• Journal of Microbiology and Biotechnology
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• 제18권9호
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• pp.1522-1528
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• 2008

The morphogenetic behavior of a tropical marine Yarrowia lipolytica strain on hydrophobic substrates was studied. Media containing coconut oil or palm kernel oil (rich in lauric and myristic acids) prepared in distilled water or seawater at a neutral pH supported 95% of the cells to undergo a transition from the yeast form to the mycelium form. With potassium laurate, 51 % of the cells were in the mycelium form, whereas with myristate, 32% were in the mycelium form. However, combinations of these two fatty acids in proportions that are present in coconut oil or palm kernel oil enhanced the mycelium formation to 65%. The culture also produced extracellular lipases during the morphogenetic change. The yeast cells were found to attach to the large droplets of the hydrophobic substrates during the transition, while the mycelia were associated with the aqueous phase. The alkane-grown yeast partitioned more efficiently in the hydrophobic phases when compared with the coconut oil-grown mycelia. A fatty acid analysis of the mycelial form revealed the presence of lauric acid in addition to the long-chain saturated and unsaturated fatty acids observed in the yeast form. The mycelia underwent a rapid transition to the yeast form with n-dodecane, a medium-chain aliphatic hydrocarbon. Thus, the fungus displayed a differential behavior towards the two types of saturated hydrophobic substrates.

• Journal of Applied Biological Chemistry
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• 제50권2호
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• pp.46-51
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• 2007

Lipases are industrially useful versatile enzymes that catalyze numerous different reactions. Among lipases functioning under extreme conditions, alkaline lipase is useful in detergent industry. Lipase from yeast strain Yarrowia lipolytica NRRL Y-2178 was most active under alkaline condition, and initial medium pH for most lipase production was also alkaline [Lee et al., 2007, J Microbiol Biotechnol, 17(6)]. High lipase production was achieved using Y. lipolytica NRRL Y-2178. Optimal incubation time for lipase production at $25^{\circ}C$ was 72 h. Optimal temperature, when incubated for 72 h, was $27.5^{\circ}C$. Lipase production but not cell growth was very sensitive to concentrations of glucose and glycerol as efficient carbon sources, showing optimal concentrations of 1.0 and 1.5% (w/v), respectively. Lipase production was highly stimulated by $Ca^{2+},\;K^+,\;and\;Na^+$, but was inhibited by $Co^{2+},\;Cu^{2+},\;Mn^{2+},\;Na^+,\;and\;Fe^{2+}$. Maximum lipase production at 0.1 mM $Ca^{2+}$ for 72 h incubation at $27.5^{\circ}C$ was 649 units/mL.

• Journal of Microbiology and Biotechnology
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• 제28권4호
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• pp.597-605
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• 2018

Acyl-CoA oxidases (ACOXs) play important roles in lipid metabolism, including peroxisomal fatty acid ${\beta}$-oxidation by the conversion of acyl-CoAs to 2-trans-enoyl-CoAs. The yeast Yarrowia lipolytica can utilize fatty acids as a carbon source and thus has extensive biotechnological applications. The crystal structure of ACOX3 from Y. lipolytica (YlACOX3) was determined at a resolution of $2.5{\AA}$. It contained two molecules per asymmetric unit, and the monomeric structure was folded into four domains; $N{\alpha}$, $N{\beta}$, $C{\alpha}1$, and $C{\alpha}2$ domains. The cofactor flavin adenine dinucleotide was bound in the dimer interface. The substrate-binding pocket was located near the cofactor, and formed at the interface between the $N{\alpha}$, $N{\beta}$, and $C{\alpha}1$ domains. Comparisons with other ACOX structures provided structural insights into how YlACOX has a substrate preference for short-chain acyl-CoA. In addition, the structure of YlACOX3 was compared with those of medium- and long-chain ACOXs, and the structural basis for their differences in substrate specificity was discussed.

• Journal of Microbiology
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• 제41권2호
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• pp.121-128
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• 2003

The identification of genes involved in true hypha formation is important in the study of mechanisms underlying the morphogenetic switch in yeast. We isolated a gene responsible for the morphogenetic switch in Yarrowia lipolytica, which forms true hyphae in response to serum or N-acetylglucosamine. The isolated gene, encoding 847 amino acids, had sequence identities of 27% and 25% with the Bud6 (Aip3) proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, respectively. Disruption of this gene, designated YIBUD6, in haploid and diploid strains significantly reduced the ability of Y. lipolytica to switch from the yeast form to the hyphal form in hypha-inducing media. It was also found that YIBud6$\Delta$ mutants were rounder than the wild type when grown in the yeast form. These results indicate that the YIBud6 protein is necessary for hyphal growth and cell polarity in both haploid and diploid Y. lipolytica cells.

