| Literature DB >> 29291859 |
Natália Carminatti Ricardi1, Eliana Weber de Menezes1, Edilson Valmir Benvenutti1, Jéssie da Natividade Schöffer2, Camila Regina Hackenhaar2, Plinho Francisco Hertz2, Tania Maria Haas Costa3.
Abstract
β-d-Galactosidase is an important enzyme in the dairy industry, and the enzyme from the yeast Kluyveromyces lactis is most widely used. Here, we report immobilization of the enzyme on a silica/chitosan composite support, devised to have 10% and 20% chitosan (SiQT10 and SiQT20, respectively). Morphological and textural characterizations showed that chitosan is dispersed in micrometric regions in silica. For comparison, a silica organofunctionalized with 3-aminopropyltrimethoxysilane (SiO2aptms) was prepared. Performance of the biocatalysts was tested for lactose hydrolysis, and the enzyme immobilized in SiQT10 and SiQT20 composites showed higher efficiency (62% and 47%, respectively) compared with the enzyme in SiO2aptms. Operational stability in this system was evaluated for the first time. After 200 h of continuous use in a fixed-bed reactor, SiQT10 remained with approximately 90% activity. Thus, in addition to demonstrating compatibility for food processing, these results align the enzyme stabilization properties of chitosan with the mechanical resistance of silica.Entities:
Keywords: Biocatalysis; Continuous operation system; Enzyme immobilization; Heterogeneous biocatalyst; Inorganic-organic composite materials; Lactose hydrolysis reaction
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Year: 2017 PMID: 29291859 DOI: 10.1016/j.foodchem.2017.11.026
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514