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Updated: Jun 4, 2026

Measurement of Chitinase Activity in Biological Samples
Published on: August 22, 2019
Production and activities of chitinases and hydrophobins from Lecanicillium lecanii
Zaizy Rocha-Pino1, Gabriel Vigueras, Keiko Shirai
1Laboratory of Biopolymers, Biotechnology Department, Universidad Autónoma Metropolitana, Av. San Rafael Atlixco, No. 186, 09340, Mexico City, Mexico.
Abstract:
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.
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