Lipase immobilization on biodegradable film with sericin

Castro, Michael da Conceição de; Garcia, Patrícia Salomão; Andrade, Milena Martins; Grossmann, Maria Victória Eiras; Simões, Bruno Matheus; Samulewski, Rafael Block; Baron, Alessandra Machado

doi:10.1002/bab.2141

Cited by 5 publications

(3 citation statements)

References 41 publications

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“…The maximum yield was obtained at 49 • C, molar ratio oleic acid: Ethanol of 1:3, 1.25 g lipase film or 50 U (1.03 ± 0.03 mg protein), and 30 h of reaction. Even after seven use cycles, immobilized lipase showed a 52% reduction in ester yield [53].…”

Section: Immobilization On Different Pva Hybrid Supportsmentioning

confidence: 98%

“…The molecular weight of SS ranges from 24 to 400 kDa,12 and serine (32.3%),13 aspartic acid (16.71%), and glycine (13.49%) are the primary amino acids. This biomaterial enriches polymer mixtures reducing environmental damage due to its degradability [53]. This material, in combination with cassava starch and PVA, has been used to immobilize Botryosphaeria ribis (Br) lipase using a sandwich adsorption methodology.…”

Section: Immobilization On Different Pva Hybrid Supportsmentioning

confidence: 99%

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Immobilization of Lipases Using Poly(vinyl) Alcohol

Guajardo

2023

Polymers

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Lipases are very versatile enzymes because they catalyze various hydrolysis and synthesis reactions in a chemo-, regio-, and stereoselective manner. From a practical point of view, immobilization allows the recovery and stabilization of the biocatalyst for its application in different types of bioreactors. Among the various support options for immobilizing lipases is polyvinyl alcohol (PVA), which, when functionalized or combined with other materials, provides different characteristics and properties to the biocatalyst. This review analyzes the multiple possibilities that PVA offers as a material to immobilize lipases when combined with alginate, chitosan, and hydroxypropylmethylcellulose (HPMC), incorporating magnetic properties together with the formation of fibers and microspheres. The articles analyzed in this review were selected using the Scopus database in a range of years from 1999 to 2023, finding a total of 42 articles. The need to expand knowledge in this area is due to the great versatility and scaling possibilities that PVA has as a support for lipase immobilization and its application in different bioreactor configurations.

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Section: Immobilization On Different Pva Hybrid Supportsmentioning

confidence: 98%

Section: Immobilization On Different Pva Hybrid Supportsmentioning

confidence: 99%

Immobilization of Lipases Using Poly(vinyl) Alcohol

Guajardo

2023

Polymers

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“…16,17 CALB is very special, having a peculiar mechanism of action. Compared with other lipases, 18,19 CALB does not have a "lid" structure and has a wider substrate selectivity. The catalysis of CALB follows the Ping Pong Bi-Bi mechanism, during which the enzyme goes through the process of free enzyme-transition state 1-acylase intermediatetransition state 2-free enzyme.…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of diisooctyl 2,5‐furandicarboxylate by Candida antarctica lipase B (CALB) immobilized on a macroporous epoxy resin

Mang

Zhou

et al. 2023

Biotech and App Biochem

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Diisooctyl 2,5‐furandicarboxylate (DEF), an ester derivative of 2,5‐furandicarboxylic acid (FDCA, a bio‐based platform chemical), resembles the physical and chemical properties of phthalates. Due to its excellent biodegradability, DEF is considered a safer alternative to the hazardous phthalate plasticizers. Although FDCA esters are currently mainly produced by chemical synthesis, the enzymatic synthesis of DEF is a green, promising alternative. The current study investigated the biosynthesis of DEF by Candida antarctica lipase B (CALB) immobilized on macroporous resins. Out of five macroporous resins (NKA‐9, LX‐1000EP, LX‐1000HA, XAD‐7HP, and XAD‐8) evaluated, the LX‐1000EP epoxy resin was identified as the best carrier for CALB, and the XAD‐7HP weakly polar resin was identified as the second best. The optimal immobilization conditions were as follows: CALB (500 μL) and LX‐1000EP (0.1 g) were incubated in phosphate butter (20 mM, pH 6.0) for 10 h at 35°C. The resulting immobilized CALB (EP‐CALB) showed an activity of 639 U/g in the hydrolysis of p‐nitrophenyl acetate, with an immobilization efficiency of 87.8% and an activity recovery rate of 56.4%. Using 0.02 g EP‐CALB as the catalyst in 10 mL toluene, and the molar ratio of 2,5‐dimethyl furanediformate (1 mmol/mL) and isooctyl alcohol (4 mmol/mL) that was 1:4, a DEF conversion rate of 91.3% was achieved after a 24‐h incubation at 50°C. EP‐CALB had similar thermal stability and organic solvent tolerance compared to Novozym 435, and both were superior to CALB immobilized on the XAD‐7HP resin. EP‐CALB also exhibited excellent operational stability, with a conversion rate of 52.6% after 10 repeated uses. EP‐CALB could be a promising alternative to Novozym 435 in the biomanufacturing of green and safe plasticizers such as DEF.

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