A β-glucosidase hyper-production Trichoderma reesei mutant reveals a potential role of cel3D in cellulase production View Full Text


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Article Info

DATE

2016-09-01

AUTHORS

Chengcheng Li, Fengming Lin, Yizhen Li, Wei Wei, Hongyin Wang, Lei Qin, Zhihua Zhou, Bingzhi Li, Fugen Wu, Zhan Chen

ABSTRACT

BackgroundThe conversion of cellulose by cellulase to fermentable sugars for biomass-based products such as cellulosic biofuels, biobased fine chemicals and medicines is an environment-friendly and sustainable process, making wastes profitable and bringing economic benefits. Trichoderma reesei is the well-known major workhorse for cellulase production in industry, but the low β-glucosidase activity in T. reesei cellulase leads to inefficiency in biomass degradation and limits its industrial application. Thus, there are ongoing interests in research to develop methods to overcome this insufficiency. Moreover, although β-glucosidases have been demonstrated to influence cellulase production and participate in the regulation of cellulase production, the underlying mechanism remains unclear.ResultsThe T. reesei recombinant strain TRB1 was constructed from T. reesei RUT-C30 by the T-DNA-based mutagenesis. Compared to RUT-C30, TRB1 displays a significant enhancement of extracellular β-glucosidase (BGL1) activity with 17-fold increase, a moderate increase of both the endoglucanase (EG) activity and the exoglucanase (CBH) activity, a minor improvement of the total filter paper activity, and a faster cellulase induction. This superiority of TRB1 over RUT-C30 is independent on carbon sources and improves the saccharification ability of TRB1 cellulase on pretreated corn stover. Furthermore, TRB1 shows better resistance to carbon catabolite repression than RUT-C30. Secretome characterization of TRB1 shows that the amount of CBH, EG and BGL in the supernatant of T. reesei TRB1 was indeed increased along with the enhanced activities of these three enzymes. Surprisingly, qRT-PCR and gene cloning showed that in TRB1 β-glucosidase cel3D was mutated through the random insertion by AMT and was not expressed.ConclusionsThe T. reesei recombinant strain TRB1 constructed in this study is more desirable for industrial application than the parental strain RUT-C30, showing extracellular β-glucosidase hyper production, high cellulase production within a shorter time and a better resistance to carbon catabolite repression. Disruption of β-glucosidase cel3D in TRB1 was identified, which might contribute to the superiority of TRB1 over RUT-C30 and might play a role in the cellulase production. These results laid a foundation for future investigations to further improve cellulase enzymatic efficiency and reduce cost for T. reesei cellulase production. More... »

PAGES

151

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/s12934-016-0550-3

DOI

http://dx.doi.org/10.1186/s12934-016-0550-3

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037842085

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27585813


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26 schema:description BackgroundThe conversion of cellulose by cellulase to fermentable sugars for biomass-based products such as cellulosic biofuels, biobased fine chemicals and medicines is an environment-friendly and sustainable process, making wastes profitable and bringing economic benefits. Trichoderma reesei is the well-known major workhorse for cellulase production in industry, but the low β-glucosidase activity in T. reesei cellulase leads to inefficiency in biomass degradation and limits its industrial application. Thus, there are ongoing interests in research to develop methods to overcome this insufficiency. Moreover, although β-glucosidases have been demonstrated to influence cellulase production and participate in the regulation of cellulase production, the underlying mechanism remains unclear.ResultsThe T. reesei recombinant strain TRB1 was constructed from T. reesei RUT-C30 by the T-DNA-based mutagenesis. Compared to RUT-C30, TRB1 displays a significant enhancement of extracellular β-glucosidase (BGL1) activity with 17-fold increase, a moderate increase of both the endoglucanase (EG) activity and the exoglucanase (CBH) activity, a minor improvement of the total filter paper activity, and a faster cellulase induction. This superiority of TRB1 over RUT-C30 is independent on carbon sources and improves the saccharification ability of TRB1 cellulase on pretreated corn stover. Furthermore, TRB1 shows better resistance to carbon catabolite repression than RUT-C30. Secretome characterization of TRB1 shows that the amount of CBH, EG and BGL in the supernatant of T. reesei TRB1 was indeed increased along with the enhanced activities of these three enzymes. Surprisingly, qRT-PCR and gene cloning showed that in TRB1 β-glucosidase cel3D was mutated through the random insertion by AMT and was not expressed.ConclusionsThe T. reesei recombinant strain TRB1 constructed in this study is more desirable for industrial application than the parental strain RUT-C30, showing extracellular β-glucosidase hyper production, high cellulase production within a shorter time and a better resistance to carbon catabolite repression. Disruption of β-glucosidase cel3D in TRB1 was identified, which might contribute to the superiority of TRB1 over RUT-C30 and might play a role in the cellulase production. These results laid a foundation for future investigations to further improve cellulase enzymatic efficiency and reduce cost for T. reesei cellulase production.
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32 schema:keywords AMT
33 BGL
34 CBH
35 Rut-C30
36 TRB1
37 Trichoderma reesei
38 Trichoderma reesei mutants
39 ability
40 activity
41 amount
42 applications
43 benefits
44 biofuels
45 biomass degradation
46 biomass-based products
47 carbon catabolite repression
48 carbon source
49 catabolite repression
50 cellulase
51 cellulase induction
52 cellulase production
53 cellulose
54 cellulosic biofuels
55 characterization
56 chemicals
57 cloning
58 conversion
59 conversion of cellulose
60 corn
61 cost
62 degradation
63 disruption
64 economic benefits
65 efficiency
66 endoglucanase activity
67 enhanced activity
68 enhancement
69 enzymatic efficiency
70 enzyme
71 exoglucanase activity
72 extracellular β-glucosidase activity
73 fermentable sugars
74 filter paper activity
75 fine chemicals
76 foundation
77 future investigations
78 gene cloning
79 good resistance
80 highest cellulase production
81 hyper production
82 improvement
83 increase
84 induction
85 industrial applications
86 industry
87 inefficiency
88 insertion
89 insufficiency
90 interest
91 investigation
92 low β-glucosidase activity
93 major workhorse
94 mechanism
95 medicine
96 method
97 minor improvements
98 moderate increase
99 mutagenesis
100 mutants
101 ongoing interest
102 paper activity
103 parental strain RUT C30
104 potential role
105 process
106 production
107 products
108 qRT-PCR
109 random insertion
110 reesei
111 reesei Rut-C30
112 reesei cellulase
113 reesei mutants
114 regulation
115 repression
116 research
117 resistance
118 results
119 role
120 saccharification ability
121 secretome characterization
122 short time
123 significant enhancement
124 source
125 strain Rut-C30
126 study
127 sugars
128 superiority
129 supernatant
130 sustainable process
131 time
132 underlying mechanism
133 waste
134 workhorse
135 β-glucosidase activity
136 β-glucosidases
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