Extracellular differential proteome analysis of substrates of different lignin model compounds degraded by Aspergillus fumigatus G-13
Abstract
Aspergillus fumigatus G-13 has the potential to degrade lignocellulose biomass. The purpose of this work is to analyze the extracellular soluble secretory protein of lignocellulose degradation by Aspergillus fumigatus G-13. The research used ferulic acid, sinapic acid and p-coumaric acid as carbon sources. By controlling the culture conditions, adding cellulose co-substrate and auxiliary carbon source, the enzymatic production law of Aspergillus fumigatus G-13 degradation of three lignin model compounds was investigated. The two groups with the greatest difference in enzyme activity expression were screened, and high throughput quantitative proteomics analysis using iTRAQ. iTRAQ analysis showed that a total of 3862 protein spots changed significantly, of which 2103 down-regulated proteins and 1759 up-regulated proteins. The differential proteins involved in the degradation process of lignin model compounds are concentrated in dioxygenase, oxidoreductase, ferulic acid esterase B-2, isoamyl alcohol oxidase, bifunctional catalase peroxidase CAT2, cellulase, cytochrome P450 monooxygenase, flavin-binding monooxygenase, etc. Lignin-related differential abundance proteins were mapped to 128 metabolic pathways. Significantly enriched pathways include metabolic pathways, glyceride metabolism, oxidative phosphorylation, riboflavin metabolism, peroxisomes, riboflavin metabolism. The information presented in this paper is helpful to better understand the lignocellulose degradation mechanisms of A. fumigatus G-13.
Keyword : Aspergillus fumigatus G-13, biodegradation, lignin model compound, iTRAQ, lignin degradation mechanism
This work is licensed under a Creative Commons Attribution 4.0 International License.
References
An, Q., Wu, X. J., Wu, B., & Dai, Y. C. (2015). Effects of carbon and nitrogen sources on lignocellulose decomposition enzyme activities in Flammulina velutipes. Mycosystema, 34, 761–771.
Arulmani, M., Sunili, S. A., & Siu, K. S. (2011). iTRAQ-based quantitative secretome analysis of Phanerochaete chrysosporium. Journal of Proteomics, 75(2), 642–654. https://doi.org/10.1016/j.jprot.2011.09.001
Chi, D. H., Giap, V. D., Anh, L. P. H., & Nghi, D. H. (2017). Feruloyl esterase from Alternaria tenuissima that hydrolyses lignocellulosic material to release hydroxycinnamic acids. Applied Biochemistry and Microbiology, 53(6), 654–660. https://doi.org/10.1134/S0003683817060047
Dawoud, M. E. A., & Abu-Taleb, A. M. (2012). Evaluation of the roles of physical (osmotic, gamma irradiation and/or heat shock) stress factors on enzyme activities and protein accumulation in Pleurotus ostreatus mushroom and its descendent progenies. Journal of Food Agriculture & Environment, 10(2), 22–32.
Grabber, J. H. (2005). How do lignin composition, structure, and cross-linking affect degradability? A review of cell wall model studies. Crop Science, 45(3), 820–831. https://doi.org/10.2135/cropsci2004.0191
Hernández-Ramírez, L. C., Trivellin, G., & Stratakis, C. A. (2018). Cyclic 3′, 5′-adenosine monophosphate (cAMP) signaling in the anterior pituitary gland in health and disease. Molecular and Cellular Endocrinology, 463, 72–86. https://doi.org/10.1016/j.mce.2017.08.006
Himmel, M. E., Ding, S. Y., Johnson, D. K., Adney, W. S., Nimlos, M. R., Brady, J. W., & Foust, T. D. (2007). Biomass recalcitrance: Engineering plants and enzymes for biofuels production. Science, 315(5813), 804–807. https://doi.org/10.1126/science.1137016
Ji, X. L., Zhang, W. T., Gai, Y. P., Lu, B. Y., Yuan, C. Z., Liu, Q. X., & Mu, Z. M. (2012). Patterns of lignocellulose degradation and secretome analysis of Trametes trogii MT. International Biodeterioration and Biodegradation, 75, 55–62. https://doi.org/10.1016/j.ibiod.2012.09.001
Li, K., Xu, F., & Eriksson, K. E. (1999). Comparison of fungal laccases and redox mediators in oxidation of a nonphenolic lignin model compound. Applied and Environmental Microbiology, 65(6), 2654–2660.
