scholarly journals Continuous process technology for glucoside production from sucrose using a whole cell-derived solid catalyst of sucrose phosphorylase

2021 ◽  
Author(s):  
Andreas Kruschitz ◽  
Linda Peinsipp ◽  
Martin Pfeiffer ◽  
Bernd Nidetzky
Keyword(s):  
Continuous Production ◽  
Polymer Materials ◽  
Packed Bed Reactor ◽  
Solid Catalyst ◽  
Scale Production ◽  
Process Technology ◽  
Sucrose Phosphorylase ◽  
Bifidobacterium Adolescentis ◽  
Whole Cell ◽  
Highly Active

Abstract Advanced biotransformation processes typically involve the upstream processing part performed continuously and interlinked tightly with the product isolation. Key in their development is a catalyst that is highly active, operationally robust, conveniently produced, and recyclable. A promising strategy to obtain such catalyst is to encapsulate enzymes as permeabilized whole cells in porous polymer materials. Here, we show immobilization of the sucrose phosphorylase from Bifidobacterium adolescentis (P134Q-variant) by encapsulating the corresponding E. coli cells into polyacrylamide. Applying the solid catalyst, we demonstrate continuous production of the commercial extremolyte 2-α-d-glucosyl-glycerol (2-GG) from sucrose and glycerol. The solid catalyst exhibited similar activity (≥70%) as the cell-free extract (~800 U g−1 cell wet weight) and showed excellent in-operando stability (40 °C) over 6 weeks in a packed-bed reactor. Systematic study of immobilization parameters related to catalyst activity led to the identification of cell loading and catalyst particle size as important factors of process optimization. Using glycerol in excess (1.8 M), we analyzed sucrose conversion dependent on space velocity (0.075–0.750 h−1) and revealed conditions for full conversion of up to 900 mM sucrose. The maximum 2-GG space-time yield reached was 45 g L−1 h−1 for a product concentration of 120 g L−1. Collectively, our study establishes a step-economic route towards a practical whole cell-derived solid catalyst of sucrose phosphorylase, enabling continuous production of glucosides from sucrose. This strengthens the current biomanufacturing of 2-GG, but also has significant replication potential for other sucrose-derived glucosides, promoting their industrial scale production using sucrose phosphorylase. Key points • Cells of sucrose phosphorylase fixed in polyacrylamide were highly active and stable. • Solid catalyst was integrated with continuous flow to reach high process efficiency. • Generic process technology to efficiently produce glucosides from sucrose is shown. Graphical abstract

scholarly journals Whole cell-based catalyst for enzymatic production of the osmolyte 2-O-α-glucosylglycerol

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Katharina N. Schwaiger ◽  
Monika Cserjan-Puschmann ◽  
Gerald Striedner ◽  
Bernd Nidetzky
Keyword(s):  
Specific Activity ◽  
Dry Mass ◽  
High Yield ◽  
Sucrose Phosphorylase ◽  
Bifidobacterium Adolescentis ◽  
Enzymatic Production ◽  
Intracellular Enzyme ◽  
Whole Cell ◽  
Freeze Thaw ◽  
Thaw Cycle

Abstract Background Glucosylglycerol (2-O-α-d-glucosyl-sn-glycerol; GG) is a natural osmolyte from bacteria and plants. It has promising applications as cosmetic and food-and-feed ingredient. Due to its natural scarcity, GG must be prepared through dedicated synthesis, and an industrial bioprocess for GG production has been implemented. This process uses sucrose phosphorylase (SucP)-catalyzed glycosylation of glycerol from sucrose, applying the isolated enzyme in immobilized form. A whole cell-based enzyme formulation might constitute an advanced catalyst for GG production. Here, recombinant production in Escherichia coli BL21(DE3) was compared systematically for the SucPs from Leuconostoc mesenteroides (LmSucP) and Bifidobacterium adolescentis (BaSucP) with the purpose of whole cell catalyst development. Results Expression from pQE30 and pET21 plasmids in E. coli BL21(DE3) gave recombinant protein at 40–50% share of total intracellular protein, with the monomeric LmSucP mostly soluble (≥ 80%) and the homodimeric BaSucP more prominently insoluble (~ 40%). The cell lysate specific activity of LmSucP was 2.8-fold (pET21; 70 ± 24 U/mg; N = 5) and 1.4-fold (pQE30; 54 ± 9 U/mg, N = 5) higher than that of BaSucP. Synthesis reactions revealed LmSucP was more regio-selective for glycerol glycosylation (~ 88%; position O2 compared to O1) than BaSucP (~ 66%), thus identifying LmSucP as the enzyme of choice for GG production. Fed-batch bioreactor cultivations at controlled low specific growth rate (µ = 0.05 h−1; 28 °C) for LmSucP production (pET21) yielded ~ 40 g cell dry mass (CDM)/L with an activity of 2.0 × 104 U/g CDM, corresponding to 39 U/mg protein. The same production from the pQE30 plasmid gave a lower yield of 6.5 × 103 U/g CDM, equivalent to 13 U/mg. A single freeze–thaw cycle exposed ~ 70% of the intracellular enzyme activity for GG production (~ 65 g/L, ~ 90% yield from sucrose), without releasing it from the cells during the reaction. Conclusions Compared to BaSucP, LmSucP is preferred for regio-selective GG production. Expression from pET21 and pQE30 plasmids enables high-yield bioreactor production of the enzyme as a whole cell catalyst. The freeze–thaw treated cells represent a highly active, solid formulation of the LmSucP for practical synthesis.

