Journal articles on the topic 'Pseudozyma antarctica'

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1

Wu, Jing, Hongjiang Wang, Bin Yang, Wei Song, Chenchen Liang, and Liming Liu. "Efficient production of (R)-3-TBDMSO glutaric acid methyl monoester by manipulating the substrate pocket of Pseudozyma antarctica lipase B." RSC Advances 7, no. 61 (2017): 38264–72. http://dx.doi.org/10.1039/c7ra06016e.

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Efficient production of optically pure (R)-3-substituted glutaric acid methyl monoesters, the multifunctional chiral building blocks used in the pharmaceutical industry, by manipulating the substrate pocket of Pseudozyma antarctica lipase B.
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2

Narayanan, Niju, and C. Perry Chou. "Alleviation of Proteolytic Sensitivity To Enhance Recombinant Lipase Production in Escherichia coli." Applied and Environmental Microbiology 75, no. 16 (June 19, 2009): 5424–27. http://dx.doi.org/10.1128/aem.00740-09.

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ABSTRACT Two amino acids, Leu149 and Val223, were identified as proteolytically sensitive when Pseudozyma antarctica lipase (PalB) was heterologously expressed in Escherichia coli. The functional expression was enhanced using the double mutant for cultivation. However, the recombinant protein production was still limited by PalB misfolding, which was resolved by DsbA coexpression.
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3

Morita, Tomotake, Masaaki Konishi, Tokuma Fukuoka, Tomohiro Imura, and Dai Kitamoto. "Physiological differences in the formation of the glycolipid biosurfactants, mannosylerythritol lipids, between Pseudozyma antarctica and Pseudozyma aphidis." Applied Microbiology and Biotechnology 74, no. 2 (February 2007): 307–15. http://dx.doi.org/10.1007/s00253-006-0672-3.

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4

Tanaka, Takumi, Ken Suzuki, Hirokazu Ueda, Yuka Sameshima-Yamashita, and Hiroko Kitamoto. "Ethanol treatment for sterilization, concentration, and stabilization of a biodegradable plastic–degrading enzyme from Pseudozyma antarctica culture supernatant." PLOS ONE 16, no. 6 (June 4, 2021): e0252811. http://dx.doi.org/10.1371/journal.pone.0252811.

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Biodegradable plastics must be sufficiently stable to maintain functionality during use but need to be able to degrade rapidly after use. We previously reported that treatment with an enzyme named PaE, secreted by the basidiomycete yeast Pseudozyma antarctica can speed up this degradation. To facilitate the production of large quantities of PaE, here, we aimed to elucidate the optimal conditions of ethanol treatment for sterilization of the culture supernatant and for concentration and stabilization of PaE. The results showed that Pseudozyma antarctica completely lost its proliferating ability when incubated in ≥20% (v/v) ethanol. When the ethanol concentration was raised to 90% (v/v), PaE formed a precipitate; however, its activity was restored completely when the precipitate was dissolved in water. To reduce ethanol use, PaE was successfully concentrated and recovered by sequential ammonium sulfate precipitation and ethanol precipitation steps. Over 90% of the activity in the original culture supernatant was recovered and the specific activity was increased 3.4-fold. By preparing the enzyme solution at a final concentration of 20% (v/v) ethanol, about 60% of the initial activity was maintained at ambient temperature for over 6 months without growth of microbes. We conclude that ethanol treatment is effective for sterilization, concentration, and stabilization of PaE, and that concentrating PaE by sequential ammonium sulfate precipitation and ethanol precipitation substantially increases the PaE purity and decreases ethanol use.
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5

Allen, Tom W., Habib A. Quayyum, Leon L. Burpee, and James W. Buck. "Effect of foliar disease on the epiphytic yeast communities of creeping bentgrass and tall fescue." Canadian Journal of Microbiology 50, no. 10 (October 1, 2004): 853–60. http://dx.doi.org/10.1139/w04-073.

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The effect of mechanical wounding or foliar diseases caused by Sclerotinia homoeocarpa or Rhizoctonia solani on the epiphytic yeast communities on creeping bentgrass and tall fescue were determined by leaf washing and dilution plating. Total yeast communities on healthy bentgrass and tall fescue leaves ranged from 7.9 × 103 to 1.4 × 105 CFU·cm–2 and from 2.4 × 103 to 1.6 × 104 CFU·cm–2, respectively. Mechanically wounded leaves (1 of 2 trials) and leaves with disease lesions (11 of 12 trials) supported significantly larger communities of phylloplane yeasts. Total yeast communities on S. homoeocarpa infected or R. solani infected bentgrass leaves were 3.6–10.2 times and 6.2–6.4 times larger, respectively, than the communities on healthy leaves. In general, healthy and diseased bentgrass leaves supported larger yeast communities than healthy or diseased tall fescue leaves. We categorized the majority of yeasts as white-pigmented species, including Cryptococcus laurentii, Cryptococcus flavus, Pseudozyma antarctica, Pseudozyma aphidis, and Pseudozyma parantarctica. The percentage of pink yeasts in the total yeast community ranged from 2.6% to 9.9% on healthy leaves and increased to 32.0%–44.7% on S. homoeocarpa infected leaves. Pink-pigmented yeasts included Rhodotorula glutinis, Rhodotorula mucilaginosa, Sakaguchia dacryoidea, and Sporidiobolus pararoseus. Foliar disease significantly affected community size and composition of epiphytic yeasts on bentgrass and tall fescue.Key words: dollar spot, phylloplane, Rhizoctonia blight.
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6

