Journal
BIORESOURCE TECHNOLOGY
Volume 345, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2021.126497
Keywords
CBD; Lactase; Magnetic particles; Lactose hydrolysis
Funding
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [308515/2020-0, 315225/2018-1, 420506/2016-0]
- Fundacao de Amparo `a Pesquisa do Estado do Rio Grande do Sul (FAPERGS)
- Universidade do Vale do Taquari (Univates)
- FAPERGS [19/2551-0001740-5]
- Quatro G Pesquisa & Desenvolvimento Ltda
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This study reported a novel enzyme immobilization process that significantly improved the efficiency and stability of immobilized enzymes. This method provides a way to quickly carry out purification and immobilization processes simultaneously, obtaining enzyme preparations with promising catalytic characteristics for applications in the food and pharmaceutical industries.
For the first time, this work reported the one-step purification and targeted immobilization process of a 13-galactosidase (Gal) with the Cellulose Binding Domain (CBD) tag, by binding it to different magnetic cellulose supports. The process efficiency after 13-galactosidase-CBD immobilization on magnetic cellulose-based supports showed values of approximately 90% for all evaluated enzymatic loads. Compared with free Gal, derivatives showed affinity values between 13-galactosidase and the substrate 1.2 x higher in the lactose hydrolysis of milk. 13-Galactosidase-CBD's oriented immobilization process on supports increased the thermal stability of the immobilized enzyme by up to 7 x . After 15 cycles of reuse, both enzyme preparations showed a relative hydrolysis percentage of 50% of lactose in milk. The oriented immobilization process developed for purifying recombinant proteins containing the CBD tag enabled the execution of both steps simultaneously and quickly and the obtention of beta-galactosidases with promising catalytic characteristics for application in the food and pharmaceutical industries.
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