• Journal of Microbiology and Biotechnology
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• 제11권1호
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• pp.112-117
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• 2001

A nonconventional yeast strain Y103 capable of degrading several aromatic hydrocarbons was isolated from the wastewater of the Yocheon industrial complex. The strain Y103 was identified as Yarrowia lipolytica on the basis of its unique dimorphic and biochemical characteristics as determined by a Biolog test. Y. lipolytica Y103 was found to degrade phenol and 4-chlorophenol to produce catechol. The catechol then will be further degraded to produce 2-hydroxymuconic semialdehyde via meta-cleavage. These results indicate that strain Y103 degrades 4-chlorophenol, phenol, and catechol through a consecutive reaction to produce 2-hydroxymuconic semialdehyde. The most active degradation of phenol by Y. lipolytica Y103 occurred with a 0.5 mM phenl concentration in an MM2 medium at $30^{\circ}C$ and pH 7.0.

• 한국미생물·생명공학회지
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• 제24권4호
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• pp.452-458
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• 1996

A yeast strain TH65 producing a high level of proteinase under alkaline condition was isolated, and identified as Yarrowia lipolytica by morphological, physiological, and biochemical characteristics. In proteinase productivity, glycerol and glucose among tested carbon sources were very effective, and optimum concentration of glucose was 0.5%. Skim milk was found to be most effective nitrogen source in productivity, and its optimum concentration was 0.6%. But, cysteine, cystine and tryptophane decreased the proteinase productivity. Yeast extract was relatively effective at the range of 0.1-0.5%. The yeast showed maximum production of proteinase at 18$\circ$C, pH 9-11, and cultivation time of 36 hours.

• Journal of Microbiology
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• 제40권2호
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• pp.173-177
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• 2002

In order to identify Yawowia lipolytica genes induced by serum, cDNA representational difference analysis was performed using a PCR-select CDNA subtraction method. One of the genes cloned from the subtraction was a gene (YIMBFl) homologous to Saccharomyces cerevisiae MBF1 encoding the coactivator multiprotein bridging factor 1. Disruption of YIMBFl revealed that the gene was net essential for viability, and the Ylmbf△ strain did not show any distinct phenotypic change on solid serum medium. In liquid medium, however. a difference was found in the ability to maintain hyphae induced by serum. This result suggests that the YIMbf1 protein may mediate transcriptional activation of certain genes involved in the hypha fonmation of Y. lipolytica.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2003년도 생물공학의 동향(XII)
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• pp.28-29
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• 2003

• Journal of Microbiology
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• 제37권3호
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• pp.128-135
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• 1999

Among oil-degrading microorganisms isolated from oil-polluted industrial areas, one yeast strain showed high degradation activity of aliphatic hydrocarbons. From the analyses of 18S rRNA sequences, fatty acid, coenzyme Q system, G+C content of DNA, and biochemical characteristics, the strain was identified as Yarrowia lipolytica 180. Y. lipolytica 180 degraded 94% of aliphatic hydrocarbons in minimal salts medium containing 0.2% (v/v) of Arabian light crude oil within 3 days at 25$^{\circ}C$. Optimal growth conditions for temperature, pH, NaCl concentration, and crude oil concentration were 30$^{\circ}C$, pH 5-7, 1%, and 2% (v/v), respectively. Y. lipolytica 180 reduced surface tension when cultured on hydrocarbon substrates (1%, v/v), and the measured values of the surface tension were in the range of 51 to 57 dynes/cm. Both the cell free culture broth and cell debris of Y. lipolytica 180 were capable of emulsifying 2% (v/v) crude oil by itself. They were also capable of degrading crude oil (2%). The strain showed a cell surface hydrophobicity higher than 90%, which did not require hydrocarbon substrates for its induction. These results suggest that Y. lipolytica has high oil-degrading activity through its high emulsifying activity and cell hydrophobicity, and further indicate that the cell surface is responsible for the metabolism of aliphatic hydrocarbons.

• Journal of Microbiology and Biotechnology
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• 제17권6호
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• pp.1054-1057
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• 2007

Lipases are industrially useful versatile enzymes that catalyze numerous different reactions including hydrolysis of triglycerides, transesterification, and chiral synthesis of esters under natural conditions. Although lipases from various sources have been widely used in industrial applications, such as in food, chemical, pharmaceutical, and detergent industries, there are still substantial current interests in developing new microbial lipases, specifically those functioning in abnormal conditions. We screened 17 lipase-producing yeast strains, which were prescreened for substrate specificity of lipase from more than 500 yeast strains from the Agricultural Research Service Culture Collection (Peoria, IL, U.S.A.), and selected Yarrowia lipolytica NRRL Y-2178 as a best lipase producer. This report presents new finding and optimal production of a novel extracellular alkaline lipase from Y. lipolytica NRRL Y-2178. Optimal culture conditions for lipase production by Y. lipolytica NRRL Y-2178 were 72 h incubation time, $27.5^{\circ}C$, pH 9.0. Glycerol and glucose were efficiently used as the most efficient carbon sources, and a combination of yeast extract and peptone was a good nitrogen source for lipase production by Y. lipolytica NRRL Y-2178. These results suggested that Y. lipolytica NRRL Y-2178 shows good industrial potential as a new alkaline lipase producer.