Immobilization studies of a pectinase produced by Aspergillus terreus.
Biotechnol Appl Biochem. 2020 Aug 08;:
Authors: Vaz RP, Vici AC, Polizeli ML, Magalhães PO, Filho EXF
Aspergillus terreus can produce different holocellulose-degrading enzymes when grown in sugarcane bagasse, with predominant pectinase activity. Thus, pectinase was selected for purification and immobilization studies. Ion exchange and molecular exclusion chromatography studies were performed, after which it was possible to semi-purify the enzyme with a yield of 80%. The crude extract pectinase (PECEB) and the partially purified enzyme (PEC2) were immobilized on monoamino-N-aminoethyl (MANAE)-agarose with pectinase activity yields of 66% and 98%, respectively. After immobilization in MANAE-agarose, the pectinase showed higher activity at acidic pH (pH 4.0) when compared to the non-immobilized enzyme. It was also found that after the immobilization process, there was a three-fold improvement in the enzyme’s thermostability. Also, it was possible to reuse the immobilized enzyme for up to 5 cycles of hydrolysis with effective production of reducing sugars (0.196 mg/g of substrate). The industrial application test revealed a significant decrease in the viscosity of guava juice when the immobilized enzyme was used. PECEB, immobilized on MANAE-agarose, was the enzyme sample that generated the highest pulp viscosity reduction (approximately 47%). Although additional studies are needed for practical industrial application, the results obtained herein reveal the potential of application of immobilized pectinase in the industry. This article is protected by copyright. All rights reserved.
PMID: 32770865 [PubMed – as supplied by publisher]