Shinozaki, Yukiko, Tomotake Morita, Xiao-hong Cao, Shigenobu Yoshida, Motoo Koitabashi, Takashi Watanabe, Ken Suzuki, et al. "Biodegradable plastic-degrading enzyme from Pseudozyma antarctica: cloning, sequencing, and characterization." Applied Microbiology and Biotechnology 97, no. 7 (June 8, 2012): 2951–59. http://dx.doi.org/10.1007/s00253-012-4188-8.

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7

Kunitake, Emi, Takumi Tanaka, Hirokazu Ueda, Akira Endo, Tohru Yarimizu, Etsuko Katoh, and Hiroko Kitamoto. "CRISPR/Cas9-mediated gene replacement in the basidiomycetous yeast Pseudozyma antarctica." Fungal Genetics and Biology 130 (September 2019): 82–90. http://dx.doi.org/10.1016/j.fgb.2019.04.012.

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8

Liu, Danni, Peter Trodler, Sabine Eiben, Katja Koschorreck, Monika Müller, Jürgen Pleiss, Steffen C. Maurer, Cecilia Branneby, Rolf D. Schmid, and Bernhard Hauer. "Rational Design of Pseudozyma antarctica Lipase B Yielding a General Esterification Catalyst." ChemBioChem 11, no. 6 (March 5, 2010): 789–95. http://dx.doi.org/10.1002/cbic.200900776.

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9

Saika, Azusa, Hideaki Koike, Shuhei Yamamoto, Takahide Kishimoto, and Tomotake Morita. "Enhanced production of a diastereomer type of mannosylerythritol lipid-B by the basidiomycetous yeast Pseudozyma tsukubaensis expressing lipase genes from Pseudozyma antarctica." Applied Microbiology and Biotechnology 101, no. 23-24 (October 26, 2017): 8345–52. http://dx.doi.org/10.1007/s00253-017-8589-6.

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10

Marchand, G., E. Fortier, B. Neveu, S. Bolduc, F. Belzile, and R. R. Bélanger. "Alternative methods for genetic transformation of Pseudozyma antarctica, a basidiomycetous yeast-like fungus." Journal of Microbiological Methods 70, no. 3 (September 2007): 519–27. http://dx.doi.org/10.1016/j.mimet.2007.06.014.

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11

Larsen, M. W., D. Zielinska, M. Martinelle, A. Hildalgo, L. J. Jensen, U. T. Bornscheuer, and K. Hult. "Suppression of water as a nucleophile in Pseudozyma (Candida) antarctica lipase B catalysis." New Biotechnology 25 (September 2009): S127. http://dx.doi.org/10.1016/j.nbt.2009.06.431.

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12

Faria, Nuno Torres, Susana Marques, César Fonseca, and Frederico Castelo Ferreira. "Direct xylan conversion into glycolipid biosurfactants, mannosylerythritol lipids, by Pseudozyma antarctica PYCC 5048T." Enzyme and Microbial Technology 71 (April 2015): 58–65. http://dx.doi.org/10.1016/j.enzmictec.2014.10.008.

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13

Buzzini, Pietro, and Alessandro Martini. "Biodiversity of killer activity in yeasts isolated from the Brazilian rain forest." Canadian Journal of Microbiology 46, no. 7 (July 1, 2000): 607–11. http://dx.doi.org/10.1139/w00-032.

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The occurrence of killer activity against a panel composed of 22 industrially and (or) medically important yeasts was investigated in 438 yeast and yeast-like cultures belonging to 96 species, isolated from different environments of the Brazilian rain forest. Altogether, 26% of ascomycetes, 56% of basidiomycetes, and 42% of yeast-like cultures exhibited killer activity against at least one of the panel yeasts. More than 15 species never reported before as toxin producers were found, with Pseudozyma antarctica, Trichosporon asteroides, and Geotrichum klebahnii, showing the broader activity spectra. Plasmid curing did not cure the killer phenotypes of Candida maltosa, Debaryomyces hansenii, G. klebahnii, Tr. asteroides, Cryptococcus laurentii, and Ps. antarctica.Key words: yeasts, killer activity, tropical environments.
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14

Omae, Natsuki, Yuka Sameshima-Yamashita, Kazunori Ushimaru, Hideaki Koike, Hiroko Kitamoto, and Tomotake Morita. "Disruption of protease A and B orthologous genes in the basidiomycetous yeast Pseudozyma antarctica GB-4(0) yields a stable extracellular biodegradable plastic-degrading enzyme." PLOS ONE 16, no. 3 (March 17, 2021): e0247462. http://dx.doi.org/10.1371/journal.pone.0247462.

