Identifying carbohydrate-active enzymes of Cutaneotrichosporon oleaginosus using systems biology
Open accessAbstract
BACKGROUND: The oleaginous yeast Cutaneotrichosporon oleaginosus represents one of the most promising microbial platforms for resource-efficient and scalable lipid production, with the capacity to accept a wide range of carbohydrates encapsulated in complex biomass waste or lignocellulosic hydrolysates. Currently, data related to molecular aspects of the metabolic utilisation of oligomeric carbohydrates are sparse. In addition, comprehensive proteomic information for C. oleaginosus focusing on carbohydrate metabolism is not available. RESULTS: In this study, we conducted a systematic analysis of carbohydrate intake and utilisation by C. oleaginosus and investigated the influence of different di- and trisaccharide as carbon sources. Changes in the cellular growth and morphology could be observed, depending on the selected carbon source. The greatest changes in morphology were observed in media containing trehalose. A comprehensive proteomic analysis of secreted, cell wall-associated, and cytoplasmatic proteins was performed, which highlighted differences in the composition and quantity of secreted proteins, when grown on different disaccharides. Based on the proteomic data, we performed a relative quantitative analysis of the identified proteins (using glucose as the reference carbon source) and observed carbohydrate-specific protein distributions. When using cellobiose or lactose as the carbon source, we detected three- and five-fold higher diversity in terms of the respective hydrolases released. Furthermore, the analysis of the secreted enzymes enabled identification of the motif with the consensus sequence LALL[LA]L[LA][LA]AAAAAAA as a potential signal peptide. CONCLUSIONS: Relative quantification of spectral intensities from crude proteomic datasets enabled the identification of new enzymes and provided new insights into protein secretion, as well as the molecular mechanisms of carbo-hydrolases involved in the cleavage of the selected carbon oligomers. These insights can help unlock new substrate sources for C. oleaginosus, such as low-cost by-products containing difficult to utilize carbohydrates. In addition, information regarding the carbo-hydrolytic potential of C. oleaginosus facilitates a more precise engineering approach when using targeted genetic approaches. This information could be used to find new and more cost-effective carbon sources for microbial lipid production by the oleaginous yeast C. oleaginosus.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Cutaneotrichosporon oleaginosus yeast is capable of producing up to 90% (w/w) lipids per biomass in a fermentation process, and can be grown on residue streams.
“the production of second-generation biodiesel is possible from microbial lipids produced by organisms, such as Cutaneotrichosporon oleaginosus, a yeast capable of producing up to 90% (w/w) lipids per biomass in a fermentation process, which can be grown on residue streams (e.g., wheat bran hydrolysate medium) [46–49].”
From The potential of biofuels from first to fourth generation (2023) · cites this paper as [46]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Ultrastructural Characterization of the Lower Motor System in a Mouse Model of Krabbe Disease
Cappello, V., Marchetti, L., Parlanti, P., Landi, S., Tonazzini, I., Cecchini, M., Piazza, V., & Gemmi, M. (2016) · Scientific Reports · doi:10.1038/s41598-016-0001-8 · Cited by 13,097 · see citing works
SWISS-MODEL: homology modelling of protein structures and complexes
Waterhouse, A. M., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F. T., de Beer, T., Rempfer, C., Bordoli, L., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky427 · Cited by 13,005 · see citing works
MEME SUITE: tools for motif discovery and searching
Bailey, T. L., Boden, M., Buske, F. A., Frith, M., Grant, C. E., Clementi, L., Ren, J., Li, W. W., & Noble, W. S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp335 · Cited by 10,648 · see citing works
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,930 · see citing works
UniProt: a worldwide hub of protein knowledge
The UniProt Consortium (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1049 · Cited by 7,698 · see citing works
Microbial Cellulose Utilization: Fundamentals and Biotechnology
Lynd, L. R., Weimer, P. J., van Zyl, W. H., & Pretorius, I. S. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.3.506-577.2002 · Cited by 4,726 · see citing works
Nile red: a selective fluorescent stain for intracellular lipid droplets.
