Imobilização da lipase de Candida Antarctica do tipo B usando como suporte fibra de coco verde pré-tratada por explosão a vapor
The present study aims to immobilize the enzyme CalB (Candida antarctica lipase B) in coconut fiber as a support. Two distinct systems were considered in order to obtain an immobilization composed, for the most part, of covalent bonds. In the first system, coconut fiber biomass was silanized w...
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| Formato: | bachelorThesis |
| Idioma: | pt_BR |
| Publicado em: |
Universidade Federal do Rio Grande do Norte
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| Endereço do item: | https://repositorio.ufrn.br/handle/123456789/53471 |
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| Resumo: | The present study aims to immobilize the enzyme CalB (Candida antarctica lipase B)
in coconut fiber as a support. Two distinct systems were considered in order to obtain an
immobilization composed, for the most part, of covalent bonds. In the first system, coconut
fiber biomass was silanized with APTES (3-aminopropyltriethoxysilane), then activated with
glutaraldehyde and an enzyme was immobilized. In the second system, the biomass was also
silanized with APTES, an enzyme was immobilized and subsequently coated with
glutaraldehyde. After immobilization, the parameters of the immobilized enzyme were
controlled to evaluate the efficiency of CalB immobilization in the coconut fiber matrix.
Subsequently, thermal stability tests were carried out, which consisted of exposing the
immobilized enzyme to high temperatures (60ºC, pH 7.0). Finally, the desorption test was
performed, which aimed to evaluate the type of bonds/interactions present in the
immobilization. Desorption was performed using NaCl (1M) and Triton X-100 (1.0% (v/v))
solutions in order to investigate whether the rejected forms were predominantly ionic or
hydrophobic. The results showed that the CalB enzyme was immobilized in both systems, with
immobilization yields of around 43.4 and 50.4% in 24 h of contact in the Biomassa-APTES GA-CalB and Biomassa-APTES-CalB systems, respectively. For both systems, the activities
of the immobilized enzymes remained similar, around 9.5 and 9.2 U/g. Furthermore, the
inactivation profiles of the immobilized enzymes showed a similar behavior, with an average
relative activity of around 65.0% at 90 min of inactivation for both systems. Coating with
glutaraldehyde after the immobilization process (Biomassa-APTES-CalB-GA biocatalyst)
achieved greater retention of enzymatic activity after transfer with NaCl (Relative activity:
55.2%) and Triton X-100 (Relative activity: 82 .3%). This evidences the formation of Schiff
bases between enzyme-support, due to the high relative activity of the enzyme after both
desorption processes. Thus, with the immobilization processes, active and stable biocatalysts
were produced, mainly in the case of the second system, with potential application in actions
of industrial interest. |
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