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The yeast Pseudozyma antarctica (currently designated Moesziomyces antarcticus) secretes a xylose-induced biodegradable plastic-degrading enzyme (PaE). To suppress degradation of PaE during production and storage, we targeted the inhibition of proteolytic enzyme activity in P. antarctica. Proteases A and B act as upper regulators in the proteolytic network of the model yeast, Saccharomyces cerevisiae. We searched for orthologous genes encoding proteases A and B in the genome of P. antarctica GB-4(0) based on the predicted amino acid sequences. We found two gene candidates, PaPRO1 and PaPRO2, with conserved catalytically important domains and signal peptides indicative of vacuolar protease function. We then prepared gene-deletion mutants of strain GB-4(0), ΔPaPRO1 and ΔPaPRO2, and evaluated PaE stability in culture by immunoblotting analysis. Both mutants exhibited sufficient production of PaE without degradation fragments, while the parent strain exhibited the degradation fragments. Therefore, we concluded that the protease A and B orthologous genes are related to the degradation of PaE. To produce a large quantity of PaE, we made a PaPRO2 deletion mutant of a PaE-overexpression strain named XG8 by introducing a PaE high-production cassette into the strain GB-4(0). The ΔPaPRO2 mutant of XG8 was able to produce PaE without the degradation fragments during large-scale cultivation in a 3-L jar fermenter for 3 days at 30°C. After terminating the agitation, the PaE activity in the XG8 ΔPaPRO2 mutant culture was maintained for the subsequent 48 h incubation at 25°C regardless of remaining cells, while activity in the XG8 control was reduced to 55.1%. The gene-deleted mutants will be useful for the development of industrial processes of PaE production and storage.
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15

Mawani, Jayata, Jagruti Jadhav, and Amit Pratap. "Fermentative Production of Mannosylerythritol Lipids using Sweetwater as Waste Substrate by Pseudozyma antarctica (MTCC 2706)." Tenside Surfactants Detergents 58, no. 4 (July 1, 2021): 246–58. http://dx.doi.org/10.1515/tsd-2020-2272.

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Abstract Mannosylerythritol lipids are glycolipid biosurfactants with promising industrial applications. However, their commercial production is hindered due to its high production cost. The current study investigates the use of sweetwater, a by-product of the fat-splitting industry in combination with soybean oil for the production of mannosylerythritol lipids using Pseudozyma antarctica (MTCC 2706). The optimum sweetwater and soybean oil concentration of 22% and 7% (w/v) yielded 7.52 g L–1and 21.5 g L–1 mannosylerythritol lipids at shake flask and fermenter level respectively. The structure and functional groups of mannosylerythritol lipids were confirmed by fourier transform infrared (FTIR) spectroscopy, liquid chromatography-mass spectrometry (LC/MS) and 1H- and 13C-nuclear magnetic resonance (NMR) analysis. Surfactant properties, such as surface tension, critical micelle concentration, foaming and emulsification of mannosylerythritol lipids were also explored.
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16

Levinson, William E., Cletus P. Kurtzman, and Tsung Min Kuo. "Production of itaconic acid by Pseudozyma antarctica NRRL Y-7808 under nitrogen-limited growth conditions." Enzyme and Microbial Technology 39, no. 4 (August 2006): 824–27. http://dx.doi.org/10.1016/j.enzmictec.2006.01.005.

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17

Morita, Tomotake, Hideaki Koike, Hiroko Hagiwara, Emi Ito, Masayuki Machida, Shun Sato, Hiroshi Habe, and Dai Kitamoto. "Genome and Transcriptome Analysis of the Basidiomycetous Yeast Pseudozyma antarctica Producing Extracellular Glycolipids, Mannosylerythritol Lipids." PLoS ONE 9, no. 2 (February 24, 2014): e86490. http://dx.doi.org/10.1371/journal.pone.0086490.

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18

Törnvall, Ulrika, Martin Hedström, Karin Schillén, and Rajni Hatti-Kaul. "Structural, functional and chemical changes in Pseudozyma antarctica lipase B on exposure to hydrogen peroxide." Biochimie 92, no. 12 (December 2010): 1867–75. http://dx.doi.org/10.1016/j.biochi.2010.07.008.