Greenspan, P., Mayer, E. P., & Fowler, S. D. (1985) · The Journal of cell biology · doi:10.1083/jcb.100.3.965 · Cited by 2,543 · see citing works
A Combined Transmembrane Topology and Signal Peptide Prediction Method
Käll, L., Krogh, A., & Sonnhammer, E. L. L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.016 · Cited by 2,474 · see citing works
Toward the estimation of the absolute quality of individual protein structure models
Benkert, P., Biasini, M., & Schwede, T. F. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq662 · Cited by 2,259 · see citing works
Guex, N., Peitsch, M. C., & Schwede, T. F. (2009) · Electrophoresis · doi:10.1002/elps.200900140 · Cited by 2,091 · see citing works
A knowledge base for predicting protein localization sites in eukaryotic cells
Nakai, K., & Kanehisa, M. I. (1992) · Genomics · doi:10.1016/s0888-7543(05)80111-9 · Cited by 1,512 · see citing works
Heterologous protein production using the Pichia pastoris expression system
Macauley‐Patrick, S., Fazenda, M. L., McNeil, B. W. J., & Harvey, L. M. (2005) · Yeast · doi:10.1002/yea.1208 · Cited by 1,226 · see citing works
QMEANDisCo—distance constraints applied on model quality estimation
Studer, G., Rempfer, C., Waterhouse, A. M., Gumienny, R., Haas, J., & Schwede, T. F. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz828 · Cited by 1,043 · see citing works
Meier, F., Brunner, A., Koch, S., Koch, H., Lubeck, M., Krause, M., Goedecke, N., Decker, J., Kosinski, T., Park, M. A., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir118.000900 · Cited by 946 · see citing works
Methods for Isolation, Phenotypic Characterization and Maintenance of Yeasts
Kurtzman, C. P., Fell, J. W., Boekhout, T., & Robert, V. (2011) · Elsevier eBooks · doi:10.1016/b978-0-444-52149-1.00007-0 · Cited by 842 · see citing works
Bertoni, M., Kiefer, F., Biasini, M., Bordoli, L., & Schwede, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-09654-8 · Cited by 791 · see citing works
Song, X., Gao, T., Wang, N., Feng, Q., You, X., Ye, T., Lei, Q., Zhu, Y., Xiong, M., Xia, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep24893 · Cited by 714 · see citing works
Yeast selection for fuel ethanol production in Brazil
Basso, L. C., de Amorim, H. V., Oliveira, A. J., & Lopes, M. L. (2008) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2008.00428.x · Cited by 587 · see citing works
van Maris, A. J. A., Abbott, D. A., Bellissimi, E., van den Brink, J., Kuyper, M., Luttik, M. A. H., Wisselink, H. W., Scheffers, W. A., van Dijken, J. P., & Pronk, J. T. (2006) · Antonie van Leeuwenhoek · doi:10.1007/s10482-006-9085-7 · Cited by 546 · see citing works
Wastewater treatment in molasses-based alcohol distilleries for COD and color removal: A review
Satyawali, Y., & Balakrishnan, M. (2007) · Journal of Environmental Management · doi:10.1016/j.jenvman.2006.12.024 · Cited by 524 · see citing works
A comprehensive review of signal peptides: Structure, roles, and applications
Owji, H., Nezafat, N., Negahdaripour, M., Hajiebrahimi, A., & Ghasemi, Y. (2018) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2018.06.003 · Cited by 523 · see citing works
Towards an integrated phylogenetic classification of the Tremellomycetes
Liu, X.-Z., Wang, Q.-M., Göker, M., Groenewald, M., Качалкин, А. В., Lumbsch, H. T., Millanes, A. M., Wedin, M., Yurkov, A. M., Boekhout, T., et al. (2015) · Studies in Mycology · doi:10.1016/j.simyco.2015.12.001 · Cited by 501 · see citing works
