Benghalensin, a highly stable serine protease from the latex of medicinal plant Ficus benghalensis.
A serine protease was purified to homogeneity from the latex of medicinal plant Ficus benghalensis by a single step procedure using anion exchange chromatography. The enzyme, named benghalensin, has a molecular mass of 47 kDa (MALDI-TOF and SDS-PAGE). The purified protein is a glycoprotein, and the enzymatic activity is solely inhibited by PMSF and chymostatin, indicating that the enzyme belongs to the serine protease class. The isoelectric point of the enzyme is pH 4.4 with optimum pH and temperature of pH 8.0 and 55 degrees C respectively. The extinction coefficient (epsilon(1%)(280)) of the enzyme is 29.25, and the molecular structure consists of 17 tryptophan, 31 tyrosine and 09 cysteine residues. Peptide mass fingerprinting and de novo sequencing of tryptic-digested fragments of the protein did not find any putative conserved domains in BLAST analysis. The enzyme is stable and retains full activity over a broad range of pH and temperature or prolonged storage at 4 degrees C. Simple purification, high yield and stability enable exploration of the protein for structure-function relationship studies as well as other applications.
Sharma
Anurag
A
Institute of Medical Sciences, Banaras Hindu University, Varanasi, India.
Kumari
Moni
M
Jagannadham
M V
MV
D004795:Enzyme Stability; D030681:Ficus / Q000737:chemistry / Q000201:enzymology*; D007526:Isoelectric Point; D007840:Latex / Q000737:chemistry / Q000378:metabolism*; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D010946:Plants, Medicinal / Q000737:chemistry / Q000201:enzymology*; D057057:Serine Proteases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
D007840:Latex; D010940:Plant Proteins; D057057:Serine Proteases