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19

Ujiie, Ayana, Hideo Nakano, and Yugo Iwasaki. "Extracellular production of Pseudozyma (Candida) antarctica lipase B with genuine primary sequence in recombinant Escherichia coli." Journal of Bioscience and Bioengineering 121, no. 3 (March 2016): 303–9. http://dx.doi.org/10.1016/j.jbiosc.2015.07.001.

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20

Morita, Tomotake, Emi Ito, Hiroko K. Kitamoto, Kaoru Takegawa, Tokuma Fukuoka, Tomohiro Imura, and Dai Kitamoto. "Identification of the gene PaEMT1 for biosynthesis of mannosylerythritol lipids in the basidiomycetous yeast Pseudozyma antarctica." Yeast 27, no. 11 (November 2010): 905–17. http://dx.doi.org/10.1002/yea.1794.

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21

Bhangale, Akash, Sushant Wadekar, Sandeep Kale, and Amit Pratap. "Optimization and monitoring of water soluble substrate for synthesis of mannosylerythritol lipids by Pseudozyma antarctica (ATCC 32657)." Biotechnology and Bioprocess Engineering 18, no. 4 (August 2013): 679–85. http://dx.doi.org/10.1007/s12257-012-0647-4.

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22

Morita, Tomotake, Masaaki Konishi, Tokuma Fukuoka, Tomohiro Imura, and Dai Kitamoto. "Microbial conversion of glycerol into glycolipid biosurfactants, mannosylerythritol lipids, by a basidiomycete yeast, Pseudozyma antarctica JCM 10317T." Journal of Bioscience and Bioengineering 104, no. 1 (July 2007): 78–81. http://dx.doi.org/10.1263/jbb.104.78.

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23

Watanabe, Takashi, Tomotake Morita, Hideaki Koike, Tohru Yarimizu, Yukiko Shinozaki, Yuka Sameshima-Yamashita, Shigenobu Yoshida, Motoo Koitabashi, and Hiroko Kitamoto. "High-level recombinant protein production by the basidiomycetous yeast Pseudozyma antarctica under a xylose-inducible xylanase promoter." Applied Microbiology and Biotechnology 100, no. 7 (December 23, 2015): 3207–17. http://dx.doi.org/10.1007/s00253-015-7232-7.

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24

Świderek, Katarzyna, Sergio Martí, and Vicent Moliner. "Theoretical Study of Primary Reaction of Pseudozyma antarctica Lipase B as the Starting Point To Understand Its Promiscuity." ACS Catalysis 4, no. 2 (January 3, 2014): 426–34. http://dx.doi.org/10.1021/cs401047k.

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Watanabe, Takashi, Yukiko Shinozaki, Shigenobu Yoshida, Motoo Koitabashi, Yuka Sameshima-Yamashita, Takeshi Fujii, Tokuma Fukuoka, and Hiroko Kuze Kitamoto. "Xylose induces the phyllosphere yeast Pseudozyma antarctica to produce a cutinase-like enzyme which efficiently degrades biodegradable plastics." Journal of Bioscience and Bioengineering 117, no. 3 (March 2014): 325–29. http://dx.doi.org/10.1016/j.jbiosc.2013.09.002.

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Otsu, Moeko, Yuichi Suzuki, Afifa Ayu Koesoema, Hai Nam Hoang, Mayumi Tamura, and Tomoko Matsuda. "CO2-expanded liquids as solvents to enhance activity of Pseudozyma antarctica lipase B towards ortho-substituted 1-phenylethanols." Tetrahedron Letters 61, no. 42 (October 2020): 152424. http://dx.doi.org/10.1016/j.tetlet.2020.152424.

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Morita, Tomotake, Masaaki Konishi, Tokuma Fukuoka, Tomohiro Imura, and Dai Kitamoto. "Analysis of expressed sequence tags from the anamorphic basidiomycetous yeast,Pseudozyma antarctica, which produces glycolipid biosurfactants, mannosylerythritol lipids." Yeast 23, no. 9 (2006): 661–71. http://dx.doi.org/10.1002/yea.1386.

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28

Wada, Keisuke, Hideaki Koike, Tatsuya Fujii, and Tomotake Morita. "Targeted transcriptomic study of the implication of central metabolic pathways in mannosylerythritol lipids biosynthesis in Pseudozyma antarctica T-34." PLOS ONE 15, no. 1 (January 10, 2020): e0227295. http://dx.doi.org/10.1371/journal.pone.0227295.

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Kitamoto, Hiroko, Shigenobu Yoshida, Motoo Koitabashi, Kimiko Yamamoto-Tamura, Hirokazu Ueda, Tohru Yarimizu, and Yuka Sameshima-Yamashita. "Enzymatic degradation of poly-butylene succinate- co -adipate film in rice husks by yeast Pseudozyma antarctica in indoor conditions." Journal of Bioscience and Bioengineering 125, no. 2 (February 2018): 199–204. http://dx.doi.org/10.1016/j.jbiosc.2017.08.017.

