Skip to main content
Log in

Purification of phytase enzyme from Lactobacillus brevis and biochemical properties

  • Original Article
  • Published:
Biologia Aims and scope Submit manuscript

Abstract

In this study, Lactobacillus brevis isolated from kashar cheese was identified by 16s rRNA method, phytase enzyme from bacteria was partially purified and characterized. Work continued in two directions. The first step was the isolation and identification of the bacteria. In the second step, the phytase enzyme from L. brevis was partially purified and the optimum pH and temperature values of the purified enzyme were determined. The phytase activity of the identified L. brevis was determined as 212.97 U/mL. The molecular mass of the enzyme was determined as 49.9 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) method. The Km and Vmax values for sodium phytate were 0.0154 mM and 2.00 µmol/min, respectively. The optimum pH and temperature values of partially purified phytase were determined as pH 3.0, 60 °C, respectively.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

Availability of data and material

All of the datasets created and/or analyzed during the current study are presented in the article.

Code Availability

Not.

Abbreviations

SDS-PAGE:

Sodium dodecyl sulfate polyacrylamide gel electrophoresis

rRNA:

Ribosomal RNA

LAB:

Lactic acid bacteria

PA:

Phytic acid

GRAS:

Generally recognized as safe

DNA:

Deoxyribonucleic acid

PCR:

Polymerase chain reaction

UV:

Ultraviolet

NCBI:

National center for biotechnology information

kDa:

Kilodalton

AC:

Accession number

BLASTn:

Basic local alignment search tool

References

Download references

Funding

The authors declare that no funds, grants, or other support were received during the preparation of this manuscript.

Author information

Authors and Affiliations

Authors

Contributions

All authors contributed to the study conception and design. Material preparation, data collection and analysis were performed by Neslihan DİKBAŞ, Sevda UÇAR and Şeyma ALIM. The first draft of the manuscript was written by Neslihan DİKBAŞ and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript.

Corresponding author

Correspondence to Neslihan Dikbaş.

Ethics declarations

Competing interests

The authors have no relevant financial or non-financial interests to disclose.

Ethics approval

Not.

Consent to participate

All authors’ consent was obtained.

Consent for publication

All authors’ consent was obtained.

Additional information

Publisher’s Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Dikbaş, N., Uçar, S. & Alım, Ş. Purification of phytase enzyme from Lactobacillus brevis and biochemical properties. Biologia 78, 2583–2591 (2023). https://doi.org/10.1007/s11756-023-01403-9

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11756-023-01403-9

Keywords

Navigation