Production and activities of chitinases and hydrophobins from Lecanicillium lecanii.

The production of chitinases and hydrophobins from Lecanicillium lecanii was influenced by the cultivation method and type of carbon source. Crude enzyme obtained from solid-substrate culture presented activities of exochitinases (32 and 51 kDa), endochitinases (26 kDa), β-N-acetylhexosaminidases (61, 80, 96 and 111 kDa). Additionally, submerged cultures produced exochitinases (32 and 45 kDa), endochitinases (10 and 26 kDa) and β-N-acetylhexosaminidases (61, 96 and 111 kDa). β-N-acetylhexosaminidases activity determined in solid-substrate culture with added chitin was ca. threefold (7.58 ± 0.57 U mg(-1)) higher than submerged culture (2.73 + 0.57 U mg(-1)). Similarly, hydrophobins displayed higher activities in solid-substrate culture (627.3 ± 2 μg protein mL(-1)) than the submerged one (57.4 ± 4.7 μg protein mL(-1)). Molecular weight of hydrophobins produced in solid-substrate culture was 7.6 kDa and they displayed surface activity on Teflon.