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Yoshida, Shigenobu, Tomotake Morita, Yukiko Shinozaki, Takashi Watanabe, Yuka Sameshima-Yamashita, Motoo Koitabashi, Dai Kitamoto, and Hiroko Kitamoto. "Mannosylerythritol lipids secreted by phyllosphere yeast Pseudozyma antarctica is associated with its filamentous growth and propagation on plant surfaces." Applied Microbiology and Biotechnology 98, no. 14 (April 5, 2014): 6419–29. http://dx.doi.org/10.1007/s00253-014-5675-x.

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31

Pfluck, Ana C. D., Dragana P. C. de Barros, Abel Oliva, and Luis P. Fonseca. "Enzymatic Poly(octamethylene suberate) Synthesis by a Two-Step Polymerization Method Based on the New Greener Polymer-5B Technology." Processes 10, no. 2 (January 25, 2022): 221. http://dx.doi.org/10.3390/pr10020221.

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Here, we report a new two-step enzymatic polymerization strategy for the synthesis of poly(octamethylene suberate) (POS) using an immobilized Pseudozyma antarctica lipase B (IMM-PBLI). The strategy overcomes the lack of enzymatic POS synthesis in solvent-free systems and increases the final polymer molecular weight. In the first step, the direct polycondensation of suberic acid and 1,8-octanediol was catalyzed by IMM-PBLI at 45 °C, leading to the production of prepolymers with molecular weights (MWs) of 2800, 3400, and 4900 g mol−1 after 8 h in miniemulsion, water, and an organic solvent (cyclohexane: tetrahydrofuran 5:1 v/v), respectively. In the second polymerization step, wet prepolymers were incubated at 60 or 80 °C, at atmospheric pressure, in the presence of IMM-PBLI, and without stirring. The final POS polymers showed a significant increase in MW to 5000, 5800, and 19,800 g mol−1 (previously synthesized in miniemulsion, water, or organic solvent, respectively). FTIR analysis of the final polymers confirmed the successful POS synthesis and a high degree of monomer conversion. This innovative two-step polymerization strategy opens up a new opportunity for implementing greener and more environmentally friendly processes for synthesizing biodegradable polyesters.
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Fotiadou, Renia, Michaela Patila, Mohamed Amen Hammami, Apostolos Enotiadis, Dimitrios Moschovas, Kyriaki Tsirka, Konstantinos Spyrou, et al. "Development of Effective Lipase-Hybrid Nanoflowers Enriched with Carbon and Magnetic Nanomaterials for Biocatalytic Transformations." Nanomaterials 9, no. 6 (May 28, 2019): 808. http://dx.doi.org/10.3390/nano9060808.

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In the present study, hybrid nanoflowers (HNFs) based on copper (II) or manganese (II) ions were prepared by a simple method and used as nanosupports for the development of effective nanobiocatalysts through the immobilization of lipase B from Pseudozyma antarctica. The hybrid nanobiocatalysts were characterized by various techniques including scanning electron microscopy (SEM), energy dispersion spectroscopy (EDS), X-ray diffraction (XRD), Raman spectroscopy, and Fourier transform infrared spectroscopy (FTIR). The effect of the addition of carbon-based nanomaterials, namely graphene oxide and carbon nanotubes, as well as magnetic nanoparticles such as maghemite, on the structure, catalytic activity, and operational stability of the hybrid nanobiocatalysts was also investigated. In all cases, the addition of nanomaterials during the preparation of HNFs increased the catalytic activity and the operational stability of the immobilized biocatalyst. Lipase-based magnetic nanoflowers were effectively applied for the synthesis of tyrosol esters in non-aqueous media, such as organic solvents, ionic liquids, and environmental friendly deep eutectic solvents. In such media, the immobilized lipase preserved almost 100% of its initial activity after eight successive catalytic cycles, indicating that these hybrid magnetic nanoflowers can be applied for the development of efficient nanobiocatalytic systems.
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Watanabe, Takashi, Yukiko Shinozaki, Ken Suzuki, Motoo Koitabashi, Shigenobu Yoshida, Yuka Sameshima-Yamashita, and Hiroko Kuze Kitamoto. "Production of a biodegradable plastic-degrading enzyme from cheese whey by the phyllosphere yeast Pseudozyma antarctica GB-4(1)W." Journal of Bioscience and Bioengineering 118, no. 2 (August 2014): 183–87. http://dx.doi.org/10.1016/j.jbiosc.2014.01.007.

