Open AccessImmobilization of lignin peroxidase from Alcaligenes aquatilis and its application in dye decolorization
Publication year - 2020
Publication title -
letters in applied nanobioscience
Language(s) - English
Resource type - Journals
ISSN - 2284-6808
DOI - 10.33263/lianbs92.10581063
Subject(s) - lignin peroxidase , chemistry , lignin , adsorption , thermostability , malachite green , peroxidase , immobilized enzyme , nuclear chemistry , thermal stability , horseradish peroxidase , chitosan , chromatography , organic chemistry , enzyme
Purefied lignin peroxidase produced from Alcaligenes aquatilis DB8 was immobilized by entrapment on Ca-alginate and chitosan by adsorption and cross linker. Immobilization yields of entrapment, adsorption and cross linking methods were 79.6%, 31.4% and 91.2%, respectively. The thermostability of immobilized LiP by entrapment, adsorption and crosslinking retained residual activity of 68%, 63% and 85%, respectively after 180 min at 50 °C. While the residual activity of free enzyme was decreased to almost half after 180 min. Lignin peroxidase immobilized by crosslinking showed high thermal stability, more than 70% of the enzymatic activity remained after 240 min. Also, immobilized lignin peroxidase by crosslinking showed better storage stability about 55% at 30 days. The application of immobilized lignin peroxidase in a packed bead bioreactor enhanced decolorization of malachite green at 20 mg/l, and the percent of decolorization was 97% at 4 h.