Purification and characterization of an extracellular trypsin-like protease of Fusarium oxysporum var. lini

Purification, Characterization and De-Staining Potentials of a Thermotolerant Protease Produced by Fusarium oxysporum

“…1). In variance to our findings, the molecular weight of the F. oxysporum FWT1 protease was higher than that reported by Ricardo et al [27], Pekkarinen et al [26] and Wu et al [28] having a molecular mass of 41, 28.7 and 28 kDa for purified protease by Fusarium culmorum, Fusarium oxysporum var iini and Fusarium sp. respectively.…”

“…The result obtained in this research was in conformity with the earlier findings of Adejuwon and Olutiola [34] which showed enhancement of protease activity in the presence of Ca 2+ and Mg 2+ by Fusarium spp. Reports by Namrata and Kantishree [39] and Ricardo et al [27] for Aspergillus tamari and Fusarium oxysporum were also in conformity with our data. This is because the metal ions had been stated as viable stability enhancers of proteases.…”

Chymotrypsin- and trypsin-like activities secreted by the multidrug-resistant yeasts forming the Candida haemulonii complex

“…Among the secreted serine peptidases correlated with the fungal pathogenesis in humans, we can highlight those belonging to the S1 family (one of the main families of fungal serine peptidases), which are well described in several genera of filamentous fungi, but very little studied in Candida spp. (Muhsin et al 1997, Barata et al 2002, Zarnowski et al 2007, Dubovenko et al 2010…”

“…With regard to human pathogenic fungi, secretion of chymotrypsin-like serine peptidases able to degrade the substrate N-succinyl-Ala-Ala-Pro-Phe-MCA and whose activity is inhibited by PMSF, was detected in the culture supernatant of the fungus S. schenckii (tsuboi et al 1987). In parallel, a secreted trypsin-like peptidase, with higher activity in basic pH at 45°C and inhibited by benzamidine, was described in the culture supernatant of Fusarium oxysporum (Barata et al 2002). In the present study, secreted serine peptidases from the S1 family were described, for the first time, in the C. haemulonii species complex, opportunistic fungal pathogens with extremely scarce knowledge about their pathophysiology processes.…”

“…albicans, C. guilliermondii, C. parapsilosis, C. tropicalis, C. dubliniensis and C. lipolytica (Santos and Soares 2005, Santos et al 2006, Melo et al 2007, Vermelho et al 2010, Portela et al 2010. Secreted serine-type peptidases belonging to the S1 family (e.g., trypsin-, chymotrypsin-and elastaselike peptidases) (Dubovenko et al 2010) have gained prominence due to their multiple roles in the pathogenicity of opportunistic fungi (Muszewska et al 2017), such as Scedosporium, Sporothrix and Aspergillus (Muhsin et al 1997, Barata et al 2002, Han et al 2017. these serine peptidases have great similarities in their sequences and tridimensional structures; however, they present different substrate specificities (Haën et al 1975, Ma et al 2005, in which trypsin-like peptidases have affinity for basic amino acid residues (e.g., lysine and arginine), chymotrypsin-like peptidases have affinity for aromatic amino acid residues (e.g., phenylalanine, tyrosine and tryptophan) (Vajda and Szabó 1976), while elastase-like peptidases have preference for aliphatic amino acid residues, particularly alanine (Zimmerman and Ashe 1977).…”