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Sameshima-Yamashita, Yuka, Hirokazu Ueda, Motoo Koitabashi, and Hiroko Kitamoto. "Pretreatment with an esterase from the yeast Pseudozyma antarctica accelerates biodegradation of plastic mulch film in soil under laboratory conditions." Journal of Bioscience and Bioengineering 127, no. 1 (January 2019): 93–98. http://dx.doi.org/10.1016/j.jbiosc.2018.06.011.

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Matsuzawa, Tomohiko, Tomoko Maehara, Yasushi Kamisaka, Yuko Ayabe-Chujo, Hiroaki Takaku, and Katsuro Yaoi. "Identification and characterization of Pseudozyma antarctica Δ12 fatty acid desaturase and its utilization for the production of polyunsaturated fatty acids." Journal of Bioscience and Bioengineering 130, no. 6 (December 2020): 604–9. http://dx.doi.org/10.1016/j.jbiosc.2020.07.019.

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Ueda, Hirokazu, Ichiro Mitsuhara, Jun Tabata, Soichi Kugimiya, Takashi Watanabe, Ken Suzuki, Shigenobu Yoshida, and Hiroko Kitamoto. "Extracellular esterases of phylloplane yeast Pseudozyma antarctica induce defect on cuticle layer structure and water-holding ability of plant leaves." Applied Microbiology and Biotechnology 99, no. 15 (March 19, 2015): 6405–15. http://dx.doi.org/10.1007/s00253-015-6523-3.

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37

Shinozaki, Yukiko, Yoshihiro Kikkawa, Shun Sato, Tokuma Fukuoka, Takashi Watanabe, Shigenobu Yoshida, Toshiaki Nakajima-Kambe, and Hiroko K. Kitamoto. "Enzymatic degradation of polyester films by a cutinase-like enzyme from Pseudozyma antarctica: surface plasmon resonance and atomic force microscopy study." Applied Microbiology and Biotechnology 97, no. 19 (January 22, 2013): 8591–98. http://dx.doi.org/10.1007/s00253-012-4673-0.

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Fukuoka, Tokuma, Tomotake Morita, Masaaki Konishi, Tomohiro Imura, Hideki Sakai, and Dai Kitamoto. "Structural characterization and surface-active properties of a new glycolipid biosurfactant, mono-acylated mannosylerythritol lipid, produced from glucose by Pseudozyma antarctica." Applied Microbiology and Biotechnology 76, no. 4 (July 3, 2007): 801–10. http://dx.doi.org/10.1007/s00253-007-1051-4.

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39

Bhangale, Akash P., Sushant D. Wadekar, Sandeep B. Kale, Suraj N. Mali, and Amit P. Pratap. "Non-traditional oils with water-soluble substrate as cell growth booster for the production of mannosylerythritol lipids by Pseudozyma antarctica (ATCC 32657) with their antimicrobial activity." Tenside Surfactants Detergents 59, no. 2 (February 28, 2022): 122–33. http://dx.doi.org/10.1515/tsd-2021-2366.

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Abstract Among glycolipids, mannosylerythritol lipids (MEL), are mild and environmentally friendly surfactants used in various industrial applications. MELs are produced by biofermentation using non-traditional oils with various water-soluble carbon sources as cell growth booster. This substrate affects the production yield and cost of MEL. In this research work, the non-traditional oils jatropha oil, karanja oil and neem oil were used as new substrates along with glucose, glycerol and honey as new water-soluble substrates. All these oils are new feedstocks for the production of MEL using Pseudozyma antarctica (ATCC 32657). Jatropha oil, karanja oil and neem oil with honey as substrates resulted in higher MEL yields of (8.07, 7.75, and 1.86) g/L and better cell growth of (8.07, 7.75, and 1.86) g/L, respectively, than non-traditional oils with glucose and glycerol as substrates. Neem oil gave a lower yield of MEL (1.54 g/L) as well as cell growth (6.06 g/L) compared to jatropha oil and karanja oil (7.03 and 6.17) g/L, respectively. Crude MEL from the fermentation broth was detected by thin-layer chromatography (TLC), Fourier transform infrared spectrommetry (FT-IR), high performance liquid chromatography (HPLC) and proton nuclear magnetic resonance spectroscopy (1H NMR). Purified MEL has been used as an antimicrobial agent in cosmetic products associated with gram-positive and gram-negative bacteria and fungi.
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Imura, Tomohiro, Seya Ito, Reiko Azumi, Hiroshi Yanagishita, Hideki Sakai, Masahiko Abe, and Dai Kitamoto. "Monolayers assembled from a glycolipid biosurfactant from Pseudozyma (Candida) antarctica serve as a high-affinity ligand system for immunoglobulin G and M." Biotechnology Letters 29, no. 6 (March 7, 2007): 865–70. http://dx.doi.org/10.1007/s10529-007-9335-4.

