期刊
WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
卷 37, 期 2, 页码 -出版社
SPRINGER
DOI: 10.1007/s11274-020-02976-2
关键词
Acidophilics; Halophilics; Metagenomics; Microbial lipases; Olive brine
资金
- Research Fund of Yildiz Technical University [2013-01-07-KAP02]
In this study, microbial analysis of cracked green olive brine from southern Turkey was conducted for the first time, revealing a high percentage of fungi, particularly from the phylum Ascomycota. Yeasts grown in high salt concentrations were found to produce lipase with high similarity to Candida diddensiae, with subsequent analysis showing cell-bound lipase activity at pH 3.0.
Searching for novel enzymes that could be active in organic solvents has become an area of interest in recent years. Olive brine naturally provides a suitable environment for the survival of halophilic and acidophilic microorganisms and the resulting genome is thought to be a gene source for determining the halophilic and acidophilic proteins that are active in a non-aqueous organic solvent medium, and so it has been used in several biotechnological and industrial applications. In this study, microbial analysis of natural, cracked green olive brine from the southern region of Turkey has been made by next-generation sequencing of the brine metagenome for the first time in the literature. The number of reads assigned to fungal operational taxonomic units was the highest percentage (73.04%) with the dominant representation of Ascomycota phylum (99% of fungi). Bacterial OTU was 3.56% of the reads and Proteobacteria phylum was 65% of the reads. The lipase production capacity of the yeasts that were grown on the media containing elevated concentrations of NaCl (1-3 M) was determined on a Rhodamine B-including medium. Molecular identification of the selected yeasts was performed and 90% of sequenced yeasts had a high level of similarity with Candida diddensiae, whereas 10% showed similarity to Candida boidinii. The hydrolytic lipase activities using olive oil were analyzed and both yeasts showed cell-bound lipase activity at pH 3.0.
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