm (Bombyx mori L) Fecal Matter

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Abstract

In this study, complete purification and biochemical characterization of protein is presented. The protein was purified by using Sephadex G-75 gel filtration column followed by reverse-phase high-performance liquid chromatography in a C18 column. The molecular weight of the protein was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis, mass spectrum matrix-assisted laser desorption/ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS) and liquid chromatography-electrospray ionization tandem mass spectrometry. Protein was fragmented by trypsin based on the m/z values obtained by MALDI-TOF-MS analysis. The peptide fragments sequence showed homology with DEAD-box-ATP-dependent RNA helicase 45, present in a public domain, National Centre for Biotechnology Information. The protein exhibited antibacterial activity against selected Gram +/− bacteria. The analgesic activity was determined by conducting acetic-acid-induced writhing test in mice.

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Acknowledgments

We acknowledge the UGC for financial support to the present research work. We are greatly thankful to S.C.S. College of Pharmacy, Harapanahalli, Karnataka (India), for their assistance in conducting animal experiments. Authors are grateful to Mr. Satish Kumar, Department of Molecular Biophysics, Indian Institute of Science, Bangalore 500 012, Karnataka (India), for his technical assistance.

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Authors have no conflict of interest.

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  1. Department of Post Graduate Studies and Research in Biochemistry, Jnana Sahyadri, Kuvempu University, Shankaraghatta, Shivamogga, Karnataka, 577451, India

    R. Raghavendra & S. E. Neelagund

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  1. R. Raghavendra
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  2. S. E. Neelagund
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Correspondence to S. E. Neelagund.

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Raghavendra, R., Neelagund, S.E. Biochemical Characterization of Novel Bioactive Protein from Silkworm (Bombyx mori L) Fecal Matter. Appl Biochem Biotechnol 167, 1002–1014 (2012). https://doi.org/10.1007/s12010-012-9588-9

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