柽柳曲霉UCP 1279固态发酵β-果糖糠醛苷酶的生产、动力学/热力学研究及静磁场对动力学参数影响的评价

IF 2.7 Q3 BIOTECHNOLOGY & APPLIED MICROBIOLOGY
BioTech Pub Date : 2023-03-03 DOI:10.3390/biotech12010021
Rodrigo Lira de Oliveira, Aldeci França Araújo Dos Santos, Bianca Alencar Cardoso, Thayanne Samille da Silva Santos, Galba Maria de Campos-Takaki, Tatiana Souza Porto, Camila Souza Porto
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引用次数: 1

摘要

β-果糖糠醛苷酶(FFases)是参与蔗糖水解的酶,可用于生产转化糖和低聚果糖(FOS)。后者是一种重要的益生元,广泛应用于食品工业。在本研究中,以小麦和豆糠为底物的混合物为固体发酵材料,研究了柽柳曲霉Kita UCP 1279的FFase产量。该酶的最佳pH值为5.0 ~ 7.0℃,最佳温度为60℃。动力学/热力学研究表明,在以蔗糖为底物的工业FOS合成中常用的50°C温度下,FFase相对稳定,其半衰期(115.52 min)和d值(383.76 min)得到了证明,热力学参数也得到了评价。1450 G的静磁场对FFase动力学参数有正向影响,暴露后酶对底物的亲和力增加,Km上降低149.70 ~ 81.73 mM。结果表明,该酶具有良好的特性,可进一步应用于食品工业。此外,磁场的积极影响是磁场存在下生物过程进一步发展的一个指标。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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

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

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

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

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 Aspergillus tamarii 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 D-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 Km. 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.

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来源期刊
BioTech
BioTech Immunology and Microbiology-Applied Microbiology and Biotechnology
CiteScore
3.70
自引率
0.00%
发文量
51
审稿时长
11 weeks
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