Orderly cascade of immobilized-enzyme catalysis and photocatalysis for continuous-microflow production of 2-phenylbenzothiazole

2021 ◽  
Author(s):  
Qiang Chen ◽  
Yujun Wang ◽  
Guangsheng Luo
Keyword(s):  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
First Time

Green, economic, efficient, and sustainable synthesis of 2-phenylbenzothiazole (2-PBZ)—an important versatile scaffold—remains challenging. Here, for the first time, we propose to cascade immobilized enzyme catalysis and photocatalysis in a continuous-microflow...

scholarly journals Immobilization of Eversa Lipase on Octyl Agarose Beads and Preliminary Characterization of Stability and Activity Features

Catalysts ◽  
2018 ◽  
Vol 8 (11) ◽  
pp. 511 ◽  
Author(s):  
Sara Arana-Peña ◽  
Yuliya Lokha ◽  
Roberto Fernández-Lafuente
Keyword(s):  
Immobilized Enzyme ◽  
Biodiesel Production ◽  
Free Form ◽  
Enzyme Specificity ◽  
Agarose Beads ◽  
The Stability ◽  
Isoform B ◽  
First Time ◽  
Commercial Lipase

Eversa is an enzyme recently launched by Novozymes to be used in a free form as biocatalyst in biodiesel production. This paper shows for first time the immobilization of Eversa (a commercial lipase) on octyl and aminated agarose beads and the comparison of the enzyme properties to those of the most used lipase, the isoform B from Candida antarctica (CALB) immobilized on octyl agarose beads. Immobilization on octyl and aminated supports of Eversa has not had a significant effect on enzyme activity versus p-nitrophenyl butyrate (pNPB) under standard conditions (pH 7), but immobilization on octyl agarose beads greatly enhanced the stability of the enzyme under all studied conditions, much more than immobilization on aminated support. Octyl-Eversa was much more stable than octyl-CALB at pH 9, but it was less stable at pH 5. In the presence of 90% acetonitrile or dioxane, octyl-Eversa maintained the activity (even increased the activity) after 45 days of incubation in a similar way to octyl-CALB, but in 90% of methanol, results are much worse, and octyl-CALB became much more stable than Eversa. Coating with PEI has not a clear effect on octyl-Eversa stability, although it affected enzyme specificity and activity response to the changes in the pH. Eversa immobilized octyl supports was more active than CALB versus triacetin or pNPB, but much less active versus methyl mandelate esters. On the other hand, Eversa specificity and response to changes in the medium were greatly modulated by the immobilization protocol or by the coating of the immobilized enzyme with PEI. Thus, Eversa may be a promising biocatalyst for many processes different to the biodiesel production and its properties may be greatly improved following a suitable immobilization protocol, and in some cases is more stable and active than CALB.

Three-phase partitioning and immobilization of Bacillus methylotrophicus Y37 cellulase on organo-bentonite and its kinetic and thermodynamic properties

Clay Minerals ◽  
2020 ◽  
Vol 55 (2) ◽  
pp. 120-131
Author(s):  
Yonca Avci Duman ◽  
A. Uğur Kaya ◽  
Çiğdem Yağci
Keyword(s):  
Immobilized Enzyme ◽  
Maximum Velocity ◽  
Catalytic Performance ◽  
Covalent Immobilization ◽  
Single Step ◽  
Free Enzyme ◽  
Phase Partitioning ◽  
Bacillus Methylotrophicus ◽  
Three Phase ◽  
First Time

AbstractIn this study, for the first time Bacillus methylotrophicus Y37 cellulase was purified and recovered in a single step by three-phase partitioning (TPP). The optimal purification parameters for TPP were 40% ammonium sulfate saturation (m/v) with a 1.0:1.0 (v/v) ratio of crude extract:t-butanol, which gave 5.8-fold purification with 155% recovery of cellulase. Non-covalent immobilization of the partitioned cellulase was performed using bentonite as a support material. The activity observed in the 20th experiment was 100%. The optimal pH values and temperatures determined for the free enzyme and the immobilized enzyme were 5.0 and 6.0 and 45°C and 50°C, respectively. The Arrhenius activation energy (Ea) of the immobilized enzyme was lower than that of the free enzyme, whereas the Michaelis–Menten constant (Km) and maximum velocity (Vm) of the immobilized enzyme increased. The turnover number (kcat) and the catalytic performance (kcat/Km) demonstrated the improved catalytic properties of the immobilized enzyme compared to the free enzyme. Immobilization of cellulase is thermodynamically preferred.

