Characterization of partially purified cysteine protease inhibitor from Tetracarpidium conophorum (African walnut)

Obayomi, Abimbola A.; Adeola, Segun; Bankole, Habeeb Adebodun; Raimi, O.G.

doi:10.5897/ajbr2014.0795

Cited by 5 publications

(5 citation statements)

References 29 publications

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“…50 -70% ammonium sulphate precipitation of protease inhibitors from seeds of Helianthus annuus gave the highest yield and inhibitory effect when incubated with larva gut proteases [46]. 65% ammonium sulphate saturation of CPI that exhibited the maximum inhibitory effect has also been reported [47].…”

Section: Discussionmentioning

confidence: 92%

Characterization of Partially Purified Cysteine Protease Inhibitor From Canavalia Ensiformis (Wonder Bean)

Adeola

2017

JRRS

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Cysteine protease inhibitors (CPIs) are widespread in plant seeds and are attractive candidates for use in the pharmaceutical industry. Wonder bean (Canavalia ensiformis) is a climbing perennial legume with fascinating pharmacological properties. A distinguishing characteristic of this plant is its ability to thrive under extreme environmental conditions such as nutrient-depleted, highly leached and acidic soil. Plants that survive in these extreme environmental conditions are known for high effective protease regulation by protease inhibitors which include CPI. Study was therefore designed with the aim to isolate and characterize CPI from wonder bean. CPI from Canavalia ensiformis was isolated and purified by simple methods consisting ammonium sulphate precipitation, ion exchange chromatography and gel filtration. Mode of inhibition, optimum temperature and pH, as well as the effect of metals on the enzyme activity were determined using spectrophotometric method. The purified CPI was confirmed to be a competitive inhibitor against papain with the same Vmax = 78.59?103?mol/min, Km=209?M, and Ki = 137 ?M. The inhibitor exhibited maximal activity at temperature and pH of 40°C and 8.0 respectively. Metal cations such as, Pb2+, Mg2+,Co2+, Mn2+, Zn2+ and Cu2+ significantly inhibited CPI at a very low concentration (1mM). The SDS-PAGE analysis revealed two bands of molecular weight estimated to be 28 and 32 KDa. CPI from Canavalia ensiformis was successfully isolated and there was an indication that it is composed of two polypeptide chains that might have been denatured under reducing condition in the presence of ?-mercaptoethanol. However, further investigation is required to verify this.

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Section: Discussionmentioning

confidence: 92%

Characterization of Partially Purified Cysteine Protease Inhibitor From Canavalia Ensiformis (Wonder Bean)

Adeola

2017

JRRS

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“…Also, CPIs have been researched and implicated in some disease conditions such as diabetes, cancer and neurodegenerative disorders among many others [19]. Plant cysteine protease inhibitors (CPIs) have therefore been studied extensively [2,9,20]. However, this study is the first at attempting to characterize CPI from A. muricata.…”

Section: Discussionmentioning

confidence: 99%

“…Several protease inhibitors extracted from plants have been reported to be more effective after precipitating with high ammonium sulphate concentration. Obayomiet al; [9] reported that 65% ammonium sulphate saturation of CPI exhibited the maximum inhibitory effect. Ashouriet al; [22], also reported that a 50-70% ammonium sulphate precipitation of protease inhibitors from seeds of Helianthus annuus produced the highest inhibitory effect (41.53%) when incubated with larva gut proteases.…”

Section: Purification Of Cysteine Protease Inhibitormentioning

confidence: 98%

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Characterization of Partially Purified Cysteine Protease Inhibitor From the Fruits and Seeds of Soursop (Annona Muricata)

Adeola

Bankole

Kanmodi

2020

JRRS

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Introduction: Soursop (Annona muricataLinn) is an edible lowland tropical fruit-bearing tree that is widely cultivated across regions of the world. It has been extensively researched as a result of its store of acetogenin; a potent anticancer agent. However, there is a dearth of information on the precise mechanism of action of acetogenin; thereby subjecting it to rigorous scrutiny. It is therefore imperative to investigate this plant in the hope of discovering a different class of anticancer agent inherent in it. Various studies have demonstrated that cysteine protease inhibitors (CPIs) have considerable therapeutic potential which can be utilized in a variety of disease states including cancer. Aim: Study was designed to isolate, purify and characterize CPI from the fruits and seeds of Soursop. Method: Isolation and purification of CPI was achieved by simple methods consisting of ammonium sulphate precipitation, anion exchange chromatography and size exclusion chromatography. Mode of inhibition, optimum pH and temperature, as well as the effect of metals on the enzyme activity were determined using spectrophotometry. Result: The purified CPI from seeds and fruits exhibited competitive and noncompetitive inhibition against papain respectively. However, maximal inhibitory activities for both fruit and seed samples were observed at similar optimal pH and temperature of 8 and 40°C respectively. Although, metal cations such as cobalt (Co2+), copper (Cu2+) and zinc (Zn2+) did not effect a considerable decrease on the inhibitory activity of the CPI; Lead (Pb2+), Magnesium (Mg2+) and manganese (Mn2+) significantly inhibited CPI at a very low concentration (1mM). Conclusion: The antagonistic properties exhibited by the purified CPI certainly indicate its likely suitability for pharmaceutical application in the treatment of some pathological conditions such as cancer in which uncontrolled proteolytic activities of cysteine proteases are implicated. There is an ample scope for further research on structure elucidation and protein engineering to facilitate its usage in wide range of application.

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“…Researchers have identified cysteine protease inhibitors as an important tool for the utilization in pharmaceutical industry due to their potent health benefits. Obayomi et al [76] purified cysteine protease inhibitors from Tetracarpidium conophorum which is competitively inhibit papain, a proteolytic enzyme that aids in digestion.…”

Section: Cysteine Protease Inhibitorsmentioning

confidence: 99%

A Review on Therapeutic Potential of Protease Inhibitors from Medicinal Plants

Gamage

Kumari

2019

AJRB

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Most of the currently available therapeutic agents, particularly for cardiovascular disorders and cancers are very expensive and induce some serious side effects. Some of these drugs have also become less effective due to the emergence of antibiotic resistance. There is a necessity and great demand for the development of novel efficacious plant-based agents that are of pharmacologically effective. In this connection, this review focuses on therapeutic potential of plant protease inhibitors. Protease inhibitors are of a particular concern at present due to their potent ability to inhibit protease enzymes that are involved in pathogenesis of various human diseases. In addition to their function as protein-degrading enzymes, protease inhibitors are now well-known for their capability to involve in many biological activities as signaling molecules. Plant protease inhibitors are also engaged in several physiological and pathological processes, such as blood clotting, inflammation, immune regulation, apoptosis and carcinogenesis. Therefore, isolation of plant protease inhibitors and evaluation of their therapeutic capacity against chronic human diseases have become a major research interest. Nevertheless, protease inhibitor content and protease specificity vary significantly even in the same plant species depending on the geographical location and environmental factors. Consequently, it is important to identify potent therapeutic potential of each plant protease inhibitor on human health individually.

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Characterization of partially purified cysteine protease inhibitor from Tetracarpidium conophorum (African walnut)

Cited by 5 publications

References 29 publications

Characterization of Partially Purified Cysteine Protease Inhibitor From Canavalia Ensiformis (Wonder Bean)

Characterization of Partially Purified Cysteine Protease Inhibitor From Canavalia Ensiformis (Wonder Bean)

Characterization of Partially Purified Cysteine Protease Inhibitor From the Fruits and Seeds of Soursop (Annona Muricata)

A Review on Therapeutic Potential of Protease Inhibitors from Medicinal Plants

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