RESUMO
Fungal lipolytic enzymes play crucial roles in various lipid bio-industry processes. Here, we elucidated the biochemical and structural characteristics of an unexplored fungal lipolytic enzyme (TaLip) from Thermoascus aurantiacus var. levisporus, a strain renowned for its significant industrial relevance in carbohydrate-active enzyme production. TaLip belongs to a poorly understood phylogenetic branch within the class 3 lipase family and prefers to hydrolyze mainly short-chain esters. Nonetheless, it also displays activity against natural long-chain triacylglycerols. Furthermore, our analyses revealed that the surfactant sodium dodecyl sulfate (SDS) enhances the hydrolytic activity of TaLip on pNP butyrate by up to 5.0-fold. Biophysical studies suggest that interactions with SDS may prevent TaLip aggregation, thereby preserving the integrity and stability of its monomeric form and improving its performance. These findings highlight the resilience of TaLip as a lipolytic enzyme capable of functioning in tandem with surfactants, offering an intriguing enzymatic model for further exploration of surfactant tolerance and activation in biotechnological applications.
Assuntos
Esterases , Lipase , Tensoativos , Tensoativos/química , Tensoativos/farmacologia , Lipase/metabolismo , Lipase/química , Esterases/metabolismo , Esterases/química , Dodecilsulfato de Sódio/química , Especificidade por Substrato , Hidrólise , Proteínas Fúngicas/química , Proteínas Fúngicas/metabolismo , Ânions/química , Ânions/metabolismo , Estabilidade EnzimáticaRESUMO
A bioreactor was built by means of immobilizing alpha-amylase from Aspergillus oryzae by encapsulation, through cryopolymerization of acrylamide monomers for the continuous starch hydrolysis. The starch hydrolysis was evaluated regarding pH, the concentration of immobilized amylase on cryogel, the concentration of starch solution and temperature. The maximum value for starch hydrolysis was achieved at pH 5.0, concentration of immobilized enzyme 111.44 mg amylase /gcryogel , concentration of starch solution 45 g/L and temperature of 35°C. The immobilized enzyme showed a conversion ratio ranging from 68.2 to 97.37%, depending on the pH and temperature employed. Thus, our results suggest that the alpha-amylase from A. oryzae immobilized on cryogel monoliths represents a potential process for industrial production of maltose from starch hydrolysis.