De novo peptide sequencing by deep learning
Tran, N. H., Zhang, X., Xin, L., Shan, B., & Li, M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705691114 · Cited by 437 · see citing works
Deep learning enables de novo peptide sequencing from data-independent-acquisition mass spectrometry
Tran, N. H., Qiao, R., Xin, L., Chen, X., Liu, C., Zhang, X., Shan, B., Ghodsi, A., & Li, M. (2018) · Nature Methods · doi:10.1038/s41592-018-0260-3 · Cited by 375 · see citing works
Bauer, Š., Vasu, P., Persson, S., Mort, A. J., & Somerville, C. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604632103 · Cited by 351 · see citing works
Cellodextrin Transport in Yeast for Improved Biofuel Production
Galazka, J. M., Tian, C., Beeson, W. T., Martinez, B., Glass, N. L., & Cate, J. H. D. (2010) · Science · doi:10.1126/science.1192838 · Cited by 326 · see citing works
A Brief History of Protein Sorting Prediction
Nielsen, H., Tsirigos, K. D., Brunak, S., & von HEIJNE, G. (2019) · The Protein Journal · doi:10.1007/s10930-019-09838-3 · Cited by 301 · see citing works
Griffiths, M. J., van Hille, R. P., & Harrison, S. T. L. (2010) · Lipids · doi:10.1007/s11745-010-3468-2 · Cited by 277 · see citing works
Watanabe, K., Hata, Y., Kizaki, H., Katsube, Y., & Suzuki, Y. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1018 · Cited by 276 · see citing works
Bisson, L. F., Coons, D. M., Kruckeberg, A. L., & LEWIS, D. A. (1993) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239309078437 · Cited by 272 · see citing works
Wood, I. P., Elliston, A., Ryden, P., Bancroft, I., Roberts, I. N., & Waldron, K. W. (2012) · Biomass and Bioenergy · doi:10.1016/j.biombioe.2012.05.003 · Cited by 260 · see citing works
Protein expression and secretion in the yeast
Nicaud, J., Madzak, C., Vandenbroek, P. J. A., Gysler, C., Duboc, P., Niederberger, P., & Gaillardin, C. M. (2002) · FEMS Yeast Research · doi:10.1016/s1567-1356(02)00082-x · Cited by 250 · see citing works
Switching the mode of metabolism in the yeast Saccharomyces cerevisiae
Otterstedt, K., Larsson, C., Bill, R. M., Ståhlberg, A., Boles, E., Hohmann, S., & Gustafsson, L. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400132 · Cited by 229 · see citing works
Carbohydrate and energy-yielding metabolism in non-conventional yeasts: Figure 1
Flores, C., Rodrı́guez, C., Petit, T., & Gancedo, C. (2000) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2000.tb00553.x · Cited by 227 · see citing works
Biochemical Conversion Processes of Lignocellulosic Biomass to Fuels and Chemicals – A Review
Brethauer, S., & Studer, M. H.-P. (2015) · CHIMIA International Journal for Chemistry · doi:10.2533/chimia.2015.572 · Cited by 226 · see citing works
Defining the physiological role of SRP in protein-targeting efficiency and specificity
Boydston, E. A., Subramanian, K., Nunnari, J. M., & Weissman, J. S. (2018) · Science · doi:10.1126/science.aar3607 · Cited by 216 · see citing works
Simultaneous utilization of glucose and xylose for lipid production by Trichosporon cutaneum
Hu, C., Wu, S., Wang, Q., Jin, G., Shen, H., & Zhao, Z. K. (2011) · Biotechnology for Biofuels · doi:10.1186/1754-6834-4-25 · Cited by 192 · see citing works
Saloheimo, M., & Pakula, T. (2011) · Microbiology · doi:10.1099/mic.0.053132-0 · Cited by 164 · see citing works
The glucose signaling network in yeast
