Protease inhibitors from jackfruit seed (Artocarpus integrifolia)

Bhat, Archana; Pattabiraman, T. N.

doi:10.1007/bf02703421

Cited by 16 publications

(11 citation statements)

References 32 publications

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“…In context to the mechanism of action, ASPI has demonstrated non competitive inhibition which is in compliance to majority of PIs showing non competitive inhibition kinetics [40]. The low Ki value also indicates high affinity of ASPI towards trypsin and also homology with other kunitz-type PIs possessing trypsin inhibitory nature [41]. …”

Section: Discussionmentioning

confidence: 99%

Allium sativum Protease Inhibitor: A Novel Kunitz Trypsin Inhibitor from Garlic Is a New Comrade of the Serpin Family

et al. 2016

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PurposeThis study was aimed to purify and characterize the Protease inhibitor (PI) from a plant Allium sativum (garlic) with strong medicinal properties and to explore its phytodrug potentials.MethodsAllium sativum Protease Inhibitor (ASPI) was purified using ammonium sulphate fractionation and Fast Protein Liquid Chromatography on anion exchanger Hi-Trap DEAE column. The purified protein was analyzed for its purity and molecular weight by SDS PAGE. The confirmation of presence of trypsin inhibiting PI was performed by MALDI TOF-TOF and analyzed by MASCOT database. The ASPI was further investigated for its kinetic properties and stability under extreme conditions of pH, temperature and chemical denaturants. Secondary structure was determined by Circular Dichorism (CD) spectroscopy.ResultsASPI of ~15 kDa inhibited trypsin and matched "truncated kunitz Trypsin Inhibitor (Glycine max)" in MASCOT database. The purified ASPI showed 30376.1371 U/mg specific activity with a fold purity of 159.92 and yield ~93%. ASPI was quite stable in the range of pH 2–12 showing a decline in the activity around pH 4–5 suggesting that the pI value of the protein as ASPI aggregates in this range. ASPI showed stability to a broad range of temperature (10–80°C) but declined beyond 80°C. Further, detergents, oxidizing agents and reducing agents demonstrated change in ASPI activity under varying concentrations. The kinetic analysis revealed sigmoidal relationship of velocity with substrate concentration with Vmax 240.8 (μM/min) and Km value of 0.12 μM. ASPI showed uncompetitive inhibition with a Ki of 0.08±0.01 nM). The Far UV CD depicted 2.0% α -helices and 51% β -sheets at native pH.ConclusionsTo conclude, purified ~15 kDa ASPI exhibited fair stability in wide range of pH and temperature Overall, there was an increase in purification fold with remarkable yield. Chemical modification studies suggested the presence of lysine and tryptophan residues as lead amino acids present in the reactive sites. Therefore, ASPI with trypsin inhibitory property has the potential to be used as a non-cytotoxic clinical agents.

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Section: Discussionmentioning

confidence: 99%

Allium sativum Protease Inhibitor: A Novel Kunitz Trypsin Inhibitor from Garlic Is a New Comrade of the Serpin Family

et al. 2016

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“…Although a few like soybean trypsin inhibitor has shown the competitive type of inhibition, the majority of the inhibitors follows non-competitive inhibition kinetics [46]. Jack fruit seed protease inhibitor isolated by Annapurna et al, [42] also showed non-competitive enzyme inhibition but the one isolated by Bhat [60] exhibited uncompetitive inhibition. The Ki value of SNTI was found to be 0.75+0.05x10-10 M. The low Ki value indicates high affinity of SNTI towards trypsin.…”

Section: Discussionmentioning

confidence: 99%

Evaluating the role of a trypsin inhibitor from soap nut (Sapindus trifoliatus L. Var. Emarginatus) seeds against larval gut proteases, its purification and characterization

et al. 2015

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“…The jackfruit, a non-leguminous plant is also edible even though it is believed that it is difficult to digested (Siddappa 1957). Earlier it was also reported that jackfruit seed extract was found to inhibit the proteolytic activities of different animal pancreatic preparations (Bhat and Pattabiraman 1989). The highest level inhibition of papain and midgut protease of YSB larvae by mature seeds extract indicated that the maturity of jackfruit contains higher content of inhibitor.…”

Section: Discussionmentioning

confidence: 96%

Inhibition of midgut protease of yellow stem borer (Scirpophaga incertulas) by cysteine protease-like inhibitor from mature jackfruit (Artocarpus heterophyllus) seed

2011

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A novel protease inhibitor was isolated and purified from the mature seeds of jackfruit (Artocarpus heterophyllus) by precipitation with ammonium sulphate, followed by DEAE-cellulose and gel filtration (Sephadex G-100) chromatography. The isolated protease inhibitor strongly inhibited papain and midgut proteases of yellow stem borer (Scipophaga incertulas) larvae, as seen by in vitro assay. The purified protease inhibitor was active over a wide range of pH with the maximum activity between pH 4 and 10. This protein was also stable up to 80°C, but the retained activity was lost at 100°C, when heated for 30 min. The molecular mass of the purified cysteine-like protease inhibitor is to be 14.50 kDa as determined by SDS-PAGE. Significant reduction in larval weight and mortality was observed, when fresh rice culms with protease inhibitor was feeded to the yellow stem borer larvae. These results may provide important information to control the yellow stem borer in rice with respect to naturally occurring insecticidal proteins. The observed differences would potentially translate into reductions in population growth of yellow stem borer, indicating a potential value of using jackfruit protease inhibitor for protecting rice plants against damage by the yellow stem borer.

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Protease inhibitors from jackfruit seed (Artocarpus integrifolia)

Cited by 16 publications

References 32 publications

Allium sativum Protease Inhibitor: A Novel Kunitz Trypsin Inhibitor from Garlic Is a New Comrade of the Serpin Family

Allium sativum Protease Inhibitor: A Novel Kunitz Trypsin Inhibitor from Garlic Is a New Comrade of the Serpin Family

Evaluating the role of a trypsin inhibitor from soap nut (Sapindus trifoliatus L. Var. Emarginatus) seeds against larval gut proteases, its purification and characterization

Inhibition of midgut protease of yellow stem borer (Scirpophaga incertulas) by cysteine protease-like inhibitor from mature jackfruit (Artocarpus heterophyllus) seed

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