In this paper, we describe the facile preparation of a chiral catalyst by the combination of the amino acid, l-proline (Pro), and the enzyme, porcine pancreas lipase (PPL), immobilized on a microporous metal-organic framework (PPL-Pro@MOF). The multipoint immobilization of PPL onto the MOF is made possible with the aid of Pro, which also provided a chiral environment for enhanced enantioselectivity. The application of the microporous MOF is pivotal in maintaining the catalytic activity of PPL, wherein it prevented the leaching of Pro during the catalytic reaction, leading to the enhanced activity of PPL. The prepared biocatalyst was applied in asymmetric carbon-carbon bond formation, demonstrating the potential of this simple approach for chemical transformations.

Download full-text PDF

Source
http://dx.doi.org/10.1039/d0dt04081aDOI Listing

Publication Analysis

Top Keywords

multipoint immobilization
8
activity ppl
8
fast multipoint
4
immobilization lipase
4
chiral
4
lipase chiral
4
chiral l-proline
4
l-proline mof
4
mof chiral
4
chiral bioreactor
4

Similar Publications

Immobilized Horseradish Peroxidase on Enriched Diazo-Activated Silica Gel Harnessed High Biocatalytic Performance at a Steady State in Organic Solvent.

Langmuir

November 2024

Analytical and Bio-analytical Laboratory, Department of Chemistry, Visva-Bharati, Santiniketan, West Bengal, India 731235.

Dimethyldichlorosilane (DMDCS), an efficient silane coupling reagent appearing between the -OH groups of silica gel (SG) and picric acid, instantaneously produces a derivative enriched with nitro groups. The nitro group acting as an end-cap terminates the reaction and subsequently was converted into diazo to couple tyrosine's phenol ring via its -carbon, the inert center to immobilize horseradish peroxidase (HRP) in a multipoint mode. It maintains the status quo of the native enzyme's protein folding and the entire protein groups' chemistry.

View Article and Find Full Text PDF

Optimizing the activation of agarose beads with divinyl sulfone for enzyme immobilization and stabilization.

Int J Biol Macromol

December 2024

Departamento de Biocatálisis, ICP-CSIC, C/Marie Curie 2, Campus UAM-CSIC, Cantoblanco, 28049 Madrid. Spain. Electronic address:

The focus of the present work is to find the optimal conditions for the activation of agarose beads with divinyl sulfone (DVS). The reactivity of the vinyl sulfone groups in the support was checked by the support capacity to react with ethylamine; via elemental analysis. In addition, trypsin was used as a model enzyme to test the immobilization and stabilization capabilities of the different supports.

View Article and Find Full Text PDF

Activation of Inert Supports for Enzyme(s) Immobilization Harnessing Biocatalytic Sustainability for Perennial Utilization.

Langmuir

September 2024

Analytical and Bio-analytical Laboratory, Department of Chemistry, Visva-Bharati, Santiniketan, West Bengal, India 731235.

Although Nature's evolution and intelligence have gifted humankind with noteworthy enzyme candidates to simplify complex reactions with ultrafast, overselective, effortless, mild biological reactions for millions of years, their availability at minute-scale, short-range time-temperature stability, and purification costs hardly justify recycling/or reuse. Covalent immobilization, particularly via multipoint bonds, prevents denaturing, maintains activities for long-range time, pH, and temperature, and makes catalysts available for repetitive usages; which attracts researchers and industries to bring more immobilized enzyme contenders in science and commercial progressions. Inert-support activation, the most crucial step, needs appropriate activators; under mild conditions, the activator's functional group(s) still present on the activated support rapidly couples the enzyme, preventing unfolding and keeping the active site alive.

View Article and Find Full Text PDF

Gestational diabetes (GD) is a condition characterized by elevated blood sugar levels during pregnancy. GD poses various health risks, such as serious birth injuries, the need for cesarean delivery, and the necessity of newborn care. Monitoring glucose levels is essential for ensuring safe delivery and reducing the risks to both the mother and fetus.

View Article and Find Full Text PDF

Characterization of a recombinant Aspergillus niger GZUF36 lipase immobilized by ionic liquid modification strategy.

Appl Microbiol Biotechnol

February 2024

Key Laboratory of Agricultural and Animal Products Store & Processing of Guizhou Province, Guizhou University, Guiyang, 550025, People's Republic of China.

Enzyme immobilized on magnetic nanomaterials is a promising biocatalyst with efficient recovery under applied magnets. In this study, a recombinant extracellular lipase from Aspergillus niger GZUF36 (PEXANL1) expressed in Pichia pastoris GS115 was immobilized on ionic liquid-modified magnetic nano ferric oxide (FeO@SiO@ILs) via electrostatic and hydrophobic interaction. The morphology, structure, and properties of FeO@SiO@ILs and immobilized PEXANL1 were characterized by scanning electron microscopy, Fourier transform infrared spectroscopy, x-ray diffraction, vibration sample magnetometer, and zeta potential analysis.

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!