Immobilization of Pseudomonas fluorescens lipase on chitosan crosslinked with polyaldehyde starch for kinetic resolution of sec-alcohols

Santos, Leandro Alves dos; Alnoch, Robson Carlos; Soares, Glêydison Amarante; Mitchell, David A.; Krieger, Nádia

doi:10.1016/j.procbio.2022.10.014

Cited by 12 publications

(3 citation statements)

References 62 publications

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“…In this study, enzyme immobilization to chitosan support cross-linked with glutaraldehyde was preferred. Chitosan, a natural biopolymer derived from the deacetylation of chitin, has gained significant attention in recent years as an attractive option for enzyme immobilization due to its cost-effectiveness (dos Santos et al, 2022;Guz et al, 2023). On the other hand, covalent enzyme immobilization protocols usually begin with support modification or an activation step.…”

Section: Introductionmentioning

confidence: 99%

Production of high quality biodiesel from sunflower soapstock acid oil as novel feedstock: Catalyzed by immobilized pancreatic lipase

Paluzar

2023

J Americ Oil Chem Soc

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Edible refined oils, which are utilized as raw materials in biodiesel production, have been replaced by by‐products (acid oil, fatty acid, deodorized distillate, and soapstock distillates) obtained from the vegetable oil refining industry, in recent years. This study aims to investigate the production of high quality biodiesel fuel in accordance with the standards (TS EN and ASTM) from sunflower soapstock acid oil. This feedstock was donated by an oil factory in the Thrace region, Turkey. Esterification reaction was performed by immobilized enzyme. For this, immobilization was carried out by covalent binding of pancreatic lipase in glutaraldehyde activated chitosan and optimum immobilization conditions were determined. The activity of the immobilized lipase and the retained activity were found to be 65.69 U/μg and 61.8%, respectively (pH: 7.5, 37°C). The Km (Michealis constant) and Vmax (maximum velocity of an enzymatically catalyzed reaction) values of the immobilized enzyme were found to be 5.1 mmol/L and 48.6 U/min/mg protein, respectively. The immobilized enzyme was employed as a biocatalyst for esterification of sunflower soapstock acid oil. Notably, an impressive yield of 75.6% was attained under the conditions of a 1:5 molar ratio of soapstock acid oil to methanol, with 10 wt% immobilized lipase as the catalyst, and a reaction temperature of 45°C for 36 h. The resulting biodiesel exhibits fuel characteristics that meet the standards outlined in TS EN 14214:2012 + A2 and ASTM D6751‐02.

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Section: Introductionmentioning

confidence: 99%

Production of high quality biodiesel from sunflower soapstock acid oil as novel feedstock: Catalyzed by immobilized pancreatic lipase

Paluzar

2023

J Americ Oil Chem Soc

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“…but only a few specified the stability in the presence of polar solvents. [12][13][14][15] It is often considered that polar solvents reduce water activity for the enzyme by removing the water-solvating layer on the surface of the enzyme eventually leading to the destabilization of the lipase. [14].…”

Section: Introductionmentioning

confidence: 99%

“…[12][13][14][15] It is often considered that polar solvents reduce water activity for the enzyme by removing the water-solvating layer on the surface of the enzyme eventually leading to the destabilization of the lipase. [14]. The polar solvent stable lipase from Pseudomonas sp.VITCLP4 could be useful for reactions in low water medium.…”

Section: Introductionmentioning

confidence: 99%

Response surface optimization of solvent tolerant cold active lipase production by Pseudomonas sp. VITCLP4

Lakshimi,

Kavitha

2023

Preprint

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The yield of solvent-tolerant cold active lipase from halo-tolerant Pseudomonas sp. VITCLP4 was improved by applying statistical methods to precisely combine medium components and other conditions. Two-level Plackett–Burman (PB) design was utilized to screen the most significant variables from a set of eleven variables that influence lipase production. Analysis of variance revealed that Tween-80, peptone, and KH2PO4 were statistically significant. Optimum levels of selected variables were ascertained by one-factor-at-a-time (OFAT) analysis. The optimum values and interactive effects of the selected three components were established by response surface methodology (RSM) based on the face-centered central composite design (FCCCD) using a three-level-three-factor approach. The optimized medium containing Tween-80, 0.5% (v/v), peptone, 0.75% (w/v), KH2PO4, 0.05% (w/v), yeast extract, 0.1% (w/v), olive oil, 0.2% (v/v) and inoculum size, 0.2% (v/v) resulted in maximum lipase production of 1342 Units ml− 1 min− 1 with 7.8 fold increase in the yield. This study provides insights into enhancing the lipase production statistically with optimized resources that can be utilized in bioprocess studies and industrial applications.

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Response Surface Optimization of Solvent-Tolerant Cold-Active Lipase Production by Pseudomonas sp. VITCLP4

Iswareya Lakshimi,

Kavitha

2024

Catal Lett

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Immobilization of Pseudomonas fluorescens lipase on chitosan crosslinked with polyaldehyde starch for kinetic resolution of sec-alcohols

Cited by 12 publications

References 62 publications

Production of high quality biodiesel from sunflower soapstock acid oil as novel feedstock: Catalyzed by immobilized pancreatic lipase

Production of high quality biodiesel from sunflower soapstock acid oil as novel feedstock: Catalyzed by immobilized pancreatic lipase

Response surface optimization of solvent tolerant cold active lipase production by Pseudomonas sp. VITCLP4

Response Surface Optimization of Solvent-Tolerant Cold-Active Lipase Production by Pseudomonas sp. VITCLP4

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