2018
DOI: 10.1016/j.enzmictec.2017.08.007
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Exploring Trichoderma and Aspergillus secretomes: Proteomics approaches for the identification of enzymes of biotechnological interest

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Cited by 52 publications
(24 citation statements)
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“…Notably, among enzymes related to saccharification and liquefaction in J3, glucoamylases were clearly active with high expression levels, indicating their collaborative roles along with high temperature in degrading starches, which would be spontaneously decomposed under high temperature, as well as suggesting a feasible way to mine thermostable glucoamylases from J3. The majority of enzymes related to saccharification and liquefaction in J3 were highly expressed by fungal species of R. emersonii , A. oryzae , A. fumigatus , and C. immitis , some of which have been found to secrete numerous carbohydrate-active enzymes and show high capacities toward degrading polymers, such as Aspergillus (Culleton et al, 2013; de Vries et al, 2017; Cologna et al, 2018) and R. emersonii (Hua et al, 2014; Martínez et al, 2016). In addition, J3 showed considerable potential for converting glucose to pivotal intermediates, such as acetate, ethanol, pyruvate, and acetyl-coA, which might then serve as direct or indirect substrates for JF flavor compounds including ethyl acetate, ethyl butanoate, ethyl propanoate, ethyl 2-hydroxypropanoate, ethyl 2-hydroxyhexanoate, acetic acid, 2-acetylpyridine, hexyl acetate, benzyl acetate ethyl, ethyl 3-methylbutanoate, ethyl benzeneacetate, and 3-methylbutyl acetate (Fan et al, 2012; Wang et al, 2014; Xiao et al, 2016; Gao et al, 2017).…”
Section: Discussionmentioning
confidence: 99%
“…Notably, among enzymes related to saccharification and liquefaction in J3, glucoamylases were clearly active with high expression levels, indicating their collaborative roles along with high temperature in degrading starches, which would be spontaneously decomposed under high temperature, as well as suggesting a feasible way to mine thermostable glucoamylases from J3. The majority of enzymes related to saccharification and liquefaction in J3 were highly expressed by fungal species of R. emersonii , A. oryzae , A. fumigatus , and C. immitis , some of which have been found to secrete numerous carbohydrate-active enzymes and show high capacities toward degrading polymers, such as Aspergillus (Culleton et al, 2013; de Vries et al, 2017; Cologna et al, 2018) and R. emersonii (Hua et al, 2014; Martínez et al, 2016). In addition, J3 showed considerable potential for converting glucose to pivotal intermediates, such as acetate, ethanol, pyruvate, and acetyl-coA, which might then serve as direct or indirect substrates for JF flavor compounds including ethyl acetate, ethyl butanoate, ethyl propanoate, ethyl 2-hydroxypropanoate, ethyl 2-hydroxyhexanoate, acetic acid, 2-acetylpyridine, hexyl acetate, benzyl acetate ethyl, ethyl 3-methylbutanoate, ethyl benzeneacetate, and 3-methylbutyl acetate (Fan et al, 2012; Wang et al, 2014; Xiao et al, 2016; Gao et al, 2017).…”
Section: Discussionmentioning
confidence: 99%
“…They characterized by specificity, stability and extremely fast labor under moderate temperatures and pressures. So, they are considered safe and eco-friendly (Cologna et al, 2018).…”
Section: Introductionmentioning
confidence: 99%
“…In the last few years, several advances have been achieved in different research fields and contributed to a better understanding of the physiology and key features behind the T. reesei hypercellulolytic capacity. Such advances include the development of new tools for genetic manipulation (Derntl et al, 2015 ; Liu et al, 2015 ), transcriptomic and proteomic studies using lignocellulosic residues (Dos Santos Castro et al, 2014 ; Borin et al, 2015 , 2017 ; Daly et al, 2017 ; Ellilä et al, 2017 ; Cologna et al, 2018 ), the discovery of new transcription factors (TFs) and regulatory elements (Derntl et al, 2016 , 2017 ; Stappler et al, 2017 ; Zheng et al, 2017b ; Benocci et al, 2018 ), promoter characterization (Zheng et al, 2017a ; Kiesenhofer et al, 2018 ) and structural studies of cellulases (Li et al, 2015 ; Bodenheimer and Meilleur, 2016 ; Eibinger et al, 2016 ; Ma et al, 2017 ; Borisova et al, 2018 ).…”
Section: Introductionmentioning
confidence: 99%