Kim, J., Roy, A., Jouandot, D. J., & Cho, K. H. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.025 · Cited by 161 · see citing works
Complete De Novo Assembly of Monoclonal Antibody Sequences
Tran, N. H., Rahman, M. Z., He, L., Xin, L., Shan, B., & Li, M. (2016) · Scientific Reports · doi:10.1038/srep31730 · Cited by 158 · see citing works
A different vision of dyslexia: Local precedence on global perception
Franceschini, S., Bertoni, S., Gianesini, T., Gori, S., & Facoetti, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-17626-1 · Cited by 139 · see citing works
Chi, Z., Zheng, Y., Ma, J., & Chen, S. (2011) · International Journal of Hydrogen Energy · doi:10.1016/j.ijhydene.2011.04.124 · Cited by 134 · see citing works
Basso, T. O., de Kok, S., Dário, M. G., do Espírito-Santo, J. C. A., Müller, G., Schlölg, P. S., Silva, C. P., Tonso, A., Daran, J.-M. G., Gombert, A. K., et al. (2011) · Metabolic Engineering · doi:10.1016/j.ymben.2011.09.005 · Cited by 132 · see citing works
Biochemical characterization of α-amylase from the yeastCryptococcus flavus
Wanderley, K. J., Torres, F. A. G., de Moraes, L. M. P., & Ulhôa, C. J. (2004) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(03)00955-8 · Cited by 114 · see citing works
Shen, X., Saburi, W., Gai, Z., Kato, K., Ojima‐Kato, T., Yu, J., Komoda, K., Kido, Y., Matsui, H., Mori, H., et al. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s139900471500721x · Cited by 106 · see citing works
Sexual reproduction and dimorphism in the pathogenic basidiomycetes
Morrow, C. A., & Fraser, J. A. (2009) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2008.00475.x · Cited by 103 · see citing works
Prepro-alpha-factor has a cleavable signal sequence.
Waters, M. G., Evans, E. A., & Blobel, G. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68773-3 · Cited by 102 · see citing works
Lignocellulosic biomass as a carbohydrate source for lipid production by Mortierella isabellina
Zeng, J., Zheng, Y., Yu, X., Yu, L., Gao, D., & Chen, S. (2012) · Bioresource Technology · doi:10.1016/j.biortech.2012.10.079 · Cited by 102 · see citing works
An Introduction to Membrane Proteins
Hedin, L. E., Illergård, K., & Elofsson, A. (2011) · Journal of Proteome Research · doi:10.1021/pr200145a · Cited by 102 · see citing works
Vidgren, V., Ruohonen, L., & Londesborough, J. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.12.7846-7857.2005 · Cited by 98 · see citing works
Masri, M. A., Garbe, D., Mehlmer, N., & Brück, T. B. (2019) · Energy & Environmental Science · doi:10.1039/c9ee00210c · Cited by 98 · see citing works
Self-citationZakhartsev, M. V., & Reuß, M. (2018) · FEMS Yeast Research · doi:10.1093/femsyr/foy052 · Cited by 94 · see citing works
Tchakouteu, S. S., Chatzifragkou, A., Kalantzi, O., Koutinas, A., Aggelis, G., & Papanikolaou, S. (2014) · European Journal of Lipid Science and Technology · doi:10.1002/ejlt.201400347 · Cited by 90 · see citing works
Nakkharat, P., & Haltrich, D. (2006) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2005.12.015 · Cited by 88 · see citing works
Novy, V., Nielsen, F., Seiboth, B., & Nidetzky, B. (2019) · Biotechnology for Biofuels · doi:10.1186/s13068-019-1571-z · Cited by 76 · see citing works
Enderlin, C. S., & Ogrydziak, D. M. (1994) · Yeast · doi:10.1002/yea.320100107 · Cited by 74 · see citing works