Li, W., Sun, Q. D., & Wang, H. X. (2016). A review on research and applications of feruloyl esterase. Journal of Shandong Agricultural University (Natural Science Edition), 47, 628–635. https://doi.org/10.3969/j.issn.1000-2324.2016.04.029
Long, T. M., Tonsing-Carter, E. Y., Chan, W. C., Griend, D. V., Conzen, S. D., & Szmulewitz, R. Z. (2018). Glucocorticoid receptor (GR)-mediated activation of cyclic-adenosine monophosphate (cAMP) pathway gene expression following androgen receptor (AR) antagonism of prostate cancer. Cancer Research, 78(13), 944. https://doi.org/10.1158/1538-7445.AM2018-944
MacDonald, J., Suzuki, H., & Master, E. R. (2012). Expression and regulation of genes encoding lignocellulose-degrading activity in the genus Phanerochaete. Applied Microbiology and Biotechnology, 94, 339–351. https://doi.org/10.1007/s00253-012-3937-z
Pan, M. F., Jiang, M., & Zhou, Z. W. (2011). Latest research advances in biodegradation of lignin. Materials Review, 25, 372–377.
Pinto, C. (2015). Feruloyl esterase: A principal biodegradative enzyme. In Bioprospects of Coastal Eubacteria (pp. 209–224). Springer, Cham. https://doi.org/10.1007/978-3-319-12910-5_12
Ray, A., Saykhedkar, S., Ayoubi-Canaan, P., Hartson, S. D., Prade, R., & Mort, A. J. (2012). Phanerochaete chrysosporium produces a diverse array of extracellular enzymes when grown on sorghum. Applied Microbiology and Biotechnology, 93(5), 2075–2089. https://doi.org/10.1007/s00253-012-3907-5
Robb, C. S., Reisky, L., Bornscheuer, U., & Hehemann, J. (2018). Specificity and mechanism of carbohydrate demethylation by cytochrome P450 monooxygenases. Biochemical Journal, 475(23), 3875–3886. https://doi.org/10.1042/BCJ20180762
Stringer, T. P., Guerrieri, D., Vivar, C., & Praag, H. V. (2015). Plant-derived flavanol (-)epicatechin mitigates anxiety in association with elevated hippocampal monoamine and BDNF levels, but does not influence pattern separation in mice. Translational Psychiatry, 5, e493. https://doi.org/10.1038/tp.2014.135
Taherzadeh, M. J., & Karimi, K. (2008). Pretreatment of lignocellulosic wastes to improve ethanol and biogas production: A Review. International Journal of Monoamine Sciences, 9(9), 1621–1651. https://doi.org/10.3390/ijms9091621
Takuya, K., Shinya, F., Hitoshi, S., & Michio, K. (2009). Occurrence, properties, and applications of feruloyl esterases. Applied Microbiology and Biotechnology, 84(5), 803–810. https://doi.org/10.1007/s00253-009-2148-8
Tao, Y. Z., & Guan, Y. T. (2003). Study of chemical composition of lignin and its application. Journal of Cellulose Science and Technology, 11, 42–50. http://en.cnki.com.cn/Article_en/CJFDTOTAL-XWSK200301008.htm
Valdes, J., Pedroso, I., Quatrini, R., Dodson, R. J., Tettelin, H., Blake, R., Eisen, J. A., & Holmes, D. S. (2008). Acidithiobacillus ferrooxidans metabolism: From genome sequence to industrial applications. BMC Genomics, 9, 597. https://doi.org/10.1186/1471-2164-9-597
Wang, S. Y., Jiang, S. C., Wang, K. Y., Wang, Y., & Zhang, M. P. (2014). Research process of cytochrome P450 in plant. Jilin Vegetables, 4, 41–45. http://en.cnki.com.cn/Article_en/CJFD-Total-JLSS201404031.htm
Wilkins, M. R., Sanchez, J. C., Gooley, A. A., Apple, R. D., Humphery-Smith, I., Hochstrasser, D. F., & Williams, K. L. (1996). Progress with proteome projects why all proteins expressed by a genome should be identified and how to do it. Biotechnology and Genetic Engineering Review, 13(1), 19–50. https://doi.org/10.1080/02648725.1996.10647923
Yang, H. J., Yue, Q., Cao, Y. C., Zhang, D. F., & Wang, J. Q. (2009). Effects of crude feruloyl and acetyl esterase solutions of Neocallimastix sp. YQ1 and Anaeromyces sp. YQ3 isolated from Holstein steers on hydrolysis of Chinese wildrye grass hay, wheat bran, maizebran, wheat straw and corn stalks. Animal Feed Science and Technology, 154(3–4), 218–227. https://doi.org/10.1016/j.anifeedsci.2009.09.006
Yu, H. Y., Zeng, G. M., Hu, T. J., & Chen, Y. N. (2003). Advance in biodegradation of lignin by fungus and expectation of research in aerobic compost. Journal of Chinese Biotechnology, 23(10), 57–61.
Zhang, Y., Morar, M., & Ealick, S. E. (2008). Structural biology of the purine biosynthetic pathway. Cellular and Molecular Life Science, 65(23), 3699–3724. https://doi.org/10.1007/s00018-008-8295-8