Characterization and Proteolytic Activity of <i>Arum palaestinum</i> extract

Medicinal plants have been utilized to treat a wide range of diseases and have constituted a primary source of bioactive compounds for pharmaceutical development. Plant proteases are essential in regulating metabolic pathways that influence gene expression and remove unfavourable metabolites. The current study aims to evaluate the in vitro proteolytic and bioactivity of the methanolic leaf extract of Arum palaestinum. The plant extract's TPC, antioxidant, anti-inflammatory, and anti-hemolytic activities were determined using colorimetric methods, and the proteolytic activity was assessed using casein as a substrate. The investigations revealed that the extracts possess anti-inflammatory properties of 90–95%, with IC50 = 1.1133 mg/mL, and anti-hemolytic activity of 90–95% with IC50 = 0.2149 mg/mL. The extract exhibited good antioxidant activity of 71.30 % with IC50 = 0.1975 mg/ml. The result also showed that the raw extracts contain phenolic compounds (65.48 mg GAE/g). The extract's proteolytic effects on casein as a substrate were observed at pH 7.0 and 50 °C. The raw extract showed the most significant activity toward casein as a substrate. The Lineweaver-Burk reciprocal plot indicated a Km score of 0.667 mg/mL and Vmax = 5.0 μmol/min for the proteases in the extracts. The plant extract demonstrates potent antioxidant, anti-inflammatory, and anti-hemolytic properties, which could be associated with the polyphenolic compounds. The extract also showed potential as a source of proteolytic enzymes and could be harnessed as a source of proteases for industrial uses. This plant can further be explored as a source of potent compounds for drug development and industrial applications.

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Publication Details

Journal
Baghdad Science Journal
Published
2026-06-17
DOI
https://doi.org/10.21123/2411-7986.5322
Primary Topic
Protein Hydrolysis and Bioactive Peptides
Type
article
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article

Characterization and Proteolytic Activity of Arum palaestinum extract

Omar M. Atrooz, Saba Khaled
Baghdad Science Journal
Protein Hydrolysis and Bioactive Peptides
article

Characterization and Proteolytic Activity of Arum palaestinum extract

Omar M. Atrooz, Saba Khaled
article en

Abstract

Medicinal plants have been utilized to treat a wide range of diseases and have constituted a primary source of bioactive compounds for pharmaceutical development. Plant proteases are essential in regulating metabolic pathways that influence gene expression and remove unfavourable metabolites. The current study aims to evaluate the in vitro proteolytic and bioactivity of the methanolic leaf extract of Arum palaestinum. The plant extract's TPC, antioxidant, anti-inflammatory, and anti-hemolytic activities were determined using colorimetric methods, and the proteolytic activity was assessed using casein as a substrate. The investigations revealed that the extracts possess anti-inflammatory properties of 90–95%, with IC50 = 1.1133 mg/mL, and anti-hemolytic activity of 90–95% with IC50 = 0.2149 mg/mL. The extract exhibited good antioxidant activity of 71.30 % with IC50 = 0.1975 mg/ml. The result also showed that the raw extracts contain phenolic compounds (65.48 mg GAE/g). The extract's proteolytic effects on casein as a substrate were observed at pH 7.0 and 50 °C. The raw extract showed the most significant activity toward casein as a substrate. The Lineweaver-Burk reciprocal plot indicated a Km score of 0.667 mg/mL and Vmax = 5.0 μmol/min for the proteases in the extracts. The plant extract demonstrates potent antioxidant, anti-inflammatory, and anti-hemolytic properties, which could be associated with the polyphenolic compounds. The extract also showed potential as a source of proteolytic enzymes and could be harnessed as a source of proteases for industrial uses. This plant can further be explored as a source of potent compounds for drug development and industrial applications.

Baghdad Science JournalVol. 23(6)
Cairo University (EG), Mutah University (JO)
Openalex Percentile: Top 11%
Protein Hydrolysis and Bioactive Peptides
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