In silico characterization and recombinant protein analysis of two subtilisin-like Serine Proteases from the mushroom Lignosus rhinocerus

Sun Y. Y., Ayesha F., Peter C. C. H., Atiqah M. A. N., Renee L. L. H.

RESEARCH JOURNAL OF BIOTECHNOLOGY, vol.15, no.9, pp.57-71, 2020 (ESCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 15 Issue: 9
  • Publication Date: 2020
  • Journal Indexes: Emerging Sources Citation Index (ESCI), Scopus
  • Page Numbers: pp.57-71
  • Keywords: Lignosus rhinocerus, serine protease, expression, homology modeling, proteolytic activity, PROTEOMIC ANALYSIS, PURIFICATION, EXPRESSION, BACILLUS, CLONING, MECHANISMS, MACROFUNGI, INSIGHTS, PEPTIDE, CHARGE
  • Bezmialem Vakıf University Affiliated: No


Serine proteases are a class of proteolytic enzymes with important physiological functions in living organisms. Due to their wide medical and industrial applications, there is an increasing interest in isolation and characterization of novel serine proteases from natural sources. Two serine proteases (4347-SPL and 8711-SPL) were isolated from the medicinal mushroom Lignosus rhinocerus for in silico characterisation and proteolytic analysis. Both the cDNA encoding for zymogens consist of 399 amino acids residues with 67.2% similiarity. Clustal sequence alignments of 4347-SPL and 8711-SPL with other serine proteases reveal active catalytic triads of Asp-His-Ser residues.