References
-
Oh J, Lee J, Baek S, Jo Y, Kim H. 2018. Characterization of three extracellular
${\beta}$ -glucosidases produced by a fungal isolate Aspergillus sp. YDJ14 and their hydrolyzing activity for a flavone glycoside. J. Microbiol. Biotechnol. 28: 757-764. https://doi.org/10.4014/jmb.1802.02051 -
Fliegmann J, Mithofer A, Wanner G, Ebel J. 2004. An ancient enzyme domain hidden in the putative
${\beta}$ -glucan elicitor receptor of soybean may play an active part in the perception of pathogen-associated molecular patterns during broad host resistance. J. Biol. Chem. 279: 1132-1140. https://doi.org/10.1074/jbc.M308552200 - Harris PV, Welner D, McFarland K, Re E, Navarro Poulsen J-C, Brown K, et al. 2010. Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family. Biochemistry. 49: 3305-3316. https://doi.org/10.1021/bi100009p
- Allgaier M, Reddy A, Park JI, Ivanova N, D'haeseleer P, Lowry S, et al. 2010. Targeted discovery of glycoside hydrolases from a switchgrass-adapted compost community. PLos One. 5: e8812. https://doi.org/10.1371/journal.pone.0008812
-
Turner C, Turner P, Jacobson G, Almgren K, Waldeback M, Sjoberg P, et al. 2006. Subcritical water extraction and
${\beta}$ -glucosidase-catalyzed hydrolysis of quercetin glycosides in onion waste. Green Chem. 8: 949-959. https://doi.org/10.1039/B608011A - Maitan-Alfenas GP, Visser EM, Guimaraes VM. 2015. Enzymatic hydrolysis of lignocellulosic biomass: converting food waste in valuable products. Curr. Opin. Food Sci. 1: 44-49. https://doi.org/10.1016/j.cofs.2014.10.001
- Amraini SZ, Ariyani LP, Hermansyah H, Setyahadi S, Rahman SF, Park D-H, et al. 2017. Production and characterization of cellulase from E. coli EgRK2 recombinant based oil palm empty fruit bunch. Biotechnol. Bioprocess Eng. 22: 287-295. https://doi.org/10.1007/s12257-017-0034-2
- Taylor LE, Dai Z, Decker SR, Brunecky R, Adney WS, Ding S-Y, et al. 2008. Heterologous expression of glycosyl hydrolases in planta: a new departure for biofuels. Trends Biotechnol. 26: 413-424. https://doi.org/10.1016/j.tibtech.2008.05.002
- Ito S, Kobayashi T, Ara K, Ozaki K, Kawai S, Hatada Y. 1998. Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures. Extremophiles 2: 185-190. https://doi.org/10.1007/s007920050059
- Cherry JR, Fidantsef AL. 2003. Directed evolution of industrial enzymes: an update. Curr. Opin. Biotechnol. 14: 438-443. https://doi.org/10.1016/S0958-1669(03)00099-5
- Dodd D, Cann IK. 2009. Enzymatic deconstruction of xylan for biofuel production. Glob Change Biol. Bioenergy. 1: 2-17. https://doi.org/10.1111/j.1757-1707.2009.01004.x
- Goddard JP, Reymond JL. 2004. Enzyme assays for high-throughput screening. Curr Opin. Biotechnol. 15: 314-322. https://doi.org/10.1016/j.copbio.2004.06.008
- Reymond JL, Fluxa VS, Maillard N. 2009. Enzyme assays. Chem. Commun. (Camb). 1: 34-46.
- Goddard JP, Reymond JL. 2004. Recent advances in enzyme assays. Trends Biotechnol. 22: 363-370. https://doi.org/10.1016/j.tibtech.2004.04.005
- Xia W, Rininsland F, Wittenburg SK, Shi X, Achyuthan KE, McBranch DW, et al. 2004. Applications of fluorescent polymer superquenching to high throughput screening assays for protein kinases. Assay Drug Dev. Technol. 2: 183-192. https://doi.org/10.1089/154065804323056521
- Beisson F, Ferte N, Nari J, Noat G, Arondel V, Verger R. 1999. Use of naturally fluorescent triacylglycerols from Parinari glaberrimum to detect low lipase activities from Arabidopsis thaliana seedlings. J. Lipid Res. 40: 2313-2321. https://doi.org/10.1016/S0022-2275(20)32106-4
- Wahler D, Reymond J-L. 2001. High-throughput screening for biocatalysts. Curr. Opin Biotechnol. 12: 535-544. https://doi.org/10.1016/S0958-1669(01)00260-9
- Wahler D, Reymond J-L. 2001. Novel methods for biocatalyst screening. Curr. Opin. Chem. Biol. 5: 152-158. https://doi.org/10.1016/S1367-5931(00)00184-8
- de Rond T, Danielewicz M, Northen T. 2015. High throughput screening of enzyme activity with mass spectrometry imaging. Curr. Opin. Biotechnol. 31: 1-9. https://doi.org/10.1016/j.copbio.2014.07.008
- Pi N, Armstrong JI, Bertozzi CR, Leary JA. 2002. Kinetic analysis of NodST sulfotransferase using an electrospray ionization mass spectrometry assay. Biochemistry. 41: 13283-13288. https://doi.org/10.1021/bi020457g
- Yu Y, Mizanur RM, Pohl NL. 2008. Glycosidase activity profiling for bacterial identification by a chemical proteomics approach. Biocatal. Biotransformation 26: 25-31. https://doi.org/10.1080/10242420701791151
- Greis KD. 2007. Mass spectrometry for enzyme assays and inhibitor screening: an emerging application in pharmaceutical research. Mass Spectrom. Rev. 26: 324-339. https://doi.org/10.1002/mas.20127
