Physiological and molecular aspects of degradation of plant polysaccharides by fungi: What have we learned from Aspergillus?

Biotechnology Journal - Tập 8 Số 8 - Trang 884-894 - 2013
Helena Culleton1, Vincent McKie, Ronald de Vries
1CBS-KNAW Fungal Biodiversity Center, Utrecht, The Netherlands

Tóm tắt

AbstractPlant biomass is the most abundant and usable carbon source for many fungal species. Due to its diverse and complex structure, fungi need to produce a large range of enzymes to degrade these polysaccharides into monomeric components. The fine‐tuned production of such diverse enzyme sets requires control through a set of transcriptional regulators. Aspergillus has a strong potential for degrading biomass, thus this genus has become the most widely studied group of filamentous fungi in this area. This review examines Aspergillus as a successful degrader of plant polysaccharides, and reviews its potential in many industries such as biofuel and as a production host of homologous and heterologous proteins.

Từ khóa


Tài liệu tham khảo

10.1128/MMBR.65.4.497-522.2001

Gruben B. S. Novel transcriptional activators of Aspergillus involved in plant biomass utilization.PhD thesis Utrecht University Utrecht The Netherlands 2012.

10.1126/science.119.3081.80

10.1111/j.1365-313X.1993.tb00007.x

Willats W. G. T., 2001, Modulation of the degree and pattern of methyl‐esterification of pectic homogalacturonan in plant cell walls: Implications for pectin methyl esterase action, matrix properties, and cell adhesion., J. Biol. Chem., 276, 19404, 10.1074/jbc.M011242200

10.1007/s00253-005-1904-7

10.1104/pp.114.1.9

10.1146/annurev-arplant-042809-112315

10.1093/jxb/40.1.1

10.1093/glycob/9.1.93

10.1002/cbdv.200590013

10.1023/A:1010662911148

10.1002/pi.4980180105

10.1128/MMBR.65.4.497-522.2001

10.1016/0008-6215(95)00287-1

10.1016/0008-6215(85)85153-3

10.1016/0008-6215(94)84229-9

Schols H. A. Voragen A. G. J. Complex pectins: Structure elucidation using enzymes in: Visser J. Voragen A. G. J. (Eds.) Progress in Biotechnology Elsevier 1996 pp. 3–19.

10.1016/S0168-9452(97)00130-1

10.1016/S0008-6215(00)00036-7

10.1128/AEM.66.1.36-41.2000

10.1016/S0008-6215(00)00066-5

10.1016/j.fgb.2008.07.020

10.1093/nar/gkn663

10.1016/S0924-2244(97)01063-7

Bedford M. R., 1991, The influence of dietary xylanase on intestinal viscosity and molecular weight distribution of carbohydrates in rye‐fed broiler chicks., Prog. Biotechnol., 7, 361

10.1016/S0032-9592(98)00117-4

Battaglia E. Benoit I. Gruben B. S. de Vries R. P. Plant cell wall derived sugars as substrates for fungi and industry in: Jenkins P. T. (Ed.) The Sugar Industry and Cotton Crops Nova Science Publishers New York 2010 65–94.

Davies R. W., 1994, Heterologous gene expression and protein secretion in Aspergillus., Prog. Ind. Microbiol., 29, 527

10.1007/s00253-002-1171-9

10.1101/gr.112169.110

10.1038/nbt1282

10.1038/nature04341

10.1038/nature04300

10.1038/nature04332

10.1080/13693780600835716

10.1093/dnares/dsr009

10.1080/13693780600835799

10.1016/0168-1656(93)90090-A

10.1007/s004380051129

10.1007/s002940000175

10.1073/pnas.87.6.2077

10.1007/s00253-012-3874-x

10.1007/s002530100772

10.1007/s00253-011-3550-6

10.1046/j.1365-2958.1998.00666.x

de Vries R. P., 1999, Differential expression of three α‐galactosidase genes and a single β‐galactosidase gene from Aspergillus niger., Appl. Environ. Microbiol., 65, 2453, 10.1128/AEM.65.6.2453-2460.1999

Gielkens M. M., 1999, Two cellobiohydrolase‐encoding genes from Aspergillus niger require D‐xylose and the xylanolytic transcriptional activator XlnR for their expression., Appl. Environ. Microbiol., 65, 4340, 10.1128/AEM.65.10.4340-4345.1999

van Peij N., 1998, The transcriptional activator XlnR regulates both xylanolytic and endoglucanase gene expression in Aspergillus niger., Appl. Environ. Microbiol., 64, 3615, 10.1128/AEM.64.10.3615-3619.1998

10.1007/s00253-011-3242-2

10.3114/sim.2011.69.03

de Groot M. J., 2007, Regulation of pentose catabolic pathway genes of Aspergillus niger., Food Technol. Biotechnol., 45, 134

10.1046/j.1365-2958.2000.01843.x

10.1046/j.0014-2956.2001.02482.x

10.1007/s00438-002-0729-7

10.1099/mic.0.26557-0

10.1073/pnas.0709964105

10.3114/sim.2011.69.03

10.1007/s00438-007-0290-5

10.1128/AEM.05290-11

10.1016/j.febslet.2012.09.029

10.1016/S0014-5793(02)03391-4

10.1074/jbc.M801065200

10.1016/j.fgb.2012.09.006

10.1007/BF00376804

10.1111/j.1365-2958.1993.tb01175.x

10.1111/j.1574-6968.1997.tb12557.x

10.1016/S0923-2508(99)80053-9

10.1111/j.1574-6968.2004.tb09579.x

10.1016/j.fgb.2008.03.002

10.1186/1471-2164-9-327

10.1002/(SICI)1097-0290(1999)66:3<164::AID-BIT4>3.0.CO;2-O

10.1128/AEM.07772-11

10.1007/BF00400559

10.1007/s002530050880

10.1016/S0167-7799(02)01933-9

10.1016/j.biotechadv.2004.11.001

10.1002/(SICI)1097-0290(19980205)57:3<321::AID-BIT9>3.0.CO;2-J

10.1002/(SICI)1097-0290(19960205)49:3<266::AID-BIT4>3.0.CO;2-I

10.1007/s002530051321

10.1016/j.biotechadv.2011.09.012

10.1007/BF02172369

10.1111/j.1574-6968.2000.tb09223.x

10.1007/BF00871952

10.1007/s00253-010-2672-6

10.1128/AEM.70.7.3954-3959.2004

10.1016/S0141-0229(98)00041-6

10.1006/fgbi.2000.1188

10.1007/s002530050020

10.1007/s002530050021

10.1016/S1389-1723(00)87662-8

10.1271/bbb.62.1938

10.1016/j.fgb.2012.09.006