RT Journal Article
T1 Modeling and experimental validation of covalent immobilization of Trametes maxima laccase on glyoxyl and MANA-Sepharose CL 4B supports, for the use in bioconversion of residual colorants
A1 Cutiño-Avila, Bessy V.
A1 Sánchez-López, María I.
A1 Cárdenas-Moreno, Yosberto
A1 González Durruthy, Michael
A1 Ramos-Leal, Miguel
A1 Guerra-Rivera, Gilda
A1 González-Bacerio, Jorge
A1 Guisán, José M.
A1 Ruso Beiras, Juan Manuel
A1 Monte-Martínez, Alberto del
K1 Colorant bioconversion
K1 Covalent immobilization
K1 Immobilized derivative activity
K1 Laccase
K1 Rational design of immobilized derivatives strategy
AB Our novel strategy for the rational design of immobilized derivatives (RDID) is directed to predict the behavior of the protein immobilized derivative before its synthesis, by the usage of mathematic algorithms and bioinformatics tools. However, this approach needs to be validated for each target enzyme. The objective of this work was to validate the RDID strategy for covalent immobilization of the enzyme laccase from Trametes maxima MUCL 44155 on glyoxyl- and monoaminoethyl-N-aminoethyl (MANA)-Sepharose CL 4B supports. Protein surface clusters, more probable configurations of the protein–supports systems at immobilization pHs, immobilized enzyme activity, and protein load were predicted by RDID1.0 software. Afterward, immobilization was performed and predictions were experimentally confirmed. As a result, the laccase-MANA-Sepharose CL 4B immobilized derivative is better than laccase-glyoxyl-Sepharose CL 4B in predicted immobilized derivative activity (63.6% vs. 29.5%). Activity prediction was confirmed by an experimentally expressed enzymatic activity of 68%, using 2,6-dimethoxyphenol as substrate. Experimental maximum protein load matches the estimated value (11.2 ± 1.3 vs. 12.1 protein mg/support mL). The laccase-MANA-Sepharose CL 4B biocatalyst has a high specificity for the acid blue 62 colorant. The results obtained in this work suggest the possibility of using this biocatalyst for wastewater treatment.
PB Wiley
YR 2021
FD 2021-02-09
LK https://hdl.handle.net/10347/44185
UL https://hdl.handle.net/10347/44185
LA eng
NO Cutiño-Avila BV, Sánchez-López MI, Cárdenas-Moreno Y, et al. Modeling and experimental validation of covalent immobilization of Trametes maxima laccase on glyoxyl and MANA-Sepharose CL 4B supports, for the use in bioconversion of residual colorants. Biotechnol. Appl. Biochem. 2022; 69: 479–491. https://doi.org/10.1002/bab.2125
NO This is the peer reviewed version of the following article:  Cutiño-Avila BV, Sánchez-López MI, Cárdenas-Moreno Y, et al. Modeling and experimental validation of covalent immobilization of Trametes maxima laccase on glyoxyl and MANA-Sepharose CL 4B supports, for the use in bioconversion of residual colorants. Biotechnol. Appl. Biochem. 2022; 69: 479–491, which has been published in final form at https://doi.org/10.1002/bab.2125. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. This article may not be enhanced, enriched or otherwise transformed into a derivative work, without express permission from Wiley or by statutory rights under applicable legislation. Copyright notices must not be removed, obscured or modified. The article must be linked to Wiley’s version of record on Wiley Online Library and any embedding, framing or otherwise making available the article or pages thereof by third parties from platforms, services and websites other than Wiley Online Library must be prohibited.
DS Minerva
RD 23 abr 2026