Short Communication

Characterization of Planococcus dechangensis isolated from a water sample of Çamaltı Saltern

Volume: 38 Number: 4 December 15, 2021
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Characterization of Planococcus dechangensis isolated from a water sample of Çamaltı Saltern

Abstract



In the present study, strain MHDS3 was isolated from a water sample of Çamaltı Saltern and identified using conventional and molecular methods. 16S rRNA gene sequence analyses showed that the strain MHDS3 belonged to Planococcus dechangensis species. It gave a positive result in the Gram staining test. The cells were coccus, non-motile, aerobic, catalase positive, oxidase negative and the colony pigmentation was yellow-orange. It showed negative results for citrate utilization, indole production from tryptophane, Voges-Proskauer and methyl red. This isolate was able to grow at 10-45°C (optimally 35°C), pH 6-8 (optimally pH 7) and 3-20% NaCl (optimally 10% NaCl). It was not able to grow at 4°C, 10°C, 50°C, salt-free, 0.5%, 25%, %30 total salt, pH 4-5, and pH 9-12. Glucose, ribose, fructose, sucrose, maltose were used by the test isolate as carbon sources. Different amino acids found in the structure of animal hide such as L-lysine, L-arginine, L-cysteine, L-alanine, L-tyrosine, L-histidine were also utilized by the bacterium. During the salt production process, this bacterium may contaminate the salt which is used in the food and leather industries. The activities of harmful moderately halophilic bacteria should be prevented by effective antimicrobial applications.


Keywords

References

  1. Alas, Akpolat, C., Ventosa, A., Birbir, M., Sanchez-Porro, C. & Caglayan, P. (2015). Molecular identification of moderately halophilic bacteria and extremely halophilic archaea isolated from salted sheep skins containing red and yellow discolourations. Journal of American Leather Chemists Association, 110, 211-220.
  2. Caglayan, P., Birbir, M., Sánchez-Porro, C. & Ventosa, A. (2017). Screening of industrially important enzymes produced by moderately halophilic bacteria isolated from salted sheep skins of diverse origin. Journal of American Leather Chemists Association, 112, 207-216.
  3. Caglayan, P., Birbir, M., Sánchez-Porro, C. & Ventosa, A. (2018). Detection of industrially potential enzymes of moderately halophilic bacteria on salted goat skins. Turkish Journal of Biochemistry, 43, 312-322. DOI: 10.1515/tjb-2017-0127
  4. De la Haba, Yilmaz, P., Sánchez-Porro, C., Birbir, M. & Ventosa, A. (2011). Salimicrobium salexigens sp. nov., a moderately halophilic bacterium from salted hides. Systematic and Applied Microbiology, 34, 435-439. DOI: 10.1016/j.syapm.2011.04.002
  5. Galinski, E.A. & Louis, P. (1998). Compatible solutes: ectoine production and gene expression. In A. Oren (Ed.), Microbiology and Bio-geochemistry of Hypersaline Environments (pp 40-45). Boca Raton: CRC Press.
  6. Gaur, V.K., Tripathi, V., Gupta, P., Dhiman, N., Regar, R.K., Gautam, K., Srivastava, J.K., Patnaik, S., Patel, D.K., Manickam, N. (2020). Rhamnolipids from Planococcus spp. and their mechanism of action against pathogenic bacteria. Bioresource Technology, 307. DOI: 10.1016/j.biortech.2020.123206
  7. Gupta, S., Sharma, P., Dev, K. & Sourirajan, A. (2016). Halophilic bacteria of Lunsu produce an array of industrially important enzymes with salt-tolerant activity. Biochemistry Research International, 1-10. DOI: 10.1155/2016/9237418
  8. Guven, K., Demirci, A., Mutlu, M.B. & Korcan, S.E. (2010). Phenotypic Characterization of Halophilic Bacteria Isolated from Camaltı Saltern in Turkey. Electronic Journal of BioTechnology, 1, 11-21.

Details

Primary Language

English

Subjects

Structural Biology

Journal Section

Short Communication

Publication Date

December 15, 2021

Submission Date

April 30, 2021

Acceptance Date

August 6, 2021

Published in Issue

Year 1970 Volume: 38 Number: 4

APA
Çağlayan, P. (2021). Characterization of Planococcus dechangensis isolated from a water sample of Çamaltı Saltern. Ege Journal of Fisheries and Aquatic Sciences, 38(4), 527-531. https://doi.org/10.12714/egejfas.38.4.15