Characterization of Trichoderma harzianum lipase purified by micellar AOT/n-heptane system and resistant in vitro to acid, pepsin hydrolysis and bile salts
Year: 2026
Type: article
Abstract: The lipase from Trichoderma harzianum was purified by reverse micelles system using AOT/n-heptane 0.1 mol/L for extraction and phosphate buffer 0.05 mol/L pH 7.0 containing 1.2 mol/L KCl for re-extraction. Was obtained 3.45 purification factor. The enzyme showed maximal activity at 20°C in citrate-phosphate buffer 0.05 mol/L pH 7.0. It was stable between 20°C and 40°C and pH between 2.2 and 7.0. Was obtained high residual activity after 1 h of incubation in nonpolar organic solvents. In polar solvents, the residual activities were 50%, 4.7%, 26% and 12% in 25% (v /v) methanol, isopropanol, ethanol and acetone, respectively. None of tested metal ions promoted more than 30% decrease in activity. An increase of 8% and 19% in the activity was observed when added Ni+2 and Zn+2. There was an increase in activity in Triton X-100 and reduced activity with in SDS and Tween-80 surfactants. In simulated gastric/intestinal environment, the enzyme remained active in presence of pepsin at pH 3.0, and only lost 30% of its activity at pH 8.0 in presence of 0.1% bile salts. Thus, the lipase from T. harzianum has potential for future applications in enzyme replacement drugs and has interesting characteristics for application in biocatalysis.
Institution: Universidade Estadual Paulista (Unesp)
Subfield: Biotechnology
Domain: Life Sciences
Open Access status: diamond
OpenAlex ID: W7203614016
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