The immobilization of an endoglucanase, benzoylformate decarboxylase (BFD) from Pseudomonas putida, as well as of lipase B from Candida antarctica (CALB) onto the carrier supports Sepabeads EC-EP, Sepabeads EC-EA, and Sepabeads EC-BU was accomplished. It is shown that via these immobilized biocatalysts the synthesis of both fine and bulk chemicals is possible. This is illustrated by the syntheses of polyglycerol esters and (S)-hydroxy phenyl propanone. The benefit of immobilization is illustrated by repetitive use in a bubble column reactor as well as in a stirred tank reactor. High stability of two biocatalysts was achieved and reusability up to eight times was demonstrated. The comparison of CALB immobilized on Sepabeads EC-EP to Novozym 435 shows similar activity.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s00449-008-0199-3DOI Listing

Publication Analysis

Top Keywords

immobilized sepabeads
8
sepabeads ec-ep
8
sepabeads
5
practical application
4
application enzymes
4
enzymes immobilized
4
sepabeads immobilization
4
immobilization endoglucanase
4
endoglucanase benzoylformate
4
benzoylformate decarboxylase
4

Similar Publications

Enhancing rhamnolipid production via immobilized Pseudomonas stutzeri lipase: A comparative study.

Bioorg Chem

December 2024

Department of Chemistry in Pharmaceutical Sciences, Faculty of Pharmacy, Complutense University of Madrid, Plaza Ramón y Cajal, E 28040 Madrid, Spain. Electronic address:

Rhamnolipids (RLs) are widely studied biosurfactants with significant industrial potential in cosmetics, pharmaceuticals, and bioremediation due to their excellent surface activity, emulsifying properties and bioactive characteristics. However, high production costs impede their mass production. This study investigates the immobilization of Pseudomonas stutzeri lipase (PSL) on various supports to enhance RL synthesis efficiency, focusing on yield and regioselectivity in the enzymatic synthesis of 4-O-lauroylrhamnose by the transesterification of rhamnose with vinyl laurate.

View Article and Find Full Text PDF

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

Appl Biochem Biotechnol

May 2022

Departamento de Biotecnología y Microbiología de los Alimentos, Instituto de Alimentación, CIAL (CSIC-UAM), Madrid, Spain.

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.

View Article and Find Full Text PDF

Microbial lipase: a new approach for a heterogeneous biocatalyst.

Prep Biochem Biotechnol

September 2021

Department of Engineering Bioprocesses and Biotechnology, School of Pharmaceutical Sciences, São Paulo State University (UNESP), Araraquara, Brazil.

Lipases are enzymes employed in several industrial process and their applicability can be increased if these biocatalysts are in the immobilize form. The objective of this work was to study the immobilization of lipase produced by submerged cultivation of sp. by hydrophobic interaction, evaluating its stability and reuse capacity.

View Article and Find Full Text PDF

Immobilization of the glucose isomerase from Caldicoprobacter algeriensis on Sepabeads EC-HA and its efficient application in continuous High Fructose Syrup production using packed bed reactor.

Food Chem

March 2020

Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS), University of Sfax, Road of Sidi Mansour Km 6, PO Box 1177, Sfax 3018, Tunisia. Electronic address:

The glucose isomerase GICA from Caldicoprobacter algeriensis was immobilized by ionic adsorption on polymethacrylate carriers (Sepabeads EC-EA and EC-HA) or covalent attachment to glyoxal agarose. The Sepabeads EC-HA yielded the highest recovery of activity (89%). The optimum temperature and pH of immobilized GICA were 90 °C and 7.

View Article and Find Full Text PDF

Biochemical characterization and application of a new lipase and its cognate foldase obtained from a metagenomic library derived from fat-contaminated soil.

Int J Biol Macromol

September 2019

Departamento de Química, Universidade Federal do Paraná, Cx. P. 19032, Centro Politécnico, Curitiba 81531-980, Paraná, Brazil. Electronic address:

LipMF3 is a new lipase isolated from a metagenomic library derived from a fat-contaminated soil. It belongs to the lipase subfamily I.1 and has identities of 68% and 67% with lipases of Chromobacterium violaceum and C.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!