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murraya tetramera/protease

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Structure-function studies of Murraya koenigii trypsin inhibitor revealed a compact structure made of central beta-sheet surrounded by alpha-helices with differences in structure and functional stability. Proteolysis studies, of native and heat-treated protein, demonstrated that inhibitor exhibited

Bioinsecticidal activity of Murraya koenigii miraculin-like protein against Helicoverpa armigera and Spodoptera litura.

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Miraculin-like proteins, belonging to the Kunitz superfamily, are natural plant defense agents against pests and predators, and therefore are potential biopesticides for incorporation into pest-resistant crops. Here, a miraculin-like protein from Murraya koenigii was assessed for its in vitro and in
The global emergence of antibiotic-resistant strains of Pseudomonas aeruginosa poses a major threat in both hospital environments and the community. P. aeruginosa is an opportunistic human pathogen, and it also infects a wide range of model organisms including the nematode Caenorhabditis elegans.
Murraya koenigii (curry tree) leaves are rich in bioactive compounds such as flavonoids, alkaloids, and coumarins. Alkaloids from M. koenigii leaves have antianalgesic, antiulcerogenic, antiobesity, and antitumor activities. In this study, we tested the cytotoxic and proteasome-inhibitory potential

Purification and characterization of approximately 35 kDa antioxidant protein from curry leaves (Murraya koenigii L.).

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Curry leaves (Murraya koenigii L. Spreng, Rutaceae) is an herbal species used in traditional medicine in eastern Asia. In this study, the antioxidant protein was purified by homogenization of curry leaves powder in Tris buffer, 65% ammonium sulphate precipitation and gel filtration on Sephadex G-75
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