Draft Genome Sequence of a Lipolytic Yeast, Candida aaseri SH-14.

We report here the draft genome sequence of the lipolytic yeast Candida aaseri SH-14, isolated from the compost of oil palm empty fruit bunches, and the identification of eight putative lipase genes. This genome information will provide the opportunity to produce potential lipases for a variety of industrial applications.

GENOME ANNOUNCEMENT

Extracellular microbial lipases (triacylglycerol hydrolase, EC 3.1.1.3) catalyze the hydrolysis of ester bonds between alcohols and carboxylic acids at the lipid-water interface (1). Lipases have been widely used for a broad range of biotechnological and industrial processes (2, 3) and have recently been utilized as an important biocatalyst for the production of biodiesel in the field of bioenergy (4). Although lipases are widely distributed in nature, yeast and fungi have the most commercial potential of the primary sources of lipases used in industrial applications (5). There are various yeasts with lipase-producing capacities; however, only a few have been commercially employed for bulk production (6, 7). Therefore, it is important to isolate and exploit lipolytic yeast species when finding novel lipases for the development of biotechnological and industrial processes. Herein, we present the draft genome sequence of Candida aaseri SH-14 as a potential lipase producer.

Candida aaseri (syn. Candida butyri) SH-14 is a lipolytic yeast isolated from the compost of oil palm empty fruit bunches. We conducted a genome sequencing of Candida aaseri SH-14 using the Illumina HiSeq 2500 platform at the Core Facility Management Center at the Korea Research Institute of Bioscience and Biotechnology (KRIBB). We obtained 42.8 million paired-end reads (approximately 400-fold coverage) and assembled them de novo using Velvet version 1.2.10, which was facilitated using VelvetOptimiser version 2.2.5 (8). The total size of the draft genome of C. aaseri SH-14 was 10,491,190 bp (62 scaffolds including 630 gaps). The N50 value and the length of the longest contig were 450,417 bp and 1,399,148 bp, respectively. The G+C content was 34.2%, and 126 tRNA-coding sequences were identified using tRNAscan-SE version 2.0 (9). Structural annotation was carried out using the Yeast Genome Annotation Pipeline (YGAP) (10), and Blast2GO was utilized for a functional prediction of the protein-coding sequences (11). As a result, a total of 5,380 proteins were predicted, and we confirmed that 5,037 of them have at least one Gene Ontology (GO) term.

Some Candida species, particularly Candida albicans, translate the CUG codon as serine instead of leucine; therefore, we have used the Bagheera server (http://www.motorprotein.de/bagheera) to analyze the CUG codon translation of the genes from C. aaseri SH-14 (12). The prediction suggested that C. aaseri SH-14 belongs to the CUG:Ser group of Candida species. We identified eight putative lipase genes from the genome of C. aaseri SH-14. Information on putative lipase genes is available from http://genoglobe.kr/kribb/candida_aaseri_2017, where the classification of the putative lipases was based on the oxyanion hole and conserved pentapeptide found in the Lipase Engineering Database (LED) (13, 14).

Accession number(s).

This whole-genome shotgun project has been deposited at DDBJ/ENA/GenBank under the accession no. LKAN00000000. The version described in this paper is version LKAN01000000.