scholarly journals Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite

Catalysts ◽  
2018 ◽  
Vol 8 (7) ◽  
pp. 287 ◽  
Author(s):  
Paula Bracco ◽  
Guzman Torrelo ◽  
Sander Noordam ◽  
Glenn de Jong ◽  
Ulf Hanefeld
Keyword(s):  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
Immobilized Enzymes ◽  
Prunus Amygdalus ◽  
Hydroxynitrile Lyase ◽  
High Enzyme ◽  
Background Reaction

The hydroxynitrile lyase from Prunus amygdalus was immobilized on Celite R-633. The immobilized enzyme could successfully be utilized in buffer saturated MTBE and excellent conversions of benzaldehyde to R-mandelonitrile were observed. No leaching occurred. To achieve high enantioselectivities, the suppression of the undesired background reaction was essential. This could be achieved by high enzyme loadings and the tight packing of the immobilized enzymes. When the immobilized enzyme is loosely packed, both the enzyme catalysis and the background reaction accelerates and only a modest enantioselectivity is observed. The enzyme was recycled for up to ten times, with some loss of activity and also enantioselectivity after 5 cycles, independent of packing.

Enzyme and photoredox sequential catalysis for the synthesis of 1,3-oxazine derivatives in one pot

2017 ◽  
Vol 7 (9) ◽  
pp. 1937-1942 ◽  
Author(s):  
Guo-Yan Zhang ◽  
Yang Xiang ◽  
Zhi Guan ◽  
Yan-Hong He
Keyword(s):  
Visible Light ◽  
Enzyme Catalysis ◽  
One Pot ◽  
Novel Strategy ◽  
First Time ◽  
Oxazine Derivatives

A novel strategy combining visible-light and enzyme catalysis for the synthesis of 1,3-oxazine derivatives is described for the first time.

Immobilized enzyme catalysis with reaction-generated pH change

1974 ◽  
Vol 16 (10) ◽  
pp. 1345-1357 ◽  
Author(s):  
J. E. Bailey ◽  
Mary T. C. Chow
Keyword(s):  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
Ph Change

Adjust the Reaction Conditions of Enzyme Catalysis to Product Fructooligosaccharides Containing Different Components Proportions

2011 ◽  
Vol 343-344 ◽  
pp. 403-411
Author(s):  
Ji Cheng Ding ◽  
Xiao Ling Lv
Keyword(s):  
Enzyme Catalysis ◽  
Maximum Yield ◽  
Reaction Parameters ◽  
Reaction Conditions ◽  
Food Ingredients ◽  
Fermentation Time ◽  
Beneficial Effects ◽  
First Time ◽  
The Relationship ◽  
Basic Investigation

Fructooligosaccharides (FOSs), as a mixture of 1-kestose, nystose, and 1F-fructofuranosylnystose oligosaccharides, exhibit lots of beneficial effects on our health and have been used as food ingredients. There have been a lot of reports on how to raise FOSs yield in different ways, but almost nobody did any deeply studies on the composition of FOSs—proportion of each component. However, different components may have different functions and some even show side-effects. In this research, we employed immobilized fructosyltransferase to produce FOSs and got a maximum yield of 56.12 %. Then we successfully produced FOSs of different components proportions by adjusting the reaction parameters—pH, temperature, and fermentation time. We designed six groups to investigate the relationship between reaction parameters and components proportions, and the results showed that pH condition mainly affects the yield while reaction time mainly affects components proportions. It is the first time that the components proportions of FOSs are systemically investigated, and we finally figured out six protocols for producing different FOSs. This is a basic investigation on the relationship between FOSs components proportions and reaction conditions. We hope this research can be helpful for other researchers who are interested in this area.

Specific immobilization of d-amino acid oxidase on hematin-functionalized support mimicking multi-enzyme catalysis

2015 ◽  
Vol 17 (8) ◽  
pp. 4465-4472 ◽  
Author(s):  
Jian Sun ◽  
Kun Du ◽  
Xiaoqiang Song ◽  
Qian Gao ◽  
Hao Wu ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Enzyme Catalysis ◽  
Immobilized Enzyme ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

Specifically immobilized enzyme and hematin sequentially catalyze the conversion of d-alanine and the decomposition of the generated hydrogen peroxide.

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