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Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase
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Insights into the reaction mechanism of glycosyl hydrolase family 49. Site-directed mutagenesis and substrate preference of isopullulanase

Akeboshi, Hiromi ; Tonozuka, Takashi ; Furukawa, Takaaki ; Ichikawa, Kazuhiro ; Aoki, Hiroyoshi ; Shimonishi, Akiko ; Nishikawa, Atsushi ; Sakano, Yoshiyuki

European journal of biochemistry, 2004-11, Vol.271 (22), p.4420-4427 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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2
A Low-Volume, Parallel Copper-Bicinchoninic Acid (BCA) Assay for Glycoside Hydrolases
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A Low-Volume, Parallel Copper-Bicinchoninic Acid (BCA) Assay for Glycoside Hydrolases

Arnal, Gregory ; Attia, Mohamed A. ; Asohan, Jathavan ; Brumer, Harry

Methods in molecular biology (Clifton, N.J.), 2017, Vol.1588, p.3-14

New York, NY: Springer New York

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3
A Low-Volume, Parallel Copper-Bicinchoninic Acid (BCA) Assay for Glycoside Hydrolases
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A Low-Volume, Parallel Copper-Bicinchoninic Acid (BCA) Assay for Glycoside Hydrolases

Arnal, Gregory ; Attia, Mohamed A. ; Asohan, Jathavan ; Lei, Zhenhuan ; Golisch, Benedikt ; Brumer, Harry

Carbohydrate-Protein Interactions, 2023, Vol.2657, p.3-14

New York, NY: Springer US

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4
Glycoside hydrolases as components of putative carbohydrate biosensor proteins in Clostridium thermocellum
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Glycoside hydrolases as components of putative carbohydrate biosensor proteins in Clostridium thermocellum

Bahari, Liat ; Gilad, Yuval ; Borovok, Ilya ; Kahel-Raifer, Hamutal ; Dassa, Bareket ; Nataf, Yakir ; Shoham, Yuval ; Lamed, Raphael ; Bayer, Edward A

Journal of industrial microbiology & biotechnology, 2011-07, Vol.38 (7), p.825-832 [Periódico revisado por pares]

Berlin/Heidelberg: Springer-Verlag

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5
Microbial Endoxylanases: Effective Weapons to Breach the Plant Cell-Wall Barrier or, Rather, Triggers of Plant Defense Systems
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Microbial Endoxylanases: Effective Weapons to Breach the Plant Cell-Wall Barrier or, Rather, Triggers of Plant Defense Systems

Beliën, T ; Campenhout, S. van ; Robben, J ; Volckaert, G

Molecular plant-microbe interactions, 2006-10, Vol.19 (10), p.1072-1081 [Periódico revisado por pares]

St Paul, MN: APS Press

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6
Cell-surface display of designer cellulosomes by Lactobacillus plantarum
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Cell-surface display of designer cellulosomes by Lactobacillus plantarum

Ben-David, Yonit ; Morais, Sarah ; Stern, Johanna ; Mizrahi, Itzhak ; Bayer, Edward A

Methods in enzymology, 2019, Vol.617, p.241-263 [Periódico revisado por pares]

United States

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7
A highly glucose-tolerant GH1 β-glucosidase with greater conversion rate of soybean isoflavones in monogastric animals
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A highly glucose-tolerant GH1 β-glucosidase with greater conversion rate of soybean isoflavones in monogastric animals

Cao, Huifang ; Zhang, Yueqi ; Shi, Pengjun ; Ma, Rui ; Yang, Hong ; Xia, Wei ; Cui, Ying ; Luo, Huiying ; Bai, Yingguo ; Yao, Bin

Journal of industrial microbiology & biotechnology, 2018-06, Vol.45 (6), p.369-378 [Periódico revisado por pares]

Cham: Springer International Publishing

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8
Novel modular enzymes encoded by a cellulase gene cluster in Cellvibrio mixtus
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Novel modular enzymes encoded by a cellulase gene cluster in Cellvibrio mixtus

CENTENO, Maria S. J ; GOYAL, Arun ; PRATES, José A. M ; FERREIRA, Luis M. A ; GILBERT, Harry J ; FONTES, Carlos M. G. A

FEMS microbiology letters, 2006-12, Vol.265 (1), p.26-34 [Periódico revisado por pares]

Oxford: Blackwell

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9
Novel modular enzymes encoded by a cellulase gene cluster in Cellvibrio mixtus
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Novel modular enzymes encoded by a cellulase gene cluster in Cellvibrio mixtus

Centeno, Maria S.J ; Goyal, Arun ; Prates, José A.M ; Ferreira, Luís M.A ; Gilbert, Harry J ; Fontes, Carlos M.G.A

FEMS microbiology letters, 2006-12, Vol.265 (1), p.26-34 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

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10
A unique combination of glycoside hydrolases in Streptococcus suis specifically and sequentially acts on host-derived αGal-epitope glycans
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A unique combination of glycoside hydrolases in Streptococcus suis specifically and sequentially acts on host-derived αGal-epitope glycans

Chen, Ping ; Liu, Ran ; Huang, Mengmeng ; Zhu, Jinlu ; Wei, Dong ; Castellino, Francis J. ; Dang, Guanghui ; Xie, Fang ; Li, Gang ; Cui, Ziyin ; Liu, Siguo ; Zhang, Yueling

The Journal of biological chemistry, 2020-07, Vol.295 (31), p.10638-10652 [Periódico revisado por pares]

United States: Elsevier Inc

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