Synthesis of carbonate esters by carboxymethylation using NaAlO2 as a highly active heterogeneous catalyst

2018 ◽  
Author(s):  
Sreerangappa Ramesh ◽  
Kiran Indukuri ◽  
Olivier Riant ◽  
Damien Debecker
Keyword(s):  
Heterogeneous Catalyst ◽  
Dimethyl Carbonate ◽  
Sodium Aluminate ◽  
High Yield ◽  
Solid Catalyst ◽  
Highly Active ◽  
Aromatic Alcohols ◽  
Green Conditions ◽  
Mixed Carbonate

<p>Sodium aluminate is presented as a highly active heterogeneous catalyst able to convert a range of alcohols into the corresponding mixed carbonate esters, in high yield and under green conditions. The reaction is carried out using dimethyl carbonate both as a reactant and solvent, at 90°C. Allylic, aliphatic and aromatic alcohols are converted in good yields. The solid catalyst is shown to be truly heterogeneous, resistant to leaching, and recyclable. </p>

Respect for the Environment is Part of Competitiveness - Best Available Technology Applied to an Old Pulp Mill at Kaskinen

1999 ◽  
Vol 40 (11-12) ◽  
pp. 201-206
Author(s):  
I. Reilama ◽  
N. Ilomäki
Keyword(s):  
Process Development ◽  
Continuous Production ◽  
Production Capacity ◽  
Pulp Mill ◽  
Process Technology ◽  
Line Production ◽  
Nutrient Emissions ◽  
Best Available Technology ◽  
Available Technology ◽  
Process Solutions

Oy Metsä-Botnia Ab's Kaskinen mill produces ECF and TCF bleached softwood and hardwood pulp on a single continuous production line. Production capacity has been raised from 250,000 tonnes to 420,000 tonnes a year after the commission in 1977. The basic process solutions date mainly from the 1970s. However, process technology has been gradually modernised. With systematic and well-timed process development investments the mill has remained competitive and among frontrunners in terms of environmental protection. Today, Kaskinen represent the best available technology (BAT) applicable to old mills. Effluent loading in general and nutrient emissions in particular has diminished during the development projects of the mill. Comparison to other mills shows that as far as effluent emissions are concerned, Kaskinen is one of the best pulp mills in Finland and Scandinavia. In this presentation, Kaskinen is also compared to Metsä-Rauma, the first greenfield TCF mill in the world, which was started up in 1996. Kaskinen's pioneering work on TCF technology was used as a basis for process solutions in the Rauma greenfield project.

Continuous production of a chiral amine in a packed bed reactor with co-immobilized amine dehydrogenase and formate dehydrogenase

2021 ◽  
Vol 407 ◽  
pp. 127065
Author(s):  
Robert D. Franklin ◽  
Joshua A. Whitley ◽  
Adam A. Caparco ◽  
Bettina R. Bommarius ◽  
Julie A. Champion ◽  
...  
Keyword(s):  
Formate Dehydrogenase ◽  
Continuous Production ◽  
Packed Bed ◽  
Packed Bed Reactor ◽  
Chiral Amine ◽  
Amine Dehydrogenase

scholarly journals Continuous Production of Lipase-Catalyzed Biodiesel in a Packed-Bed Reactor: Optimization and Enzyme Reuse Study

