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Production, Kinetic/Thermodynamic Study, and Evaluation of the Influence of Static Magnetic Field on Kinetic Parameters of β-Fructofuranosidase from Kita UCP 1279 Produced by Solid-State Fermentation.

作者信息

de Oliveira Rodrigo Lira, Dos Santos Aldeci França Araújo, Cardoso Bianca Alencar, da Silva Santos Thayanne Samille, de Campos-Takaki Galba Maria, Porto Tatiana Souza, Porto Camila Souza

机构信息

School of Food Engineering, Federal University of Agreste of Pernambuco/UFAPE, Av. Bom Pastor, Boa Vista, s/n, Garanhuns 55296-901, Brazil.

Education Unit of Penedo, Federal University of Alagoas/UFAL, Avenida Beira Rio, s/n, Penedo 57200-000, Brazil.

出版信息

BioTech (Basel). 2023 Mar 3;12(1):21. doi: 10.3390/biotech12010021.


DOI:10.3390/biotech12010021
PMID:36975311
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10046036/
Abstract

β-fructofuranosidases (FFases) are enzymes involved in sucrose hydrolysis and can be used in the production of invert sugar and fructo-oligosaccharides (FOS). This last is an important prebiotic extensively used in the food industry. In the present study, the FFase production by Kita UCP 1279 was assessed by solid-state fermentation using a mixture of wheat and soy brans as substrate. The FFase presents optimum pH and temperature at 5.0-7.0 and 60 °C, respectively. According to the kinetic/thermodynamic study, the FFase was relatively stable at 50 °C, a temperature frequently used in industrial FOS synthesis, using sucrose as substrate, evidenced by the parameters half-life (115.52 min) and -value (383.76 min) and confirmed by thermodynamic parameters evaluated. The influence of static magnetic field with a 1450 G magnetic flux density presented a positive impact on FFase kinetic parameters evidenced by an increase of affinity of enzyme by substrate after exposition, observed by a decrease of 149.70 to 81.73 mM on . The results obtained indicate that FFases present suitable characteristics for further use in food industry applications. Moreover, the positive influence of a magnetic field is an indicator for further developments of bioprocesses with the presence of a magnetic field.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/11dc8887b1fb/biotech-12-00021-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/5c33850085fd/biotech-12-00021-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/efdc7ff03c52/biotech-12-00021-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/160fb1b4ba57/biotech-12-00021-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/c4a5ec4965bf/biotech-12-00021-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/2005b201bb35/biotech-12-00021-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/11dc8887b1fb/biotech-12-00021-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/5c33850085fd/biotech-12-00021-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/efdc7ff03c52/biotech-12-00021-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/160fb1b4ba57/biotech-12-00021-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/c4a5ec4965bf/biotech-12-00021-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/2005b201bb35/biotech-12-00021-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/16c8/10046036/11dc8887b1fb/biotech-12-00021-g006.jpg

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Production, Kinetic/Thermodynamic Study, and Evaluation of the Influence of Static Magnetic Field on Kinetic Parameters of β-Fructofuranosidase from Kita UCP 1279 Produced by Solid-State Fermentation.

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[1]
Regulation mechanism of magnetic field on pectinase and its preliminary application in postharvest sapodilla (Manilkara zapota).

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[2]
Investigation of static magnetic field effect on horseradish peroxidase enzyme activity and stability in enzymatic oxidation process.

Int J Biol Macromol. 2021-2-15

[3]
Fructo-oligosaccharides production by an Aspergillus aculeatus commercial enzyme preparation with fructosyltransferase activity covalently immobilized on FeO-chitosan-magnetic nanoparticles.

Int J Biol Macromol. 2020-5-1

[4]
Production of β-fructofuranosidase with transfructosylating activity by Aspergillus tamarii URM4634 Solid-State Fermentation on agroindustrial by-products.

Int J Biol Macromol. 2019-12-12

[5]
Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β-fructofuranosidase with transfructosylating activity.

Biotechnol Prog. 2019-7-25

[6]
Technological Aspects of the Production of Fructo and Galacto-Oligosaccharides. Enzymatic Synthesis and Hydrolysis.

Front Nutr. 2019-5-31

[7]
Rotating magnetic field as tool for enhancing enzymes properties - laccase case study.

Sci Rep. 2019-3-6

[8]
Characterization of a mycelial fructosyltransferase from Aspergillus tamarii NKRC 1229 for efficient synthesis of fructooligosaccharides.

Food Chem. 2019-2-14

[9]
Effect of magnetic field on the Eversa® Transform 2.0 enzyme: Enzymatic activity and structural conformation.

Int J Biol Macromol. 2018-10-25

[10]
Static magnetic field effects on proteases with fibrinolytic activity produced by Mucor subtilissimus.

Bioelectromagnetics. 2017-2

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