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

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 en...

Celý popis

Uloženo v:
Podrobná bibliografie
Vydáno v:Biotechnology and applied biochemistry Ročník 69; číslo 2; s. 479 - 491
Hlavní autoři: Cutiño‐Avila, Bessy V., Sánchez‐López, María I., Cárdenas‐Moreno, Yosberto, González‐Durruthy, Michael, Ramos‐Leal, Miguel, Guerra‐Rivera, Gilda, González‐Bacerio, Jorge, Guisán, José M., Ruso, Juan M., Monte‐Martínez, Alberto
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States Wiley Subscription Services, Inc 01.04.2022
Témata:
Algorithms
Biocatalysts
Bioconversion
Bioinformatics
colorant bioconversion
Coloring agents
covalent immobilization
Enzymatic activity
Enzyme activity
Enzyme Stability
Enzymes
Enzymes, Immobilized - metabolism
Hydrogen-Ion Concentration
Immobilization
immobilized derivative activity
Laccase
Laccase - metabolism
Maxima
Polyporaceae
Predictions
Proteins
rational design of immobilized derivatives strategy
Sepharose - analogs & derivatives
Substrates
Trametes
Trametes maxima
Wastewater treatment
covalent immobilization
colorant bioconversion
laccase
rational design of immobilized derivatives strategy
immobilized derivative activity
ISSN:0885-4513, 1470-8744, 1470-8744
On-line přístup:Získat plný text
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
Popis
Shrnutí: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.
Bibliografie:www.wileyonlinelibrary.com
.
Supporting Information is available in the online issue at
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
ISSN:0885-4513
1470-8744
1470-8744
DOI:10.1002/bab.2125