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Hsiao-Ching Chen ◽  
Hen-Yi Ju ◽  
Tsung-Ta Wu ◽  
Yung-Chuan Liu ◽  
Chih-Chen Lee ◽  
...  
Keyword(s):  
Flow Rate ◽  
Immobilized Lipase ◽  
Continuous Production ◽  
Packed Bed ◽  
Packed Bed Reactor ◽  
Molar Ratio ◽  
System Response ◽  
Biodiesel Synthesis ◽  
Substrate Molar Ratio ◽  
Molar Conversion

An optimal continuous production of biodiesel by methanolysis of soybean oil in a packed-bed reactor was developed using immobilized lipase (Novozym 435) as a catalyst in atert-butanol solvent system. Response surface methodology (RSM) and Box-Behnken design were employed to evaluate the effects of reaction temperature, flow rate, and substrate molar ratio on the molar conversion of biodiesel. The results showed that flow rate and temperature have significant effects on the percentage of molar conversion. On the basis of ridge max analysis, the optimum conditions were as follows: flow rate 0.1 mL/min, temperature52.1∘C, and substrate molar ratio 1 : 4. The predicted and experimental values of molar conversion were83.31±2.07% and82.81±.98%, respectively. Furthermore, the continuous process over 30 days showed no appreciable decrease in the molar conversion. The paper demonstrates the applicability of using immobilized lipase and a packed-bed reactor for continuous biodiesel synthesis.

Effectiveness of Adjustable-Volume Packed-Bed Reactor with an Ion-Exchange Resin Catalyst for Continuous Production

2016 ◽  
Vol 49 (7) ◽  
pp. 668-672 ◽  
Author(s):  
Kota Yamazaki ◽  
Naomi Shibasaki-Kitakawa ◽  
Kazunori Nakashima ◽  
Toshikuni Yonemoto
Keyword(s):  
Ion Exchange ◽  
Exchange Resin ◽  
Continuous Production ◽  
Packed Bed ◽  
Ion Exchange Resin ◽  
Packed Bed Reactor ◽  
Resin Catalyst

scholarly journals Directed immobilization of CGTase: The effect of the enzyme orientation on the enzyme activity and its use in packed-bed reactor for continuous production of cyclodextrins

2017 ◽  
Vol 58 ◽  
pp. 120-127 ◽  
Author(s):  
Jéssie da Natividade Schöffer ◽  
Carla Roberta Matte ◽  
Douglas Santana Charqueiro ◽  
Eliana Weber de Menezes ◽  
Tania Maria Haas Costa ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Continuous Production ◽  
Packed Bed ◽  
Packed Bed Reactor

A nanostructured bifunctional acid–base catalyst resin formed by lyotropic liquid crystal monomers

2020 ◽  
Vol 98 (7) ◽  
pp. 332-336
Author(s):  
Gregory E. Dwulet ◽  
Benjamin J. Coscia ◽  
Michael R. Shirts ◽  
Douglas L. Gin
Keyword(s):  
Liquid Crystal ◽  
Self Assembly ◽  
Polymeric Materials ◽  
Dimethyl Acetal ◽  
Bifunctional Catalyst ◽  
Lyotropic Liquid Crystal ◽  
Solid Catalyst ◽  
Test Reaction ◽  
Highly Active ◽  
Nitroaldol Reaction

An ordered, nanoporous polymer resin was prepared from the self-assembly of lyotropic liquid crystal monomers and employed as a heterogeneous, bifunctional catalyst. This material contains antagonistic acid and base sites in the periodic nanopores and efficiently catalyzes a model tandem reaction (i.e., the deacetalization–nitroaldol reaction between benzaldehyde dimethyl acetal and nitromethane to yield β-nitrostyrene) with excellent product selectivity. This lyotropic liquid crystal-based solid catalyst represents one of the few examples of polymeric tandem catalysts synthesized by a “bottom-up” strategy that imparts control over the stoichiometry of acidic and basic monomers and is the only reported example of a lyotropic liquid crystal-based polymer that contains mutually incompatible catalytic groups. Furthermore, this heterogeneous catalyst is highly active, exhibiting a turnover frequency for this tandem test reaction that exceeds other reported catalytic polymeric materials.

Sign in / Sign up

Export Citation Format

Share Document