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Biochemical characterization of a novel glucose-tolerant GH3 [beta]-glucosidase from Leifsonia sp. ZF2019
Biochemical characterization of a novel glucose-tolerant GH3 [beta]-glucosidase from Leifsonia sp. ZF2019
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Biochemical characterization of a novel glucose-tolerant GH3 [beta]-glucosidase from Leifsonia sp. ZF2019

He, Yi ; Wang, Chenxi ; Jiao, Ronghu ; Ni, Qinxue ; Wang, Yan ; Gao, Qianxin ; Zhang, Youzuo ; Xu, Guangzhi

Applied microbiology and biotechnology, 2022-08, Vol.106 (13-16), p.5063 [Periódico revisado por pares]

Springer

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2
Streptomyces: implications and interactions in plant growth promotion
Streptomyces: implications and interactions in plant growth promotion
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Streptomyces: implications and interactions in plant growth promotion

Olanrewaju, Oluwaseyi Samuel ; Babalola, Olubukola Oluranti

Applied microbiology and biotechnology, 2019-02, Vol.103 (3), p.1179-1188 [Periódico revisado por pares]

Berlin/Heidelberg: Springer Berlin Heidelberg

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3
Overexpression of nicotinamide mononucleotide adenylyltransferase increases the growth rate, Ca.sup.2+ concentration and cellulase production in Ganoderma lucidum
Overexpression of nicotinamide mononucleotide adenylyltransferase increases the growth rate, Ca.sup.2+ concentration and cellulase production in Ganoderma lucidum
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Overexpression of nicotinamide mononucleotide adenylyltransferase increases the growth rate, Ca.sup.2+ concentration and cellulase production in Ganoderma lucidum

Wang, Shengli ; Han, Jing ; Xia, Jiale ; Hu, Yanru ; Shi, Liang ; Ren, Ang ; Zhu, Jing

Applied microbiology and biotechnology, 2020-08, Vol.104 (16), p.7079 [Periódico revisado por pares]

Springer

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4
A novel multifunctional GH9 enzyme from Paenibacillus curdlanolyticus B-6 exhibiting endo/exo functions of cellulase, mannanase and xylanase activities
A novel multifunctional GH9 enzyme from Paenibacillus curdlanolyticus B-6 exhibiting endo/exo functions of cellulase, mannanase and xylanase activities
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A novel multifunctional GH9 enzyme from Paenibacillus curdlanolyticus B-6 exhibiting endo/exo functions of cellulase, mannanase and xylanase activities

Phakeenuya, Vanarat ; Ratanakhanokchai, Khanok ; Kosugi, Akihiko ; Tachaapaikoon, Chakrit

Applied microbiology and biotechnology, 2020-03, Vol.104 (5), p.2079-2096 [Periódico revisado por pares]

Berlin/Heidelberg: Springer Berlin Heidelberg

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5
Safety of the fungal workhorses of industrial biotechnology: update on the mycotoxin and secondary metabolite potential of Aspergillus niger, Aspergillus oryzae, and Trichoderma reesei
Safety of the fungal workhorses of industrial biotechnology: update on the mycotoxin and secondary metabolite potential of Aspergillus niger, Aspergillus oryzae, and Trichoderma reesei
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Safety of the fungal workhorses of industrial biotechnology: update on the mycotoxin and secondary metabolite potential of Aspergillus niger, Aspergillus oryzae, and Trichoderma reesei

Frisvad, Jens C. ; Møller, Lars L. H. ; Larsen, Thomas O. ; Kumar, Ravi ; Arnau, José

Applied microbiology and biotechnology, 2018-11, Vol.102 (22), p.9481-9515 [Periódico revisado por pares]

Berlin/Heidelberg: Springer Berlin Heidelberg

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6
Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production
Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production
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Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production

Ahmad, Mudassar ; Hirz, Melanie ; Pichler, Harald ; Schwab, Helmut

Applied microbiology and biotechnology, 2014-06, Vol.98 (12), p.5301-5317 [Periódico revisado por pares]

Berlin/Heidelberg: Springer-Verlag

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7
EcXyl43 [beta]-xylosidase: molecular modeling, activity on natural and artificial substrates, and synergism with endoxylanases for lignocellulose deconstruction
EcXyl43 [beta]-xylosidase: molecular modeling, activity on natural and artificial substrates, and synergism with endoxylanases for lignocellulose deconstruction
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EcXyl43 [beta]-xylosidase: molecular modeling, activity on natural and artificial substrates, and synergism with endoxylanases for lignocellulose deconstruction

Ontañon, Ornella M ; Ghio, Silvina ; Marrero Díaz de Villegas, Rubén ; Piccinni, Florencia E ; Talia, Paola M ; Cerutti, María L ; Campos, Eleonora

Applied microbiology and biotechnology, 2018-08, Vol.102 (16), p.6959 [Periódico revisado por pares]

Springer

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8
Capture of carbon dioxide and hydrogen by engineered Escherichia coli: hydrogen-dependent CO.sub.2 reduction to formate
Capture of carbon dioxide and hydrogen by engineered Escherichia coli: hydrogen-dependent CO.sub.2 reduction to formate
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Capture of carbon dioxide and hydrogen by engineered Escherichia coli: hydrogen-dependent CO.sub.2 reduction to formate

Leo, Felix ; Schwarz, Fabian M ; Schuchmann, Kai ; Müller, Volker

Applied microbiology and biotechnology, 2021-08, Vol.105 (14-15), p.5861 [Periódico revisado por pares]

Springer

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9
G protein [gamma] subunit modulates expression of plant-biomass-degrading enzyme genes and mycelial-development-related genes in Penicillium oxalicum
G protein [gamma] subunit modulates expression of plant-biomass-degrading enzyme genes and mycelial-development-related genes in Penicillium oxalicum
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G protein [gamma] subunit modulates expression of plant-biomass-degrading enzyme genes and mycelial-development-related genes in Penicillium oxalicum

Pang, Xiao-Ming ; Tian, Di ; Zhang, Ting ; Liao, Lu-Sheng ; Li, Cheng-Xi ; Luo, Xue-Mei ; Feng, Jia-Xun ; Zhao, Shuai

Applied microbiology and biotechnology, 2021-06, Vol.105 (11), p.4675 [Periódico revisado por pares]

Springer

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10
Cytochromes P450 as promising catalysts for biotechnological application: chances and limitations
Cytochromes P450 as promising catalysts for biotechnological application: chances and limitations
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Cytochromes P450 as promising catalysts for biotechnological application: chances and limitations

Bernhardt, Rita ; Urlacher, Vlada B

Applied microbiology and biotechnology, 2014, Vol.98 (14), p.6185-6203 [Periódico revisado por pares]

Berlin/Heidelberg: Springer-Verlag

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