Immobilization of lipases in hydrophobic chitosan for selective hydrolysis of fish oil: The impact of support functionalization on lipase activity, selectivity and stability

Urrutia, Paulina; Arrieta, Roy; Alvarez, L.; Cárdenas, Constanza; Mesa, Mónica; Wilson, Lorena

doi:10.1016/j.ijbiomac.2017.12.062

Cited by 63 publications

(27 citation statements)

References 63 publications

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“…A similar result was obtained from the chitosan-coated DSO3, ZGC351MB, and ZGC35 resins, which exhibited a resin bond with the NH 2 group (Jin and Bai, 2002). The intensity was also changed due to the deformation of the C-H bond and the support's alkyl chain (Urrutia et al, 2017). An immobilization process that occurred in the reaction was able to distract the chain of enzyme or support.…”

Section: Fourier Transform Infrared Spectrometry Analysissupporting

confidence: 73%

Effect of Additional Amino Group to Improve the Performance of Immobilized Lipase From Aspergillus niger by Adsorption-Crosslinking Method

et al. 2021

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Adsorption-crosslinking is one of the immobilization methods to improve the reusability of lipase. It requires amino groups to reduce cross-link immobilization risk so that lipase–support interaction increases and the immobilization is attainable. Also, the amino group on the support is expected to increase lipase performance. This study aimed to analyze the effect of amino group addition on immobilized Aspergillus niger lipase by the adsorption-crosslinking using MP-64 macroporous anion resin and XAD-7HP macroporous nonionic resin that has been treated with chitosan. The chitosan-coated resin was characterized by Fourier transform infrared spectrometry (FTIR) and scanning electron microscope (SEM). Lipase immobilization was carried out by adding 10 ml lipase solution containing 0.75 g resins and shaken at 25°C for 150 rpm. Adsorption was achieved for 4 h, followed by cross-linking separately (adding 0.5% (v/v) glutaraldehyde and re-reacting for 20 min). Lipase activity was measured with the titrimetric of olive oil emulsion; mixed with Aspergillus niger lipase, emulsion, and a buffer solution (pH 6.5, ionic strength of 0.7); and incubated for 30 min at 37°C. The effect of amino-functional groups was investigated based on lipase loading and lipase activity. The best lipase loading and lipase activity of 83.79% and 29.41 U/g support were achieved in the adsorption-crosslinking using MP-64 resin coated with chitosan. After four cycles, biodiesel synthesis was maintained at 70.61% of the initial yield. These results indicated that chitosan as an affordable and readily available source of amino groups could be used to modify support for Aspergillus niger lipase immobilization.

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Section: Fourier Transform Infrared Spectrometry Analysissupporting

confidence: 73%

Effect of Additional Amino Group to Improve the Performance of Immobilized Lipase From Aspergillus niger by Adsorption-Crosslinking Method

et al. 2021

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“…Results are not outstanding because it is well known that temperature, pH and saline concentration are influencing factors on enzymes [33–35]. Sensibility to temperature is related to the activation energy for enzymatic reaction [36]. Our results indicate a significate influence in temperature, pH, saline concentration, and speed.…”

Section: Resultsmentioning

confidence: 61%

Chitosan–heparin functionalised magnetic nanoparticles for the magnetic recovery of Aspergillus niger lipase enzyme

Pérez-Guzmán

Ilyiná

Zugasti–Cruz

et al. 2019

Micro & Nano Letters

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This work focuses on the obtention of magnetic nanoparticles functionalised with heparin (MNPH) and their interaction with Aspergillus niger lipase enzyme. The MNPH were obtained by the coprecipitation method, its characterisation was carried out by Fourier transform infrared spectroscopy, X-ray diffraction, and alternating gradient magnetometry. Functionalisation with heparin was carried out by ultrasound at various times, later the absorption of the enzyme was carried out with two temperatures 4 and 25°C at different concentrations of lipase. For the recovery of the enzyme, a Plackett-Burman design was used, which indicates that the recovered lipase maintains its enzymatic activity when the ionic strength is lower, it was characterised by sodium dodecyl sulphate-page with which it is demonstrated that it is possible to recover the lipase enzyme through the designed nanostructured system.

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“…This result indicated that the attachment of SrtA onto the chitosan surface had no improvement effect for its thermal stability. This phenomenon may be caused by the change of enzyme conformation because of strong random multipoint covalent interaction between the enzyme and the chitosan carrier, which reduced the enzyme’s operational stability [ 50 , 51 ].…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Staphylococcus aureus Sortase A on Chitosan Particles and Its Applications in Peptide-to-Peptide Ligation and Peptide Cyclization

et al. 2018

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Chitosan macro-particles prepared by the neutralization method were applied to Sortase A (SrtA) immobilization using glutaraldehyde as a crosslinking agent. The particles were characterized by Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). Response surface methodology (RSM) was employed to optimize the immobilization process. An average specific activity of 3142 U (mg protein)−1 was obtained under optimized immobilization conditions (chitosan concentration 3%, SrtA concentration 0.5 mg·mL−1, glutaraldehyde concentration 0.5%, crosslinking and immobilization at 20 °C, crosslinking for 3 h, and an immobilization time of 8 h). The transpeptidase activity of immobilized SrtA was proved by a peptide-to-peptide ligation with a conversion yield approximately at 80%, and the immobilized catalyst was successfully reused for five cycles without obvious activity loss. Moreover, the scale-up capability of using immobilized SrtA to catalyze a head-to-tail peptide cyclization was investigated in a batch reaction and the conversion yield was more than 95% when using 20 mg of peptide as a substrate.

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Immobilization of lipases in hydrophobic chitosan for selective hydrolysis of fish oil: The impact of support functionalization on lipase activity, selectivity and stability

Cited by 63 publications

References 63 publications

Effect of Additional Amino Group to Improve the Performance of Immobilized Lipase From Aspergillus niger by Adsorption-Crosslinking Method

Effect of Additional Amino Group to Improve the Performance of Immobilized Lipase From Aspergillus niger by Adsorption-Crosslinking Method

Chitosan–heparin functionalised magnetic nanoparticles for the magnetic recovery of Aspergillus niger lipase enzyme

Immobilization of Staphylococcus aureus Sortase A on Chitosan Particles and Its Applications in Peptide-to-Peptide Ligation and Peptide Cyclization

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