Jordà, J., Suarez-Mendez, C., Carnicer, M., ten Pierick, A., Heijnen, J. J., van Gulik, W. M., Ferrer, P., Albiol, J., & Wahl, A. (2013) · BMC Systems Biology · doi:10.1186/1752-0509-7-17 · Cited by 74 · see citing works
Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1
Alblova, M., Smidova, A., Dočekal, V., Veselý, J., Heřman, P., Obšilová, V., & Obšil, T. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714491114 · Cited by 73 · see citing works
Awad, D., Bohnen, F., Mehlmer, N., & Brueck, T. (2019) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00054 · Cited by 73 · see citing works
Self-citationHOY1 , a Homeo Gene Required for Hyphal Formation in Yarrowia lipolytica
Guzmán, J. C. T., & Domínguez, Á. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6283 · Cited by 72 · see citing works
Tsukada, T., Igarashi, K., Yoshida, M., & Samejima, M. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0526-z · Cited by 71 · see citing works
Characterization of lignocellulose biomass and model compounds by thermogravimetry
Kök, M. V., & Özgür, E. (2017) · Energy Sources Part A Recovery Utilization and Environmental Effects · doi:10.1080/15567036.2016.1214643 · Cited by 68 · see citing works
Production and Uses of Lactose
Paterson, A. H. J. (2009) · Springer eBooks · doi:10.1007/978-0-387-84865-5_4 · Cited by 65 · see citing works
Comparative assessment of fermentative capacity of different xylose-consuming yeasts
Veras, H. C. T., Parachin, N. S., & de Almeida, J. R. M. (2017) · Microbial Cell Factories · doi:10.1186/s12934-017-0766-x · Cited by 65 · see citing works
Converting lignin derived phenolic aldehydes into microbial lipid by Trichosporon cutaneum
Hu, M.-S., Wang, J., Gao, Q., & Bao, J. (2018) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2018.06.341 · Cited by 58 · see citing works
Standardisation of rapid in‐gel digestion by mass spectrometry
Granvogl, B., Gruber, P., & Eichacker, L. A. (2007) · PROTEOMICS · doi:10.1002/pmic.200600607 · Cited by 54 · see citing works
Role of maltase in the utilization of sucrose by Candida albicans
Williamson, P. R., Huber, M. A., & Bennett, J. E. (1993) · Biochemical Journal · doi:10.1042/bj2910765 · Cited by 54 · see citing works
Younes, S., Bracharz, F., Awad, D., Qoura, F., Mehlmer, N., & Brueck, T. (2020) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-020-02354-0 · Cited by 54 · see citing works
Self-citationWoortman, D. V., Fuchs, T., Striegel, L., Fuchs, M., Weber, N., Brück, T., & Rychlik, M. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00481 · Cited by 53 · see citing works
Self-citationMetabolism of aromatics by Trichosporon oleaginosus while remaining oleaginous
Yaguchi, A., Robinson, A., Mihealsick, E., & Blenner, M. (2017) · Microbial Cell Factories · doi:10.1186/s12934-017-0820-8 · Cited by 52 · see citing works
Burgard, J., Grünwald‐Gruber, C., Altmann, F., Zanghellini, J., Valli, M., Mattanovich, D., & Gasser, B. (2019) · Microbial Biotechnology · doi:10.1111/1751-7915.13499 · Cited by 51 · see citing works
Han, P., Zhou, P., Hu, S., Yang, S., Yan, Q., & Jiang, Z. (2013) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-013-0198-y · Cited by 50 · see citing works
Nicaud, J., Fabre, E., Beckerich, J. M., Fournier, P., & Gaillardin, C. M. (1989) · Journal of Biotechnology · doi:10.1016/0168-1656(89)90048-5 · Cited by 50 · see citing works
Serum-induced hypha formation in the dimorphic yeast Yarrowia lipolytica