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Flores, Ronilo Jose D., Takao Ohashi, Kanae Sakai, Tohru Gonoi, Hiroko Kawasaki, and Kazuhito Fujiyama. "The neutral N-linked glycans of the Basidiomycetous yeasts Pseudozyma antarctica and Malassezia furfur (Subphylum Ustilaginomycotina)." Journal of General and Applied Microbiology 65, no. 2 (2019): 53–63. http://dx.doi.org/10.2323/jgam.2018.05.003.

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Sameshima-Yamashita, Yuka, Takashi Watanabe, Takumi Tanaka, Shun Tsuboi, Tohru Yarimizu, Tomotake Morita, Hideaki Koike, Ken Suzuki, and Hiroko Kitamoto. "Construction of a Pseudozyma antarctica strain without foreign DNA sequences (self-cloning strain) for high yield production of a biodegradable plastic-degrading enzyme." Bioscience, Biotechnology, and Biochemistry 83, no. 8 (February 3, 2019): 1547–56. http://dx.doi.org/10.1080/09168451.2019.1571898.

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Sato, Shun, Azusa Saika, Yukiko Shinozaki, Takashi Watanabe, Ken Suzuki, Yuka Sameshima-Yamashita, Tokuma Fukuoka, Hiroshi Habe, Tomotake Morita, and Hiroko Kitamoto. "Degradation profiles of biodegradable plastic films by biodegradable plastic-degrading enzymes from the yeast Pseudozyma antarctica and the fungus Paraphoma sp. B47-9." Polymer Degradation and Stability 141 (July 2017): 26–32. http://dx.doi.org/10.1016/j.polymdegradstab.2017.05.007.

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Nyyssölä, Antti, Hanna Miettinen, Hanna Kontkanen, Martina Lille, Riitta Partanen, Susanna Rokka, Eila Järvenpää, Raija Lantto, and Kristiina Kruus. "Treatment of milk fat with sn-2 specific Pseudozyma antarctica lipase A for targeted hydrolysis of saturated medium and long-chain fatty acids." International Dairy Journal 41 (February 2015): 16–22. http://dx.doi.org/10.1016/j.idairyj.2014.09.003.

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Morita, Tomotake, Emi Ito, Tokuma Fukuoka, Tomohiro Imura, and Dai Kitamoto. "The role of PaAAC1 encoding a mitochondrial ADP/ATP carrier in the biosynthesis of extracellular glycolipids, mannosylerythritol lipids, in the basidiomycetous yeast Pseudozyma antarctica." Yeast 27, no. 7 (February 10, 2010): 379–88. http://dx.doi.org/10.1002/yea.1761.

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Jan, Anne-Hélène, Maeva Subileau, Charlotte Deyrieux, Véronique Perrier, and Éric Dubreucq. "Elucidation of a key position for acyltransfer activity in Candida parapsilosis lipase/acyltransferase (CpLIP2) and in Pseudozyma antarctica lipase A (CAL-A) by rational design." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1864, no. 2 (February 2016): 187–94. http://dx.doi.org/10.1016/j.bbapap.2015.11.006.

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47

Pfluck, Ana C. D., Dragana P. C. de Barros, and Luis P. Fonseca. "Biodegradable Polyester Synthesis in Renewed Aqueous Polycondensation Media: The Core of the New Greener Polymer-5B Technology." Processes 9, no. 2 (February 16, 2021): 365. http://dx.doi.org/10.3390/pr9020365.

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An innovative enzymatic polycondensation of dicarboxylic acids and dialcohols in aqueous polymerization media using free and immobilized lipases was developed. Various parameters (type of lipases, temperature, pH, stirring type and rate, and monomer carbon chain length) of the polycondensation in an oil-in-water (o/w) miniemulsion (>80% in water) were evaluated. The best results for polycondensation were achieved with an equimolar monomer concentration (0.5 M) of octanedioic acid and 1,8-octanediol in the miniemulsion and water, both at initial pH 5.0 with immobilized Pseudozyma antarctica lipase B (PBLI). The synthesized poly(octamethylene suberate) (POS) in the miniemulsion is characterized by a molecular weight of 7800 g mol−1 and a conversion of 98% at 45 °C after 48 h of polycondensation in batch operation mode. A comparative study of polycondensation using different operation modes (batch and fed-batch), stirring type, and biocatalyst reutilization in the miniemulsion, water, and an organic solvent (cyclohexane:tetrahydrofuran 5:1 v/v) was performed. Regarding the polymer molecular weight and conversion (%), batch operation mode was more appropriate for the synthesis of POS in the miniemulsion and water, and fed-batch operation mode showed better results for polycondensation in the organic solvent. The miniemulsion and water used as polymerization media showed promising potential for enzymatic polycondensation since they presented no enzyme inhibition for high monomer concentrations and excellent POS synthesis reproducibility. The PBLI biocatalyst presented high reutilization capability over seven cycles (conversion > 90%) and high stability equivalent to 72 h at 60 °C on polycondensation in the miniemulsion and water. The benefits of polycondensation in aqueous media using an o/w miniemulsion or water are the origin of the new concept strategy of the green process with a green product that constitutes the core of the new greener polymer-5B technology.
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Ueda, Hirokazu, Jun Tabata, Yasuyo Seshime, Kazuo Masaki, Yuka Sameshima-Yamashita, and Hiroko Kitamoto. "Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity." Bioscience, Biotechnology, and Biochemistry 85, no. 8 (June 23, 2021): 1890–98. http://dx.doi.org/10.1093/bbb/zbab113.

