Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli

Çömlekçioğlu, Uğur; Gunes, Merva; Altun, Hanifi; Ekiz, Dilek Özgün; Aygan, Ashabil

doi:10.1590/1678-4324-2017160462

Cited by 2 publications

(3 citation statements)

References 23 publications

(18 reference statements)

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“…The oxidation rate of vanillin in vanillic acid increased with an increase in pH (3.6-5.2) at 308 K. The oxidation rate of vanillin was difficult to measure using a pH more value above 5.2. 20 The set temperature to analyze the activity of cellulase and protease activity from rumen bovine liquid were appointed at 313 K and 323 K. [29][30] The highest value of k was obtained by processing the extraction at 323 K with the protease addition of enzyme-substrate ratio at 0.01 (6.09×10 -3 L⋅mg -1 ⋅min -1 ), however the value of h and Cs provided the lowest value, 4.10 mg⋅L -1 ⋅min -1 and 25.97 mg⋅L -1 , respectively. Although the 2 nd -order extraction rate at 323 K with the protease addition was performed relatively faster than others, however, the lower initial extraction rate resulted in the lower saturation extraction capacity.…”

Section: Kinetics Of Vanillin Extractionmentioning

confidence: 99%

Kinetic Modelling and Activation Energy on Microwave-Integrated Enzymatic-Leaching of Vanillin From Dried Vanilla Pods

Paramita¹,

Yulianto²,

Hartati³

2019

RJC

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Vanillin, a major component of Vanilla planifolia, performs a delicate, sweet and tender aroma with intense sensation. Due to its pleasant aroma and calming ability, low temperature and the short time duration during the extraction process lead to numerous advantages of the microwave integrated enzymatic leaching. The extraction consists of simultaneous cell wall degradation and release of vanillin. The kinetic study of the microwave-integrated enzymatic-leaching of vanillin was studied with regards to the temperature, enzyme types (cellulase and protease) and concentration. The enzymes applied were un-commercial enzymes, obtained by isolating it from rumen bovine liquid. The extraction process was integrated with the microwave and temperatures set at 313 and 323 K. The enzyme was added to the substrate in the ratio of 0.04 and 0.02 for cellulase and 0.02 and 0.01 for protease at pH 4.5. The experimental data corresponded to the 2 nd -order model of kinetic parameter, i.e. the initial extraction rate, the extraction rate constant, and the saturation capacity of extraction for the processing at 313 K. By using the Arrhenius law, the value of activation energy obtained by the addition of protease with enzyme-substrate ratio at 0.01 was 2.37×10 4 J⋅mol -1 , due to the lower value of A than the addition of cellulase with enzyme-substrate ratio at 0.02. It is concluded that the decreasing of the activation energy well performed by the higher enzyme activity. The disruption of the cell wall worthwhile for the extraction process, properly.

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Section: Kinetics Of Vanillin Extractionmentioning

confidence: 99%

Kinetic Modelling and Activation Energy on Microwave-Integrated Enzymatic-Leaching of Vanillin From Dried Vanilla Pods

Paramita¹,

Yulianto²,

Hartati³

2019

RJC

View full text Add to dashboard Cite

show abstract

“…For multi-enzymatic reactions, including synergistic enzymatic reactions, the enzymes are usually cloned separately in an adequate plasmid and host cell. Then, they are mixed in different ratios for subsequent applications following their expression and purification; which demands extra costs and time (Roongsawang et al, 2010;Comlekcioglu et al, 2017). The co-expression of multiple enzymes in a single host is gaining more interest since it allows the costeffective production of biocatalysts increasing their applicability in biocatalysis.…”

Section: Introductionmentioning

confidence: 99%

“…Some studies about enzymes co-expression have been carried out with different purposes. Among then, to reduce the production cost of carbohydrate degrading enzymes either to exploit sustainable biomass (Kumar et al, 2015;Comlekcioglu et al, 2017;Panpetch et al, 2018) or to be used as additives in animal feed (Roongsawang et al, 2010). Also, to develop whole cell biocatalysts through the co-expression of several degrading enzymes in bacteria or the construction of multi-enzymes synthetic pathways (Lan et al, 2006;Zhu et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Co-expression of thermophilic pectinases in a single host for cost-effective pectin bioconversion into D-galacturonic acid

Flores-Fernández

Cárdenas-Fernández²,

Lye³

et al. 2023

Front. Catal.

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Co-expression of enzymes allow to produce multiple enzymes in a single host, representing a cost-effective alternative in biocatalytic processes which can be used for pectin bioconversion. Pectin-rich biomass is an abundant by-product from the fruit and sugar industries that is usually disposed in landfill or sold as a low value feedstock. The aim of this work was to co-express a thermophilic pectin methyl esterase (PME) and exo-polygalacturonases (exo-PGs) in a single host for pectin bioconversion into D-galacturonic acid (GalA) using different pectic substrates such as apple, citrus and sugar beet pectin. To achieve this, a PME from Bacillus licheniformis (BLI09) with either an exo-PG from Thermotoga maritima (TMA01) or from Bacillus licheniformis (BLI04) were cloned in pETDuet-1 and co-expressed in E. coli BL21 (DE3). Four co-expression plasmids containing both pectinases were constructed and factors such as the effect of the genes’ cloning order and their expression were evaluated. Co-expression constructs 3 and 4 (pETDuet-TMA01-BLI09 and pETDuet-BLI04-BLI09, respectively) showed better expression of both pectinases compared to co-expression constructs 1 and 2 (pETDuet-BLI09-TMA01 and pETDuet-BLI09-BLI04, respectively). Co-expression constructs 3 and 4 were the most efficient for pectin bioconversion into GalA reaching 3 and 2.5 mM GalA, respectively from apple and citrus pectin after 4 h reaction. In conclusion, this work demonstrates that the co-expression of pectinases can potentially contribute to reduce the cost associated to their production and purification as well as to increase their applicability for exploiting pectin-rich biomass to obtain bio-based chemicals.

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Coexpression of rumen fungal xylanase and bifunctional cellulase genes in Escherichia coli

Abstract: Rumen fungi inhabit the gastro-intestinal tract of ruminants and the most non

Cited by 2 publications

References 23 publications

Kinetic Modelling and Activation Energy on Microwave-Integrated Enzymatic-Leaching of Vanillin From Dried Vanilla Pods

Kinetic Modelling and Activation Energy on Microwave-Integrated Enzymatic-Leaching of Vanillin From Dried Vanilla Pods

Co-expression of thermophilic pectinases in a single host for cost-effective pectin bioconversion into D-galacturonic acid

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