PubMed · 5023946
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L Pospísil, A Kabátová. 1972. [Oxidase complex in Candida].. https://pubmed.ncbi.nlm.nih.gov/5023946/
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Candida yeasts represent a versatile yet underexploited platform for industrial biotechnology. These yeasts utilize a remarkably broad range of carbon sources, particularly for hydrophobic carbon sources, coupled with robust growth and diverse biosynthetic capacities, making them promising hosts for sustainable production of chemicals, fuels, and proteins. Despite these advantages, industrial deployment of Candida species has been hindered by concerns regarding opportunistic pathogenicity and the historical lack of efficient genetic manipulation tools, leading to a substantial gap between metabolic potential and practical utilization. Recent advances in functional genomics, genome editing, and systems metabolic engineering are rapidly overcoming these barriers, enabling more precise and efficient strain development. In this review, we systematically summarize recent progress in the metabolic engineering of Candida species as microbial cell factories, with particular emphasis on expanding genetic toolkits, utilizting renewable and non-conventional carbon sources, and biosynthesizing high-value compounds. In addition, we propose a biosafety-oriented classification framework to support their safe industrial deployment. Finally, we discuss current challenges and emerging opportunities, emphasizing that the synergy of synthetic biology and artificial intelligence-driven design holds the key to unlocking the biotechnological potential of Candida yeasts.
Culture supernatants of Candida albicans were examined for factors with inhibitory activity against the chemiluminescence of human neutrophils. By high resolution gel chromatography, a low-molecular-mass chemiluminescence inhibitor was isolated. The compound was identified as 2,4-(hydroxyphenyl)-ethanol. Half-maximum inhibition (IC50) of the chemiluminescence response of neutrophils phagocytizing opsonized zymosan or C. albicans occurred at 38.1 +/- 2.3 microM and 19.9 +/- 8.3 microM, respectively. As shown by flow cytometry, the compound protected C. albicans against phagocytic killing (IC50 = 73.8 +/- 16.9 microM). Substantially higher concentrations of the inhibitor were produced by C. albicans and C. tropicalis than by C. parapsilosis and C. glabrata, suggesting a potential role in pathogenicity ranking.
Two inorganic tin compounds, as well as mono- and tri-substituted methyl-, butyl-, and phenyltins were examined for their interactions with a hydrocarbon-using strain of Candida maltosa. Neither of the inorganic tins (SnII and SnIV) inhibited growth at concentrations up to 0.8 mM while binding to the yeast cells occurred to levels of 0.3 and 0.23 mM Sn/g cells, respectively. Neither inorganic tin caused leakage of potassium from the yeast cells. Among the organotins, tributyl- and triphenyltins caused total viability loss and near maximum potassium loss at initial concentrations of 0.08 mM. For these compounds binding to the cells increased with increasing initial concentrations to maximum values of 0.51 and 0.65 mM Sn/g cells respectively. The other organotin compounds were not inhibitory and did not cause potassium leakage from the cells. Tin from them became cell associated only in the cases of monobutyl- and monophenyl tin, which were bound at markedly lower levels (<0.1 mM Sn/g cells). These results are consistent with the conclusion that the inhibitory compounds can act on the yeast cell membrane but, although binding to the cells is a prerequisite for growth inhibition and cell leakage, no simple correlation was established between binding levels and toxicity effects.