- Kiran GS, Lipton AN, Kennedy J, Dobson AD, Selvin J. 2014. A halotolerant thermostable lipase from the marine bacterium Oceanobacillus sp. PUMB02 with an ability to disrupt bacterial biofilms. Bioengineered 5: 305-318. https://doi.org/10.4161/bioe.29898
- Mirande C, Canard I, Blanche SBC, Charrier J-P, Van Belkum A, Welker M, et al. 2015. Rapid detection of carbapenemase activity: benefits and weaknesses of MALDI-TOF MS. Eur. J. Clin. Microbiol. Infect. Dis. 34: 2225-2234. https://doi.org/10.1007/s10096-015-2473-z
- Weiskopf AS, Vouros P, Harvey DJ. 1997. Characterization of oligosaccharide composition and structure by quadrupole ion trap mass spectrometry. Rapid Commun Mass Spectrom. 11: 1493-1504. https://doi.org/10.1002/(SICI)1097-0231(199709)11:14<1493::AID-RCM40>3.0.CO;2-1
-
Cocuron J-C, Lerouxel O, Drakakaki G, Alonso AP, Liepman AH, Keegstra K, et al. 2007. A gene from the cellulose synthase-like C family encodes a
${\beta}$ -1,4 glucan synthase. Proc. Natl. Acad. Sci. USA 104: 8550-8555. https://doi.org/10.1073/pnas.0703133104 - Creaser CS, Reynolds JC, Harvey DJ. 2002. Structural analysis of oligosaccharides by atmospheric pressure matrix-assisted laser desorption/ionisation quadrupole ion trap mass spectrometry. Rapid Commun. Mass Spectrom. 16: 176-184. https://doi.org/10.1002/rcm.563
- Lopez-Garcia M, Garcia MSD, Vilarino JML, Rodriguez MVG. 2016. MALDI-TOF to compare polysaccharide profiles from commercial health supplements of different mushroom species. Food Chem. 199: 597-604. https://doi.org/10.1016/j.foodchem.2015.12.016
- Bungert D, Bastian S, Heckmann-Pohl DM, Giffhorn F, Heinzle E, Tholey A. 2004. Screening of sugar converting enzymes using quantitative MALDI-ToF mass spectrometry. Biotechnol. Lett. 26: 1025-1030. https://doi.org/10.1023/B:BILE.0000032965.18721.62
-
Jiang G, Vasanthan T. 2000. MALDI-MS and HPLC quantification of oligosaccharides of lichenase-hydrolyzed water-soluble
${\beta}$ -glucan from ten barley varieties. J. Agric. Food Chem. 48: 3305-3310. https://doi.org/10.1021/jf0001278 - de Carvalho CC. 2011. Enzymatic and whole cell catalysis: finding new strategies for old processes. Biotechnol. Adv. 29: 75-83. https://doi.org/10.1016/j.biotechadv.2010.09.001
- Adrio JL, Demain AL. 2014. Microbial enzymes: tools for biotechnological processes. Biomolecules. 4: 117-139. https://doi.org/10.3390/biom4010117
-
Li Y, Ku S, Park MS, Li Z, Ji GE. 2017. Acceleration of aglycone isoflavone and
${\gamma}$ -aminobutyric acid production from doenjang using whole-cell biocatalysis accompanied by protease treatment. J. Microbiol. Biotechnol. 27: 1952-1960. https://doi.org/10.4014/jmb.1705.05052 - Yang M, Galizzi A, Henner D. 1983. Nucleotide sequence of the amylase gene from Bacillus subtilis. Nucl. Acids Res. 11: 237-250. https://doi.org/10.1093/nar/11.2.237
- Hatfield RD, Nevins DJ. 1987. Hydrolytic activity and substrate specificity of an endoglucanase from Zea mays seedling cell walls. Plant Physiol. 83: 203-207. https://doi.org/10.1104/pp.83.1.203
- Ivanova N, Sorokin A, Anderson I, Galleron N, Candelon B, Kapatral V, et al. 2003. Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis. Nature 423: 87-91. https://doi.org/10.1038/nature01582
- Perna NT, Plunkett III G, Burland V, Mau B, Glasner JD, Rose DJ, et al. 2001. Genome sequence of enterohaemorrhagic Escherichia coli O157: H7. Nature 409: 529-533. https://doi.org/10.1038/35054089
- Blattner FR, Plunkett G, Bloch CA, Perna NT, Burland V, Riley M, et al. 1997. The complete genome sequence of Escherichia coli K-12. Science 277: 1453-1462. https://doi.org/10.1126/science.277.5331.1453
- Park Y, Yun H. 1999. Cloning of the Escherichia coli endo-1, 4-Dglucanase gene and identification of its product. Mol. Gen. Genet. 261: 236-241. https://doi.org/10.1007/s004380050962
- McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, Courtney L, et al. 2001. Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature 413: 852-856. https://doi.org/10.1038/35101614
- Timme RE, Pettengill JB, Allard MW, Strain E, Barrangou R, Wehnes C, et al. 2013. Phylogenetic diversity of the enteric pathogen Salmonella enterica subsp. enterica inferred from genome-wide reference-free SNP characters. Genome Biol. Evol. 5: 2109-2123. https://doi.org/10.1093/gbe/evt159
- Portmann A-C, Fournier C, Gimonet J, Ngom-Bru C, Barretto C, Baert L. 2018. A validation approach of an end-to-end whole genome sequencing workflow for source tracking of Listeria monocytogenes and Salmonella enterica. Front Microbiol. 9: 446-458. https://doi.org/10.3389/fmicb.2018.00446