Journals / Sakarya University Journal of Science / 2026 / Volume: 17 Issue: 2

Purification Of Invertase By Three-Phase Partitioining Systems And Determination Of Its Thermal Stability

İnvertaz Enziminin Üçlü Faz Sistemi İle Saflaştırılması Ve Termal Kararlılığının İncelenmesi

Pages
—
Publication Date
2013-06-01
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

Purified enzyme is also very stable in the temperature range from 4 to 50 °C.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:The enzyme invertase (β-fructofuranosidase, EC 3.2.1.26) is class of the hydrolase that catalyzes the hydrolysis of sucrose into glucose and fructose.
📊
Key Findings & Data:The invertase has been used in a wide range of industrial applications.
💡
Conclusion & Impact:Purified enzyme is also very stable in the temperature range from 4 to 50 °C.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:TPP (three phase partitation) · invertase · thermal stability

Abstract

The enzyme invertase (β-fructofuranosidase, EC 3.2.1.26) is class of the hydrolase that catalyzes the hydrolysis of sucrose into glucose and fructose. The invertase has been used in a wide range of industrial applications. In spite of various methods have been developed for the separation and purification of enzymes, most of them involved a number of steps and furthermore the scale up of these methods is difficult and also expensive to produce in large scale. Therefore, the process called as three-phase partitioning (TPP) is a simple, more efficient and economical method for separation and purification of target proteins. One of the important criteria to be preferred enzyme preparations used in industrial processes, the stability of these preparations. Factors such as thermal, microbial destruction, pH, chemical inactivation are effective in maintaining the enzyme activity with time. In this work, the thermal stability of invertase that purified from Vitis labrusca by TPP process was investigated. Purified enzyme is also very stable in the temperature range from 4 to 50 °C.

Özet

The enzyme invertase (β-fructofuranosidase, EC 3.2.1.26) is class of the hydrolase that catalyzes the hydrolysis of sucrose into glucose and fructose. The invertase has been used in a wide range of industrial applications. In spite of various methods have been developed for the separation and purification of enzymes, most of them involved a number of steps and furthermore the scale up of these methods is difficult and also expensive to produce in large scale. Therefore, the process called as three-phase partitioning (TPP) is a simple, more efficient and economical method for separation and purification of target proteins. One of the important criteria to be preferred enzyme preparations used in industrial processes, the stability of these preparations. Factors such as thermal, microbial destruction, pH, chemical inactivation are effective in maintaining the enzyme activity with time. In this work, the thermal stability of invertase that purified from Vitis labrusca by TPP process was investigated. Purified enzyme is also very stable in the temperature range from 4 to 50 °C.

🔖

Cite This Article

Keskin, S. Y., Kat, B. (2013). Purification Of Invertase By Three-Phase Partitioining Systems And Determination Of Its Thermal Stability. Sakarya University Journal of Science, Volume: 17 Issue: 2. https://doi.org/10.16984/saufbed.35530

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (6)

  1. Karkaş, T., İkili-faz ayırma sistemlerinin geliştirilmesi, Bornova İzmir, 61, 2009.
  2. Telefoncu, A., Enzimolojiye Genel Bakış, Ege Üniversitesi Yayınları, İzmir, 1986.
  3. Wiseman A., Handbook of Enzyme Biotechnology, TJ Pres Ltd., Cornwall, UK, 465466, 1995.
  4. Roy, I., Gupta, M.N., Three-phase affinity partitioning of proteins, Anal. Biochem., 300, 11– 14, 2002.
  5. Dhananjay, S.K., Mulimani, V.H., Three-phase partitioning of galactosidase from fermented media of Aspergillus oryzae and comparison with conventional purification techniques, J. Ind. Microbiol. Biotechnol., 36, 123–128, 2009.
  6. Narayan, A.V., Madhusudhan, M.C., Raghavarao, K.S.M.S., Extraction and purification of Ipomoea peroxidase employing three-phase Fazlar 20 40 60 80 100 120 20 40 60 80 100 Ba ğı l Aktivite (% ) Sıcaklık (°C) Bağıl aktivite (%)