Turning biomass into functional composite materials: Rice husk for fully renewable immobilized biocatalysts

Spennato, Mariachiara; Todea, Anamaria; Corîci, Livia; Asaro, Fioretta; Cefarin, Nicola; Savonitto, Gilda; Deganutti, Caterina; Gardossi, Lucia

doi:10.1016/j.bioeco.2021.100008

Cited by 12 publications

(8 citation statements)

References 39 publications

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“…The activity of covalently immobilized CalB was measured using the tributyrin as substrate as previously described [30] …”

Section: Methodsmentioning

confidence: 99%

“…The activity of covalently immobilized CalB was measured using the tributyrin as substrate as previously described. [30] Enzymatic polycondensation of azelaic acid and glycerol using a thin-film reaction system…”

Section: Physical Immobilization Of Lipase Tllmentioning

confidence: 99%

“…More than 98 % of protein was immobilized and it was verified that there was no enzyme leaching from the support using a method previously reported. [30] The same protocol was used for the immobilization of TLL and ROL, by loading 50000 U per gram of dry resin.…”

Section: Covalent Immobilization Of Lipasesmentioning

confidence: 99%

“…The physical immobilization of TLL was carried out on milled rice husk according to the method described previously. [30] Activity assay for immobilized CalB lipase…”

Section: Physical Immobilization Of Lipase Tllmentioning

confidence: 99%

“…The spontaneous hydrolysis test was performed by preparing an emulsion using milliQ water (23.4 mL), gum arabic suspension (5.1 mL; prepared as previously described for the tributyrin test [30] ) and oligoester sample (1.5 mL). 0.1 m pH 5 acetate buffer (2 mL) was added and the titration was performed for 8 h at 31 °C by using 0.1 m aqueous NaOH solution as titrant.…”

Section: Esi-ms Analysismentioning

confidence: 99%

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Rational Guidelines for the Two‐Step Scalability of Enzymatic Polycondensation: Experimental and Computational Optimization of the Enzymatic Synthesis of Poly(glycerolazelate)

et al. 2022

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The lipase‐catalyzed polycondensation of azelaic acid and glycerol is investigated according to a Design‐of‐Experiment approach that helps to elucidate the effect of experimental variables on monomer conversion, Mn and regioselectivity of acylation of glycerol. Chemometric analysis shows that after 24 h the reaction proceeds regardless of the presence of the enzyme. Accordingly, the biocatalyst was removed after a first step of synthesis and the chain elongation continued at 80 °C. That allowed the removal of the biocatalyst and the preservation of its activity: pre‐requites for efficient applicability at industrial scale. The experimental study, combined with docking‐based computational analysis, provides rational guidelines for the optimization of the regioselective acylation of glycerol. The process is scaled up to 73.5 g of monomer. The novelty of the present study is the rigorous control of the reaction conditions and of the integrity of the immobilized biocatalyst, which serve to avoiding any interference of free enzyme or fines released in the reaction mixture. The quantitative analysis of the effect of experimental conditions and the overcoming of some major technical bottlenecks for the scalability of enzymatic polycondensation opens new scenarios for industrial exploitation.

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“…The activity of covalently immobilized CalB was measured using the tributyrin as substrate as previously described [30] …”

Section: Methodsmentioning

confidence: 99%

Section: Physical Immobilization Of Lipase Tllmentioning

confidence: 99%

Section: Covalent Immobilization Of Lipasesmentioning

confidence: 99%

“…The physical immobilization of TLL was carried out on milled rice husk according to the method described previously. [30] Activity assay for immobilized CalB lipase…”

Section: Physical Immobilization Of Lipase Tllmentioning

confidence: 99%

Section: Esi-ms Analysismentioning

confidence: 99%

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