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ABSTRACT Phylloplane yeast genera Pseudozyma and Cryptococcus secrete biodegradable plastic (BP)-degrading enzymes, termed cutinase-like enzymes (CLEs). Although CLEs contain highly conserved catalytic sites, the whole protein exhibits ≤30% amino acid sequence homology with cutinase. In this study, we analyzed whether CLEs exhibit cutinase activity. Seventeen Cryptococcus magnus strains, which degrade BP at 15 °C, were isolated from leaves and identified the DNA sequence of the CLE in one of the strains. Cutin was prepared from tomato leaves and treated with CLEs from 3 Cryptococcus species (C. magnus, Cryptococcus flavus, and Cryptococcus laurentii) and Pseudozyma antarctia (PaE). A typical cutin monomer, 10,16-dihydroxyhexadecanoic acid, was detected in extracts of the reaction solution via gas chromatography–mass spectrometry, showing that cutin was indeed degraded by CLEs. In addition to the aforementioned monomer, separation analysis via thin-layer chromatography detected high-molecular-weight products resulting from the breakdown of cutin by PaE, indicating that PaE acts as an endo-type enzyme.
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Dzięgielewska, Ewelina, and Marek Adamczak. "Evaluation of waste products in the synthesis of surfactants by yeasts." Chemical Papers 67, no. 9 (January 1, 2013). http://dx.doi.org/10.2478/s11696-013-0349-1.

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AbstractThe highest yields of biosurfactants were obtained by: (i) Pseudozyma antarctica (107.2 g L−1) cultivated in a medium containing post-refining waste; (ii) Pseudozyma aphidis (77.7 g L−1); and (iii) Starmerella bombicola (93.8 g L−1) both cultivated in a medium with soapstock; (iv)Pichia jadinii (67.3 g L−1) cultivated in a medium supplemented with waste frying oil. It was found that the biosurfactant synthesis yield increased in all strains when the cell surface hydrophobicity reached 70–80 %, enabling the microbial cells to make good contact with hydrophobic substrates. The lowest surface tension of the post-cultivation medium was from 32.0 mN m−1 to 37.8 mN m−1. However, this parameter (which was also determined by a drop collapse assay) was of limited use in monitoring biosurfactant synthesis in this study. The crude glycerol was not a good substrate for biosurfactant synthesis although, in the case of P. aphidis, 67.4 g L−1 of biosurfactants were obtained after cultivation in the medium supplemented with glycerol fraction (GF2). In a low-cost medium containing soapstock and whey permeate or molasses, about 90 g L−1 of mannosylerythritol lipids were synthesised by P. aphidis and approximately 40 g L−1 by P. antarctica.
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Sameshima-Yamashita, Yuka, Tohru Yarimizu, Hirohide Uenishi, Takumi Tanaka, and Hiroko Kitamoto. "Uracil-auxotrophic marker recycling system for multiple gene disruption in Pseudozyma antarctica." Bioscience, Biotechnology, and Biochemistry, May 24, 2022. http://dx.doi.org/10.1093/bbb/zbac075.

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Abstract The basidiomycetous yeast Pseudozyma antarctica, which has multiple auxotrophic markers, was constructed, without inserting a foreign gene, as the host strain for the introduction of multiple useful genes. P. antarctica was more resistant to ultraviolet (UV) irradiation than the model yeast Saccharomyces cerevisiae, and a Paura3 mutant (C867T) was obtained after 3 min of UV exposure. A uracil-auxotrophic marker (URA3) recycling system developed in ascomycetous yeasts and fungi was applied to the P. antarctica Paura3 strain. The PaLYS12 and PaADE2 loci were disrupted via site-directed homologous recombination of PaURA3 (pop-in), followed by the removal of PaURA3 (pop-out). In the obtained double auxotrophic strain (Palys12Δ, Paura3), PaADE2 was further disrupted, and PaURA3 was removed to obtain the triple auxotrophic strain PGB800 (Paura3, Palys12Δ, Paade2Δ). The whole-genome sequence of the PGB800 strain did not contain foreign genes used for genetic manipulation and disrupted PaADE2 and PaLYS12 and removed PaURA3, as planned.
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