Different strategies for the lipase immobilization on the chitosan based supports and their applications

Rafiee, Fatemeh; Rezaee, Malahat

doi:10.1016/j.ijbiomac.2021.02.198

Cited by 103 publications

(55 citation statements)

References 366 publications

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“…This makes the opening of the lipase by other external interfaces unnecessary, and it becomes a guarantee of the immobilization of the lipases in the monomeric and open form [3]. In some cases, like lipase B from Candida antarctica the lid is very small and does not cover the whole active site but in some other cases like lipase LipA from Bacillus subtilis, there is not lid domain is present and the active-site [27][28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Free

Remonatto

Oliveira²,

Guisán

et al. 2022

Appl Biochem Biotechnol

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Lipases are an important group of biocatalysts for many industrial applications. Two new commercial low-cost lipases Eversa® Transform and Eversa® Transform 2.0 was immobilized on four different hydrophobic supports: Lewatit-DVB, Purolite-DVB, Sepabeads-C18, and Purolite-C18. The performance of immobilized lipases was investigated in the transesterification of sunflower oil solvent-free in an anhydrous medium. Interesting results were obtained for both lipases and the four supports, but with Sepabeads support the lipases Eversa showed high catalytic activity. However, the more stable and efficient derivative was Eversa® Transform immobilized on Sepabeads C-18. A 98 wt% of ethyl ester of fatty acid (FAEE) was obtained, in 3 h at 40ºC, ethanol/sunflower oil molar ratio of 3:1 and a 10 wt% of the immobilized biocatalyst. After 6 reaction cycles, the immobilized biocatalyst preserved 70 wt% of activity. Both lipases immobilized in Sepabeads C-18 were highly active and stable in the presence of ethanol. The immobilization of Eversa Transform and Eversa Transform 2.0 in hydrophobic supports described in this study appears to be a promising alternative to the immobilization and application of these news lipases still unexplored.

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Section: Introductionmentioning

confidence: 99%

Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Free

Remonatto

Oliveira²,

Guisán

et al. 2022

Appl Biochem Biotechnol

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“…PEI can form covalent bonds with lipases by adding bifunctional agents as well [ 11 , 12 ]. Another cationic polymer, chitosan (CS), has been used to directly support or entrap lipases and showed promising results in maintaining lipase activity [ 13 ]. To apply these polymers in crosslinking enzymes, two concerns should be carefully addressed, i.e., how do their characteristics, such as molecular weight (MW), functional group, etc., affect the coating/crosslinking efficiency and intensity?…”

Section: Introductionmentioning

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

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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.

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“…There are many methods for enzymatic immobilization, such as covalent bonding, cross-linking, adsorption, and encapsulation methods [ 28 ]. Among these methods, covalent bonding of the enzyme onto the support is the most practical method.…”

Section: Introductionmentioning

confidence: 99%

“…Among these methods, covalent bonding of the enzyme onto the support is the most practical method. It has more attention due to the firm interaction between the enzyme and the support materials, inhibiting the enzyme leakage from the support and increasing enzyme stability [ 13 , 28 , 29 ]. To carry out lipase immobilization, nano-scale magnetic carbon nanotubes (mCNTs) have been widely investigated by researchers.…”

Section: Introductionmentioning

confidence: 99%

Co-Immobilization of Rhizopus oryzae and Candida rugosa Lipases onto mMWCNTs@4-arm-PEG-NH2—A Novel Magnetic Nanotube–Polyethylene Glycol Amine Composite—And Its Applications for Biodiesel Production

Abdulmalek

Wang

et al. 2021

IJMS

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This article describes the successful synthesis of a novel nanocomposite of superparamagnetic multi-walled nanotubes with a four-arm polyethylene glycol amine polymer (mMWCNTs@4-arm-PEG-NH2). This composite was then employed as a support for the covalent co-immobilization of Rhizopus oryzae and Candida rugosa lipases under appropriate conditions. The co-immobilized lipases (CIL-mMWCNTs@4-arm-PEG-NH2) exhibited maximum specific activity of 99.626U/mg protein, which was 34.5-fold superior to that of free ROL, and its thermal stability was greatly improved. Most significantly, CIL-mMWCNTs@4-arm-PEG-NH2 was used to prepare biodiesel from waste cooking oil under ultrasound conditions, and within 120 min, the biodiesel conversion rate reached 97.64%. This was due to the synergy effect between ROL and CRL and the ultrasound-assisted enzymatic process, resulting in an increased biodiesel yield in a short reaction time. Moreover, after ten reuse cycles, the co-immobilized lipases still retained a biodiesel yield of over 78.55%, exhibiting excellent operational stability that is attractive for practical applications. Consequently, the combined use of a novel designed carrier, the co-immobilized lipases with synergy effect, and the ultrasound-assisted enzymatic reaction exhibited potential prospects for future applications in biodiesel production and various industrial applications.

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Different strategies for the lipase immobilization on the chitosan based supports and their applications

Cited by 103 publications

References 366 publications

Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Free

Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Free

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

Co-Immobilization of Rhizopus oryzae and Candida rugosa Lipases onto mMWCNTs@4-arm-PEG-NH2—A Novel Magnetic Nanotube–Polyethylene Glycol Amine Composite—And Its Applications for Biodiesel Production

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