High stabilization of immobilized Rhizomucor miehei lipase by additional coating with hydrophilic crosslinked polymers: Poly-allylamine/Aldehyde–dextran

Cejudo-Sanches, Janaina; Orrego, Alejandro H.; Jaime-Mendoza, Adriana; Ghobadi, Roohollah; Moreno-Pérez, Sonia; Fernández‐Lorente, Gloria; Rocha-Martín, Javier

doi:10.1016/j.procbio.2020.02.026

Cited by 17 publications

(6 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Their conformations of lipase attaching on hydrophilic support became highly stable. Thus, immobilised lipase showed higher enzyme activity than when it was used in the free form [27]. Based on specific activity, it was implied that the GAL bead could be entrapped lipase at about 0.48 U/g support, while 0.46 U of lipase could be absorbed within PAL 1 g. Furthermore, the highest immobilisation efficiency of GAL (97.61%) and PAL (98.30%) beads were observed.…”

Section: Lipase Activity and Immobilisation Yieldmentioning

confidence: 95%

Entrapping Immobilisation of Lipase on Biocomposite Hydrogels toward for Biodiesel Production from Waste Frying Acid Oil

2020

View full text Add to dashboard Cite

A new application of biocomposite hydrogels named gelatin-alginate (GA) and pectin alginate (PA) enables the use of the hydrogels as carriers for lipase entrapment during biodiesel production. Waste frying acid oil (WFAO), a raw material, was converted to biodiesel via an esterification reaction catalysed by two different immobilised biocatalysts: gelatin-alginate lipase (GAL) and pectin-alginate lipase (PAL). The highest immobilisation yield of GAL and PAL beads was achieved at 97.61% and 98.30%, respectively. Both of them gave biodiesel yields in the range of 75–78.33%. Furthermore, capability and reusability of biocatalysts were improved such that they could be reused up to 7 cycles. Moreover, the predicted biodiesel properties met the European biodiesel standard (EN14214). Interestingly, entrapped lipase on composite hydrogels can be used as an alternative catalyst choice for replacing the chemical catalyst during the biodiesel production.

show abstract

Section: Lipase Activity and Immobilisation Yieldmentioning

confidence: 95%

Entrapping Immobilisation of Lipase on Biocomposite Hydrogels toward for Biodiesel Production from Waste Frying Acid Oil

2020

View full text Add to dashboard Cite

show abstract

“…TLL is a typical lipase requiring interfacial activation, as its active center is covered by a lid composed of hydrophobic residues, which renders TLL more capable of hydrolyzing long-chain substrates [ 21 ]. p-Nitrophenyl butyrate (NPB) is a water-soluble short-chain substrate for esterase, and it is widely used in many works [ 24 , 25 , 26 , 27 ] to monitor the hydrolytic activity of lipases. p-Nitrophenyl palmitate (NPP) is a long-chain substrate for lipase, which is commonly applied in an emulsion or is dissolved in organic solvents, such as heptane [ 28 ].…”

Section: Resultsmentioning

confidence: 99%

Characteristics of Crosslinking Polymers Play Major Roles in Improving the Stability and Catalytic Properties of Immobilized Thermomyces lanuginosus Lipase

Mao

Cai

Zhou

et al. 2022

IJMS

View full text Add to dashboard Cite

This study aimed to improve the stability and catalytic properties of Thermomyces lanuginosus lipase (TLL) adsorbed on a hydrophobic support. At the optimized conditions (pH 5 and 25 °C without any additions), the Sips isotherm model effectively fitted the equilibrium adsorption data, indicating a monolayer and the homogenous distribution of immobilized lipase molecules. To preserve the high specific activity of adsorbed lipase, the immobilized lipase (IL) with a moderate loading amount (approximately 40% surface coverage) was selected. Polyethylenimine (PEI) and chitosan (CS) were successfully applied as bridging units to in situ crosslink the immobilized lipase molecules in IL. At the low polymer concentration (0.5%, w/w) and with 1 h incubation, insignificant changes in average pore size were detected. Short-chain PEI and CS (MW ≤ 2 kDa) efficiently improved the lipase stability, i.e., the lipase loss decreased from 40% to <2%. Notably, CS performed much better than PEI in maintaining lipase activity. IL crosslinked with CS-2 kDa showed a two- to three-fold higher rate when hydrolyzing p-nitrophenyl butyrate and a two-fold increase in the catalytic efficiency in the esterification of hexanoic acid with butanol. These in situ crosslinking strategies offer good potential for modulating the catalytic properties of TLL for a specific reaction.

show abstract

“…The association of these agents and the immobilization of the lipase on the support provides the formation of a biocatalyst with large enzyme planar aggregates simultaneously interacting with the support at multiple sites. [103][104][105][106] Therefore, to achieve desorption of the lipase, it will be necessary to release all the enzyme molecules forming each planar physical or chemical aggregate, which is much more difficult than the release of a single lipase protein. Another advantage of crosslinking with physical or chemical agents is the modulation of catalytic properties and, in some cases, improvements in the stability of the biocatalyst.…”

Section: Problems Of Lipase Immobilization On Hydrophobic Supportsmentioning

confidence: 99%

A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles

Guimarães,

Oliveira,

Gonçalves

et al. 2023

React. Chem. Eng.

View full text Add to dashboard Cite

show abstract

High stabilization of immobilized Rhizomucor miehei lipase by additional coating with hydrophilic crosslinked polymers: Poly-allylamine/Aldehyde–dextran

Cited by 17 publications

References 47 publications

Entrapping Immobilisation of Lipase on Biocomposite Hydrogels toward for Biodiesel Production from Waste Frying Acid Oil

Entrapping Immobilisation of Lipase on Biocomposite Hydrogels toward for Biodiesel Production from Waste Frying Acid Oil

Characteristics of Crosslinking Polymers Play Major Roles in Improving the Stability and Catalytic Properties of Immobilized Thermomyces lanuginosus Lipase

A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles

Contact Info

Product

Resources

About