Overproduction, purification, and property analysis of an extracellular recombinant fructosyltransferase

Guo, Wenwen; Yang, Haiquan; Qiang, Shumin; Fan, You; Shen, Wei; Chen, Xianzhong

doi:10.1007/s00217-015-2620-x

Cited by 20 publications

(46 citation statements)

References 35 publications

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“…The profiles of FFase activities at different temperatures show that the optimum temperature for both hydrolytic and transfructosylating activities was 50°C (Figure a). Guo et al reported the same optimum temperature for transfructosylating activity of recombinant FTase from Aspergillus oryzae overexpressed in Pichia pastoris . The optimum pH was 6.0 for both activities (Figure b), a value coincident with that reported for an A. oryzae FTase .…”

Section: Resultsmentioning

confidence: 88%

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Oliveira

Silva

Converti

et al. 2019

Biotechnology Progress

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This study reports on the biochemical characterization as well as the kinetic and thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase (FFase) with transfructosylating activity. Conditions for FFase activity were optimized by means of a central composite rotational design using pH and temperature as the independent variables, while residual activity tests carried out in the temperature range of 45–65°C enabled us to investigate FFase thermostability and estimate the kinetic and thermodynamic parameters of enzyme denaturation. Optimal conditions for sucrose hydrolysis and fructosyl transfer catalyzed by crude FFase were 50°C, and pH 6.0 and 7.4, respectively. The thermodynamic properties of irreversible enzyme inactivation were found to be activation energy of 293.1 kJ mol−1, and activation enthalpy, entropy, and Gibbs free energy in the ranges 290.3–290.4 kJ mol−1, 568.7–571.0 J mol−1 K−1, and 97.9–108.8 kJ mol−1, respectively. The results obtained in this study point out satisfactory enzyme activity and thermostability at temperatures commonly used for industrial fructo‐oligosaccharide (FOS) synthesis; therefore, this novel FFase appears to be a promising biocatalyst with great potential for long‐term FOS synthesis and invert sugar production. To the best of our knowledge, this is the first report on kinetic and thermodynamic parameters of an A. tamarii FFase.

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Section: Resultsmentioning

confidence: 88%

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Oliveira

Silva

Converti

et al. 2019

Biotechnology Progress

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show abstract

“…To determine the optimal pH of FT-A, the activity assay was performed at 50 C using different phosphate buffers (pH from 3 to 9), 15,22 and the other reaction conditions and activity assay method are as described in "Enzyme activity assays". The highest activity measured under different pH conditions is dened as 100%.…”

Section: Effects Of Ph On Ft-a Activitymentioning

confidence: 99%

“…19,31 A. niger SG610 fructosyltransferase (FruSG, GenBank accession no. KT724055), 15 A. niger YZ59 fructosyltransferase (fwt), 22 A. niger QU10 fructosyltransferase (s1, GenBank accession no. AHC54391) 14 with FT-A in this study shared an identity between 96 and 99%, and the residues inside the domains A, D and E are completely conserved, while there are variable outside the conserved domains ( Fig.…”

Section: Structural Analysis Of the Ft-a Homology Modelmentioning

confidence: 99%

“…7 In subsequent years, more and more gene sequence of fructosyltransferase from A. niger were deciphered and deposited in the GenBank database (GeneBank accession no: L06844, AF029359, BAB67771, DQ233218, DQ233219, DQ233220, HQ450381, KF699529 and KT724055. [7][8][9][10][11][12][13][14][15] ), in which three putative invertase genes (SucA, SucB, SucC) were reported based on the available complete genome sequence of A. niger CBS 513.88. 10,11 SucA (DQ233218) was previously characterized as the secreted invertase encoded by gene suc1.…”

Section: Introductionmentioning

confidence: 99%

“…21 Several fructosyltransferases from A. niger were heterologously expressed in P. pastoris, and these recombinant fructosyltransferases showed better activity and higher FOSsynthesis ability than the corresponding native enzymes. 14,15,22 A gene encoding an invertase from A. niger was isolated from xerophilic A. niger GH1, and the invertase was produced in the methylotrophic yeast P. pastoris with a specic activity of 3389 U mg À1 protein. 12 However, data on FOS production using recombinant fructosyltransferase isolated from A. niger and expressed in P. pastoris were available only in three studies.…”

Section: Introductionmentioning

confidence: 99%

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Cloning, expression and characterization of a novel fructosyltransferase from Aspergillus niger and its application in the synthesis of fructooligosaccharides

et al. 2019

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Research Progress and Prospects for Fructosyltransferases

et al. 2021

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Fructosyltransferases can be used to produce fructooligosaccharides from sucrose and are obtained from different sources, mostly microorganisms and plants. Heterologous expression and several mutagenesis methods were applied to improve the production of fructosyltransferases. The structures and characteristics of fructosyltransferases were investigated. Immobilization and protein engineering can improve their characteristics. In this review, screening and mutagenesis of microorganisms, heterologous expression, purification, characterization, structural analysis, immobilization, and protein engineering of fructosyltransferases are discussed. Future prospects in this field are also considered.

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Overproduction, purification, and property analysis of an extracellular recombinant fructosyltransferase

Cited by 20 publications

References 35 publications

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Cloning, expression and characterization of a novel fructosyltransferase from Aspergillus niger and its application in the synthesis of fructooligosaccharides

Research Progress and Prospects for Fructosyltransferases

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