Enhancing rhamnolipid production via immobilized Pseudomonas stutzeri lipase: A comparative study DOI Creative Commons
Guillermo Cruz,

Cecilia García‐Oliva,

Almudena Perona

et al.

Bioorganic Chemistry, Journal Year: 2024, Volume and Issue: 153, P. 107855 - 107855

Published: Oct. 9, 2024

Rhamnolipids (RLs) are widely studied biosurfactants with significant industrial potential in cosmetics, pharmaceuticals, and bioremediation due to their excellent surface activity, emulsifying properties bioactive characteristics. However, high production costs impede mass production. This study investigates the immobilization of Pseudomonas stutzeri lipase (PSL) on various supports enhance RL synthesis efficiency, focusing yield regioselectivity enzymatic 4-O-lauroylrhamnose by transesterification rhamnose vinyl laurate. Three methods were compared: covalent binding, adsorption Celite, hydrophobic supports. The efficiency varied depending method used, lowest observed for Celite (56 %), followed Sepabeads (EC-EP/S 78 % EC-EP/L 70 highest (83-97 %, EC-OD being best at 97 %). For 4-O-lauroylrhamnose, Sepabeads™ EC-EP yielded low conversions restricted conformational freedom enzyme. Celite® 545 resulted moderate conversion rates, limited electrostatic interactions restricting enzyme activity. most promising results obtained supports, particularly Purolite® ECR8806F, achieving nearly complete maintaining 4-position both THF green solvent 2-methyltetrahydrofuran (2-MeTHF). highlights critical role support hydrophobicity active area immobilized performance. PSL ECR8806F demonstrated sustainable RLs production, showing reusability, stability productivity across multiple reaction cycles. presents a advancement optimizing conditions, facilitating way more cost-effective applications.

Language: Английский

A comprehensive review of lipase-catalyzed acidolysis as a method for producing structured glycerides DOI
Veymar G. Tacias-Pascacio, Pedro Abellanas-Pérez, Diandra de Andrades

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 142878 - 142878

Published: April 1, 2025

Language: Английский

Citations

2
A review of lipase immobilization on hydrophobic supports incorporating systematic mapping principles DOI Creative Commons
José Renato Guimarães, Kaíque Souza Gonçalves Cordeiro Oliveira, Maria Carolina Pereira Gonçalves

et al.

Reaction Chemistry & Engineering, Journal Year: 2023, Volume and Issue: 8(11), P. 2689 - 2702

Published: Jan. 1, 2023

A review of the literature covering research on immobilization lipases hydrophobic supports was performed using systematic mapping (SM) concepts.

Language: Английский

Citations

22
Propelling of Enzyme Activity by Using Different Triggering Strategies: Applications and Perspectives DOI Creative Commons
Gamze Dik, Büşra Bakar, Ahmet Ulu

et al.

Industrial & Engineering Chemistry Research, Journal Year: 2023, Volume and Issue: 62(36), P. 14111 - 14129

Published: Aug. 29, 2023

Enzymes have been widely used as biocatalysts to meet the increasing demand for industrial approaches. Even if method of immobilization stabilize enzymes seems easy and effective scientists, maintenance activity remains currently an open challenge in various applications. Activity enhancement has recently gained a huge interest since this is significant point terms In context, external stimulants such ultrasound, magnetic field, electric light irradiation affect enzyme different aspects. Among these, ultrasound induction exhibits prominent role immobilized enzyme. On other hand, although large number articles reported improvements catalytic activities by methods, best our knowledge, review describing these not yet reported. Therefore, novel focused on effects it will provide perspectives recent information development application related research areas. addition, give insight into mechanisms at molecular level response question how methods enhance activity.

Language: Английский

Citations

11
Optimization of the production of a lipase from Staphylococcus pasteuri and its immobilization/stabilization on a hydrophobic support DOI

TIOUCHE Amina,

Haddadi-Guemghar Hayate,

GUENDOUZ Naima

et al.

Process Biochemistry, Journal Year: 2025, Volume and Issue: unknown

Published: March 1, 2025

Language: Английский

Citations

0
ALGINATE COATED MgO-NPs IMPROVES THE STABILITY OF Kluyveromyces lactis β-GALACTOSIDASE FOR BIOTECHNOLOGICAL APPLICATIONS DOI Creative Commons
Shakeel Ahmed Ansari,

Rukhsana Satar,

Nadeem Ikram

et al.

Química Nova, Journal Year: 2023, Volume and Issue: unknown

Published: Jan. 1, 2023

The current study was undertaken to immobilize Kluveromyces lactis β-galactosidase on alginate coated magnesium oxide nanoparticles (ACMONPs). Transmission electron microscopy showed that MgO-NPs synthesized by wet chemical approach were of 27 nm size and spherical in shape. Excellent biocompatibility sodium resulted 90% immobilization yield for due covalent attachment. Soluble immobilized exhibited its pH temperature-optima at 7.0 40 oC, respectively. However, the enzyme attached ACMONPs enhanced activity higher lower temperature ranges, contrast solution. bound displayed greater under effect galactose mediated product inhibition as well reusability experiment. Our indicated 88% lactose hydrolyzed oC compared 71% soluble identical controlled batch reactors. Hence, this nanomatrix can find potential application continuous packed-bed reactors obtaining lactose-free dairy products.

Language: Английский

Citations

1
Synthesis and microencapsulation of acylglycerols rich in omega-3 PUFAs by glycerolysis using lipase immobilized on activated carbon DOI
Priscilla Amaral Nascimento, Jéssica Ferreira Borges, Annie Nolasco Alves

et al.

Journal of environmental chemical engineering, Journal Year: 2024, Volume and Issue: 12(6), P. 114617 - 114617

Published: Oct. 30, 2024

Language: Английский

Citations

0
Enhancing rhamnolipid production via immobilized Pseudomonas stutzeri lipase: A comparative study DOI Creative Commons
Guillermo Cruz,

Cecilia García‐Oliva,

Almudena Perona

et al.

Bioorganic Chemistry, Journal Year: 2024, Volume and Issue: 153, P. 107855 - 107855

Published: Oct. 9, 2024

Rhamnolipids (RLs) are widely studied biosurfactants with significant industrial potential in cosmetics, pharmaceuticals, and bioremediation due to their excellent surface activity, emulsifying properties bioactive characteristics. However, high production costs impede mass production. This study investigates the immobilization of Pseudomonas stutzeri lipase (PSL) on various supports enhance RL synthesis efficiency, focusing yield regioselectivity enzymatic 4-O-lauroylrhamnose by transesterification rhamnose vinyl laurate. Three methods were compared: covalent binding, adsorption Celite, hydrophobic supports. The efficiency varied depending method used, lowest observed for Celite (56 %), followed Sepabeads (EC-EP/S 78 % EC-EP/L 70 highest (83-97 %, EC-OD being best at 97 %). For 4-O-lauroylrhamnose, Sepabeads™ EC-EP yielded low conversions restricted conformational freedom enzyme. Celite® 545 resulted moderate conversion rates, limited electrostatic interactions restricting enzyme activity. most promising results obtained supports, particularly Purolite® ECR8806F, achieving nearly complete maintaining 4-position both THF green solvent 2-methyltetrahydrofuran (2-MeTHF). highlights critical role support hydrophobicity active area immobilized performance. PSL ECR8806F demonstrated sustainable RLs production, showing reusability, stability productivity across multiple reaction cycles. presents a advancement optimizing conditions, facilitating way more cost-effective applications.

Language: Английский

Citations

0