Kim, J., Cheon, S. A., Park, S., Song, Y., & Kim, J. (2000) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2000.tb09254.x · Cited by 49 · see citing works
Masri, M. A., Jurkowski, W., Shaigani, P., Haack, M., Mehlmer, N., & Brück, T. (2018) · Applied Energy · doi:10.1016/j.apenergy.2018.04.089 · Cited by 46 · see citing works
Self-citationSatoh, T., Toshimori, T., Yan, G., Yamaguchi, T., & Kato, K. (2016) · Scientific Reports · doi:10.1038/srep20575 · Cited by 45 · see citing works
Maltose Production Using Starch from Cassava Bagasse Catalyzed by Cross-Linked β-Amylase Aggregates
Silva, R. A., Mafra, A. C. O., Rojas, M. J., Kopp, W., Giordano, R. C., Fernández‐Lafuente, R., & Tardioli, P. W. (2018) · Catalysts · doi:10.3390/catal8040170 · Cited by 44 · see citing works
Liang, Y., Jarosz, K., Wardlow, A., Zhang, J., & Cui, Y. (2014) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-014-1007-y · Cited by 43 · see citing works
Cutfield, J. F., Sullivan, P. A., & Cutfield, S. M. (2000) · Protein Engineering Design and Selection · doi:10.1093/protein/13.10.735 · Cited by 41 · see citing works
Masri, M. A., Younes, S., Haack, M., Qoura, F., Mehlmer, N., & Brück, T. (2018) · Energy Technology · doi:10.1002/ente.201700604 · Cited by 41 · see citing works
Self-citationPark, Y. K., Vandermies, M., Soudier, P., Telek, S., Thomas, S., Nicaud, J., & Fickers, P. (2019) · Microbial Cell Factories · doi:10.1186/s12934-019-1218-6 · Cited by 41 · see citing works
Modes of lactose uptake in the yeast species Kluyveromyces marxianus
Carvalho‐Silva, M., & Spencer‐Martins, I. (1990) · Antonie van Leeuwenhoek · doi:10.1007/bf00403158 · Cited by 40 · see citing works
Structural and mutagenetic analyses of a 1,3–1,4-β-glucanase from Paecilomyces thermophila
Cheng, Y., Huang, C., Chen, C., Huang, T.-Y., Ko, T., Huang, J., Wu, T., Liu, J., & Guo, R. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.11.005 · Cited by 36 · see citing works
Structural features of cold-adapted dimeric GH2 β-D-galactosidase from Arthrobacter sp. 32cB
Rutkiewicz, M., Bujacz, A., & Bujacz, G. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.06.001 · Cited by 36 · see citing works
Lyhne-Iversen, L., Hobley, T. J., Kaasgaard, S. G., & Harris, P. (2006) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s174430910603096x · Cited by 35 · see citing works
Transport and hydrolysis of disaccharides by Trichosporon cutaneum
Mörtberg, M., & Neujahr, H. Y. (1986) · Journal of Bacteriology · doi:10.1128/jb.168.2.734-738.1986 · Cited by 35 · see citing works
Доценко, Г. С., Semenova, M. V., Sinitsyna, O. A., Hinz, S. W. A., Wery, J., Zorov, I. N., Kondratieva, E. G., & Sinitsyn, A. P. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912110090 · Cited by 30 · see citing works
Optimization of protein isolation by proteomic qualification from Cutaneotrichosporon oleaginosus
Awad, D., & Brueck, T. (2019) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-02254-7 · Cited by 30 · see citing works
Self-citationSimplified high-throughput methods for deep proteome analysis on the timsTOF ProPreprint
Sandow, J. J., Infusini, G., Dagley, L. F., Larsen, R. H., & Webb, A. I. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/657908 · Cited by 27 · see citing works
α-Galactosidases production by Debaryomyces hansenii UFV-1
Viana, P. A., de Rezende, S. T., Passos, F. M. L., Machado, S. G., Maitan‐Alfenas, G. P., Coelho, V. T. D. S., & Guimarães, V. M. (2011) · Food Science and Biotechnology · doi:10.1007/s10068-011-0085-7 · Cited by 24 · see citing works
