Enzyme inhibitors from plants. Isolation and characterization of a protease inhibitor from arrow root (Maranta arundinaceae) tuber

Rao, N. Mallikarjuna; Rao, Huishan; Pattabiraman, T. N.

doi:10.1007/bf02702590

Cited by 5 publications

(3 citation statements)

References 25 publications

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“…The acetone precipitate was suspended in 100mΜ phosphate buffer, pH 7.6. This was designated as the crude protein acetone extract [5].…”

Section: Acetone Precipitationmentioning

confidence: 99%

“…This enzyme has drawn special attention as drug targets for the cure of several diseases such as osteoporosis, arthritis, cancer, and many parasitic infections [4]. The interaction between cysteine proteases and inhibitors is necessary for averting unwanted potentially destructive proteolysis [5]. These plant-derived inhibitors are gaining consideration as potential candidates which can be exploited in the [6].…”

Section: Introductionmentioning

confidence: 99%

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Partial Purification of Phytocystatin from Moringa oleifera lam

Abdulkadir¹,

Kabiru²,

Muhammad³

et al. 2022

AROC Pharm. Biotech.

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Background: Phytocystatins are plants cysteine protease inhibitors (CPIs) that are known for their numerous uses in medicine and biotechnology. Methods: Different extraction media which include, Sodium Hydroxide, Hydrochloric acid, Sodium Chloride, Sodium phosphate buffer and distilled Water were used to evaluate flower, leave, root, latex, and stem bark of Moringa oleifera for inhibitory activity against cysteine protease (Papain enzyme). The phosphate buffer extract with higher protease inhibitory activity was concentrated by cold acetone precipitation and further subjected to partial purification using ammonium sulphate fractionation and Hydrophobic chromatography on Phenyl Sepharose column. The molecular weight of partially purified protein was estimated by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis. Results: The extracts of Sodium phosphate buffer from the seeds of Moringa oleifera showed higher CPI activity of 11.23 units/mg protein. Cold acetone precipitated extract gave high yield of 94.6% protein with 60% inhibition of protease. The partially purified protein showed a fifty percent inhibitory concentration (IC50) of 1.22±0.3 mg/ml protein against the enzyme with 63% inhibition. An estimated molecular weight of 13.5kDa was obtained from electrophoretic analysis of partially purified protein. Conclusion: Moringa oleifera seeds could be a good source of low molecular weight protein Inhibitor of Cysteine protease and might be useful in biotechnology of traditional medicinal plants, in transgenic crops to arrest the negative pathogenic over expressions of cysteine proteases

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“…The acetone precipitate was suspended in 100mΜ phosphate buffer, pH 7.6. This was designated as the crude protein acetone extract [5].…”

Section: Acetone Precipitationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Partial Purification of Phytocystatin from Moringa oleifera lam

Abdulkadir¹,

Kabiru²,

Muhammad³

et al. 2022

AROC Pharm. Biotech.

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show abstract

“…The unbound fraction, washing and eluted fractions were subjected to an overnight dialysis against 500 ml of phosphate buffer (0.1 M, pH 7.0). The dialyzed samples of unbound fraction, washing and eluted fractions were subjected to the chitinase assay (Rao et al, 1983).…”

Section: Purification and Analysis Of Chitinase(s) Using Ion Exchangementioning

confidence: 99%

Chitinases from pitcher fluid of <i>Nepenthes distillatoria</i>

2019

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Chitinases belong to a diverse family of enzymes among many other hydrolytic enzymes of the pitcher fluid of Nepenthes sp. There are no existing studies on identification of chitinases in Nepenthes distillatoria the only representative of the genus Nepenthes in Sri Lanka. In this study an assay procedure was developed and optimized to detect the chitinolytic activity in the pitcher fluid of N. distillatoria using colloidal Chitin Azure as the substrate. Crude Nepenthes pitcher fluid was subjected to DEAE Cellulose chromatography in an attempt to partially purify and separate chitinases. The optimum pH, temperature and incubation time for the chitinolytic activity were 5.0, 27 °C and 30 min, respectively. DEAE Cellulose Chromatography revealed the presence of more than one type of chitinases within the pitcher juice. Further studies are required to characterize and confirm the origin/s of these chitinases.

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Natural plant enzyme inhibitors. Studies on a proteinase inhibitor from Italian millet (Setaria italica)

Udupa

Pattabiraman

1984

J Sci Food Agric

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A proteinase inhibitor specific for trypsin was purified from Italian millet (Setaria italica) 170-fold by extraction with 0.02M HCI, ammonium sulphate fractionation, chromatography on CM-cellulose and trypsin-affigel chromatography. The inhibitor with an M, of 14000 was found to be homogeneous by gel chromatography on Sephadex G-100 and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. It reacted with bovine trypsin in a 1 : 1 stoichiometric fashion. Inhibition of trypsin was nearly double when assayed with benzoyl m-arginine p-nitroanilide as substrate compared to the activity with casein as substrate. The inhibitor affected the tryptic activity in human and bovine pancreatic preparations to an equal extent. Chemical modification studies showed that amino groups, disulphide bridges and sulphydryl groups are essential for the action of the inhibitor. Pretreatment with porcine pepsin or bovine a-chymotrypsin increased the antitryptic activity of the inhibitor when assayed with the low molecular weight substrate but not with casein.

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Enzyme inhibitors from plants. Isolation and characterization of a protease inhibitor from arrow root (Maranta arundinaceae) tuber

Cited by 5 publications

References 25 publications

Partial Purification of Phytocystatin from Moringa oleifera lam

Partial Purification of Phytocystatin from Moringa oleifera lam

Chitinases from pitcher fluid of <i>Nepenthes distillatoria</i>

Natural plant enzyme inhibitors. Studies on a proteinase inhibitor from Italian millet (Setaria italica)

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