scholarly journals Intraparticle Kinetics Unveil Crowding and Enzyme Distribution Effects on the Performance of Cofactor-Dependent Heterogeneous Biocatalysts

ACS Catalysis ◽  
2021 ◽  
pp. 15051-15067
Author(s):  
Eleftheria Diamanti ◽  
Javier Santiago-Arcos ◽  
Daniel Grajales-Hernández ◽  
Nicolette Czarnievicz ◽  
Natalia Comino ◽  
...  
Keyword(s):  
Heterogeneous Biocatalysts ◽  
Enzyme Distribution

Effect of enzyme distribution in immobilized membranes

1991 ◽  
Vol 15 ◽  
pp. 249-250
Author(s):  
S. Kunugi ◽  
T. Nakajima ◽  
A. Nomura
Keyword(s):  
Enzyme Distribution

Biotransformation of phenolic acids from by-products using heterogeneous biocatalysts: one more step toward a circular economy

2021 ◽  
Vol 32 ◽  
pp. 100550
Author(s):  
Daniel A. Grajales-Hernández ◽  
Mariana A. Armendáriz Ruiz ◽  
Victor Contreras-Jácquez ◽  
Juan Carlos Mateos-Díaz
Keyword(s):  
Phenolic Acids ◽  
Circular Economy ◽  
Heterogeneous Biocatalysts ◽  
By Products

Entrapment of Lipases in Hydrophobic Sol-Gel-Materials: Efficient Heterogeneous Biocatalysts in Aqueous Medium

Synthesis ◽  
2000 ◽  
Vol 2000 (06) ◽  
pp. 781-783 ◽  
Author(s):  
Manfred T. Reetz ◽  
Regina Wenkel ◽  
David Avnir
Keyword(s):  
Aqueous Medium ◽  
Sol Gel ◽  
Heterogeneous Biocatalysts

scholarly journals Selective biomineralization of Co3(PO4)2-sponges triggered by His-tagged proteins: efficient heterogeneous biocatalysts for redox processes

2015 ◽  
Vol 51 (42) ◽  
pp. 8753-8756 ◽  
Author(s):  
Fernando López-Gallego ◽  
Luis Yate
Keyword(s):  
Redox Processes ◽  
His Tag ◽  
Heterogeneous Biocatalysts ◽  
Cobalt Phosphate

Heterogeneous redox biocatalyts fabricated by mineralization of cobalt phosphate triggered by His-tag enzymes.

scholarly journals ENZYME DISTRIBUTION IN PSEUDOMONAS AERUGINOSA

1962 ◽  
Vol 83 (5) ◽  
pp. 1155-1160 ◽  
Author(s):  
J. J. R. Campbell ◽  
Loretta A. Hogg ◽  
G. A. Strasdine
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Enzyme Distribution

Recombinant strains producing thermostable lipase from Thermomyces lanuginosus and their use in heterogeneous biocatalysis, including in the processes of low-temperature synthesis of esters

2021 ◽  
Vol 37 (5) ◽  
pp. 5-19
Author(s):  
M.B. Pykhtina ◽  
L.V. Perminova ◽  
G.A. Kovalenko
Keyword(s):  
Escherichia Coli ◽  
Fatty Acids ◽  
Pichia Pastoris ◽  
Substrate Specificity ◽  
Carbon Aerogel ◽  
Operational Stability ◽  
Thermomyces Lanuginosus ◽  
Thermostable Lipase ◽  
Recombinant Strains ◽  
Heterogeneous Biocatalysts

Abstract-This work was devoted to the construction of recombinant strains Escherichia coli BL21 (DE3) and Pichia pastoris X33, producing a 1,3-specific thermostable lipase from Thermomyces lanuginosus. The sequences of two lipase genes were optimized for expression in bacteria and methylotrophic yeasts, then synthesized and cloned into the corresponding expression vectors. As a result of genetic engineering manipulations, E. coli and P. pastoris strains were constructed that efficiently produced recombinant lipase from T. lanuginosus, which accumulated in the cytoplasm in an amount of 30-40% of the total cellular protein. Recombinant P. pastoris clones secreted lipase into the nutrient medium at a concentration of at least 1 g/L. Lipases produced by the recombinant clones, designated as rE.coli/lip and rPichia/lip, respectively, contained a six-histidine sequence (-His6) in the C-terminal region. The resulting lipases were immobilized on/in solid inorganic supports in order to develop heterogeneous biocatalysts (HB) for the enzymatic conversion of triglycerides and fatty acids. The rPichia/lip enzyme was adsorbed on mesoporous silica and macroporous carbon aerogel. The properties of the prepared HB, their enzymatic activity, substrate specificity and operational stability were studied in the reaction of esterification of fatty acids with aliphatic alcohols in organic solvents at 20 ± 2°C. It was found that immobilized lipases had a relatively wide substrate specificity, as well as high operational stability, and the prepared HB almost completely retained their high esterifying activity for several tens of reaction cycles. Key words: Escherichia coli, Pichia pastoris, recombinant strains-producers, Thermomyces lanuginosus lipase gene, immobilization, biocatalysts, esterification The authors are grateful to V. L. Kuznetsov for the provided samples of carbon aerogel and A. V. Ryabchenko for gene-engineering manipulation aimed at obtaining the recombinant rE. coli strain, a producer of the rE.coli/lip enzyme. The work was carried out under the Project on Fundamental Research within the framework of a state assignment to the Institute for Catalysis "Catalysts and Processes of Renewable Raw Material Conversion" (no. 0239-2021-0005).

BIOCATALYTIC PROCESSES OF LOW-TEMPERATURE SYNTHESIS OF ESTERS. MODULATION OF THE FUNCTIONAL PROPERTIES OF LIPASE BY THE CHOICE OF SOLVENT AND SUPPORT FOR IMMOBILIZATION

2021 ◽  
Vol 1 (19) ◽  
pp. 271-273
Author(s):  
L.V. Perminova ◽  
M.B. Pykhtina ◽  
A.B. Beklemishev
Keyword(s):  
Organic Solvent ◽  
Functional Properties ◽  
Chemical Nature ◽  
Immobilized Lipase ◽  
Carbon Aerogel ◽  
Low Temperature Synthesis ◽  
Temperature Synthesis ◽  
Heterogeneous Biocatalysts ◽  
Adsorptive Immobilization ◽  
Selection Of

Biocatalytic processes for the synthesis of valuable products, such as different esters for various purposes, have been studied using heterogeneous biocatalysts prepared by immobilizing the recombinant lipase rPichia/lip on mesoporous silica (SiO2) and macroporous carbon aerogel (MCA). It was found that the functional properties of immobilized lipase, such as enzymatic activity, specificity toward pair of substrates (acid and alcohol), the molecules of which differ in the number of carbon atoms (C), as well as operational stability, depended on the method of adsorptive immobilization, the chemical nature of the support, and polarity of the organic solvent, i.e. logP. The functional properties of rPichia/lip have been shown to be modulated by the selection of an organic solvent and support for lipase immobilization.

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