Kothari, N., Bhagia, S., Zaher, M., Pu, Y., Mittal, A., Yoo, C. G., Himmel, M. E., Ragauskas, A. J., Kumar, R., & Wyman, C. E. (2019) · Green Chemistry · doi:10.1039/c9gc00262f · Cited by 24 · see citing works
Mohapatra, S., Mishra, S. S., Das, S. K., & Thatoi, H. (2018) · International Journal of Energy Research · doi:10.1002/er.4294 · Cited by 16 · see citing works
Flagged first, then by citations
1 of the 93 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The potential of biofuels from first to fourth generation
Cavelius, P., Engelhart-Straub, S., Mehlmer, N., Lercher, J., Awad, D., & Brück, T. (2023) · PLOS Biology · doi:10.1371/journal.pbio.3002063 · Cited by 224 · see citing works
Self-citationPadder, S. A., Khan, R., & Rather, R. A. (2024) · Biomass and Bioenergy · doi:10.1016/j.biombioe.2024.107220 · Cited by 97 · see citing works
Abdullah, M., Ali, Z., Yasin, M. T., Amanat, K., Sarwar, F., Khan, J., & Ahmad, K. (2024) · Environmental Research · doi:10.1016/j.envres.2024.119902 · Cited by 73 · see citing works
Chaudhary, A., Rathour, R. K., Solanki, P., Kakkar, P. M., Pathania, S., Walia, A., Baadhe, R. R., & Bhatia, R. K. (2025) · Renewable Energy · doi:10.1016/j.renene.2025.122714 · Cited by 55 · see citing works
Shaigani, P., Fuchs, T., Graban, P., Prem, S., Haack, M., Masri, M. A., Mehlmer, N., & Brueck, T. (2023) · Microbial Cell Factories · doi:10.1186/s12934-023-02033-1 · Cited by 21 · see citing works
Self-citationRingel, M., Paper, M., Willing, M., Schneider, M., Melcher, F., Stellner, N. I., & Brück, T. (2025) · Microorganisms · doi:10.3390/microorganisms13091988 · Cited by 15 · see citing works
Self-citationEffects of Light on Growth and Metabolism of Rhodococcus erythropolis
Engelhart-Straub, S., Cavelius, P., Hölzl, F. T., Haack, M., Awad, D., Brueck, T., & Mehlmer, N. (2022) · Microorganisms · doi:10.3390/microorganisms10081680 · Cited by 15 · see citing works
Self-citationStellner, N. I., Rerop, Z. S., Mehlmer, N., Masri, M. A., Ringel, M., & Brück, T. (2023) · BMC Biotechnology · doi:10.1186/s12896-023-00812-7 · Cited by 13 · see citing works
Self-citationKeil, L., Mehlmer, N., Cavelius, P., Garbe, D., Haack, M., Ritz, M., Awad, D., & Brück, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015374 · Cited by 12 · see citing works
Self-citationStellner, N. I., Rerop, Z. S., Kyselka, J., Alishevich, K., Beneš, R., Filip, V., Çelik, G., Haack, M., Ringel, M., Masri, M. A., et al. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c01703 · Cited by 13 · see citing works
Self-citationProteomic insights into the physiology and metabolism of oleaginous yeasts and filamentous fungi
Gluth, A., Trejo, J. B., Czaijka, J. J., Deng, S. H., Qian, W., Yang, B., & Zhang, T. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1637123 · Cited by 7 · see citing works
Arnold, N. D., Paper, M., Fuchs, T., Ahmad, N., Jung, P., Lakatos, M., Rodewald, K., Rieger, B., Qoura, F., Kandawa‐Schulz, M., et al. (2024) · MicrobiologyOpen · doi:10.1002/mbo3.70000 · Cited by 6 · see citing works
Self-citationCavelius, P., Engelhart-Straub, S., Biewald, A., Haack, M., Awad, D., Brueck, T., & Mehlmer, N. (2023) · Microorganisms · doi:10.3390/microorganisms11030553 · Cited by 6 · see citing works
Self-citationProteomic and Transcriptomic Analyses to Decipher the Chitinolytic Response of Jeongeupia spp.
Arnold, N. D., Garbe, D., & Brück, T. (2023) · Marine Drugs · doi:10.3390/md21080448 · Cited by 6 · see citing works
Prem, S., Haack, M., Melcher, F., Ringel, M., Garbe, D., & Brück, T. (2023) · Catalysts · doi:10.3390/catal13091236 · Cited by 6 · see citing works
Self-citationOptimizing the Enzymatic Hydrolysis of Microchloropsis salina Biomass for Single-Cell Oil Production
Melcher, F., Schneider, M., Paper, M., Ringel, M., Garbe, D., & Brück, T. (2025) · Biomass · doi:10.3390/biomass5030056 · Cited by 3 · see citing works
Self-citationWu, H., Chen, Q., & Song, J. (2025) · Applied Soil Ecology · doi:10.1016/j.apsoil.2025.106752 · Cited by 1 · see citing works
The oleaginous yeast Cutaneotrichosporon oleaginosum modifies corn stover alkali lignin
Gluth, A., Pu, Y., Hu, D., Chen, X., Johnson, Z., Li, X., Ragauskas, A. J., Qian, W., Zhang, T., & Yang, B. (2026) · Scientific Reports · doi:10.1038/s41598-026-36483-5 · Cited by 1 · see citing works
Shaigani, P., Fuchs, T., Graban, P., Prem, S., Haack, M., Masri, M. A., Mehlmer, N., & Brueck, T. (2024) · Figshare · doi:10.6084/m9.figshare.26567228
Self-citationStellner, N. I., Rerop, Z. S., Mehlmer, N., Masri, M. A., Ringel, M., & Brück, T. (2024) · Figshare · doi:10.6084/m9.figshare.26618074
Self-citationStellner, N. I., Rerop, Z. S., Mehlmer, N., Masri, M. A., Ringel, M., & Brück, T. (2024) · Figshare · doi:10.6084/m9.figshare.26618071
Self-citationShaigani, P., Fuchs, T., Graban, P., Prem, S., Haack, M., Masri, M. A., Mehlmer, N., & Brueck, T. (2024) · Figshare · doi:10.6084/m9.figshare.26567222
Self-citationShaigani, P., Fuchs, T., Graban, P., Prem, S., Haack, M., Masri, M. A., Mehlmer, N., & Brueck, T. (2024) · Figshare · doi:10.6084/m9.figshare.26567225
Self-citationVolatile fatty acids as sustainable feedstocks for tailored microbial lipid production
Willing, M., Schneider, M., Kornilova, M., Weber, M., Awad, D., Melcher, F., Paper, M., Ringel, M., & Garbe, D. (2026) · Biotechnology for Biofuels and Bioproducts · doi:10.1186/s13068-026-02814-x
Self-citationYan, H., Feng, L., Xiang, J., Yi, H., Xie, Z., Amir, A., Zhang, Y., Zhou, P., 赵金标, Tiande, Z., et al. (2026) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-026-11253-x
- Authors
- Fuchs, T., Melcher, F., Rerop, Z. S., Lorenzen, J., Shaigani, P., Awad, D., Haack, M., Prem, S. A., Masri, M., Mehlmer, N., & Brueck, T. B.
- Affiliations
- Technical University of Munich (DE)
- Corresponding author
- Mehlmer, Norbert
- Brueck, Thomas B.
- Venue
- Microbial Cell Factories
- Published
- 2021-10-28
- Volume
- 20
- Issue
- 1
- Pages
- 205-205
- ISSN
- 1475-2859 (ISSN-L)
- PMC
- PMC8555327
- OpenAlex
- W3209450932
- Cited by
- 22
- References
- 93
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 5 · 2023: 8 · 2022: 1
- FWCI
- 1.33
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Microbial Cell Factories (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- mediaTUM (Technical University of Munich) (submittedVersion, other-oa)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion, other-oa)
- Funders
- bundesministerium für bildung und forschung (033RC012B)
- Technische Universität München
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Physical Sciences › Engineering › Biomedical Engineering › Biofuel production and bioconversion
- Keywords
- Cutaneotrichosporon oleaginosus, carbohydrate-active enzymes, carbohydrate metabolism, oligosaccharide hydrolysis, trehalose, cellobiose, lactose, secreted proteins, protein secretion, signal peptide, hydrolytic enzymes, proteomics, microbial lipid production, oleaginous yeast, lignocellulosic hydrolysates, biomass waste
- MeSH terms
- Basidiomycota, Fungal Proteins, Hydrolases, Industrial Microbiology, Proteome, Systems Biology, Carbohydrate Metabolism, Lipid Metabolism
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
