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Journal articles on the topic 'Glycosyl hydrolase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Fülöp, László, and Tamás Ponyi. "Classification of glycosyl hydrolases based on structural homology." Journal of Universal Science Online 2, no. 1 (2015): 1–9. http://dx.doi.org/10.17202/juso.2015.2.1.

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Glycosyl hydrolases are a well-known group of enzymes, which hydrolyze the glycosidic bond between carbohydrates, or between a carbohydrate and different molecules. Glycosyl hydrolases play a vital role in the human body, and are widely used in industrial applications. Glycosyl hydrolases classification is based on substrate specificity and amino acid or nucleotide sequence similarity which reflects their evolutionary relationship. Our aim, in this study, was to carry out the classification of glycosyl hydrolases, based solely on structural similarity which was made possible by the several str

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2

Haseltine, Cynthia, Rafael Montalvo-Rodriguez, Audrey Carl, Elisabetta Bini, and Paul Blum. "Extragenic Pleiotropic Mutations That Repress Glycosyl Hydrolase Expression in the Hyperthermophilic Archaeon Sulfolobus solfataricus." Genetics 152, no. 4 (1999): 1353–61. http://dx.doi.org/10.1093/genetics/152.4.1353.

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Abstract The hyperthermophilic archaeon Sulfolobus solfataricus employs a catabolite repression-like regulatory system to control enzymes involved in carbon and energy metabolism. To better understand the basis of this system, spontaneous glycosyl hydrolase mutants were isolated using a genetic screen for mutations, which reduced expression of the lacS gene. The specific activities of three glycosyl hydrolases, including an α-glucosidase (malA), a β-glycosidase (lacS), and the major secreted α-amylase, were measured in the mutant strains using enzyme activity assays, Western blot analysis, and

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3

Chen, Hanchi, Xiao Jin, Linjiang Zhu, et al. "Glycosyl hydrolase catalyzed glycosylation in unconventional media." Applied Microbiology and Biotechnology 104, no. 22 (2020): 9523–34. http://dx.doi.org/10.1007/s00253-020-10924-1.

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4

Jasso-Martínez, Jovana M., Alexander Donath, Dieter Schulten, Alejandro Zaldívar-Riverón, and Manuela Sann. "Midgut transcriptome assessment of the cockroach-hunting wasp Ampulex compressa (Apoidea: Ampulicidae)." PLOS ONE 16, no. 6 (2021): e0252221. http://dx.doi.org/10.1371/journal.pone.0252221.

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The emerald jewel wasp Ampulex compressa (Hymenoptera: Ampulicidae) is a solitary wasp that is widely known for its specialized hunting of cockroaches as larvae provision. Adult wasps mainly feed on pollen and nectar, while their larvae feed on the cockroachs’ body, first as ecto- and later as endoparsitoids. Little is known about the expression of digestive, detoxification and stress-response-related genes in the midgut of A. compressa, or about its transcriptional versatility between life stages. To identify gut-biased genes related to digestion, detoxification, and stress response, we explo

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5

Radford, Alan. "Glycosyl Hydrolase Genes and Enzymes of Neurospora crassa." Fungal Genetics Reports 53, no. 1 (2006): 12–14. http://dx.doi.org/10.4148/1941-4765.1107.

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6

Jones, Richard W. "Plant vascular system-feeding Psyllidae (Hemiptera) and Nematoda genomes encode family 12 glycosyl hydrolases." Canadian Entomologist 151, no. 3 (2019): 291–97. http://dx.doi.org/10.4039/tce.2019.11.

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AbstractInsect-encoded cellulolytic plant cell wall hydrolases have thus far been found mostly from glycosyl hydrolase family 5, 9, 10, and 45. We now report the first evidence for genomic encoding of family 12 glycosyl hydrolases in vascular feeding Psyllidae (Hemiptera) and Nematoda. The genes were identified in three psyllids (Acanthocasuarina muellerianae Taylor, Pachypsylla venusta (Osten-Sacken), and Diaphorina citri Kuwayama) and a root tip feeding dagger nematode (Xiphinema index Thorne and Allen; Dorylaimida: Longidoridae). While the final gene products were highly similar, the genomi

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7

Bharadwaj, Rajiv, Zhiwei Chen, Supratim Datta, et al. "Microfluidic Glycosyl Hydrolase Screening for Biomass-to-Biofuel Conversion." Analytical Chemistry 82, no. 22 (2010): 9513–20. http://dx.doi.org/10.1021/ac102243f.

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8

Pons, Tirso, Osvaldo Olmea, Glay Chinea, et al. "Structural model for family 32 of glycosyl-hydrolase enzymes." Proteins: Structure, Function, and Genetics 33, no. 3 (1998): 383–95. http://dx.doi.org/10.1002/(sici)1097-0134(19981115)33:3<383::aid-prot7>3.0.co;2-r.

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9

Davison, Angus, and Mark Blaxter. "Ancient Origin of Glycosyl Hydrolase Family 9 Cellulase Genes." Molecular Biology and Evolution 22, no. 5 (2005): 1273–84. http://dx.doi.org/10.1093/molbev/msi107.

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10

Guillotin, Assaf, Pistorio, Lafite, Demchenko, and Daniellou. "Hydrolysis of Glycosyl Thioimidates by Glycoside Hydrolase Requires Remote Activation for Efficient Activity." Catalysts 9, no. 10 (2019): 826. http://dx.doi.org/10.3390/catal9100826.

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Chemoenzymatic synthesis of glycosides relies on efficient glycosyl donor substrates able to react rapidly and efficiently, yet with increased stability towards chemical or enzymatic hydrolysis. In this context, glycosyl thioimidates have previously been used as efficient donors, in the case of hydrolysis or thioglycoligation. In both cases, the release of the thioimidoyl aglycone was remotely activated through a protonation driven by a carboxylic residue in the active site of the corresponding enzymes. A recombinant glucosidase (DtGly) from Dictyoglomus themophilum, previously used in biocata

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11

Ahn, Young Ock, Masaharu Mizutani, Hiromichi Saino, and Kanzo Sakata. "Furcatin Hydrolase fromViburnum furcatumBlume Is a Novel Disaccharide-specific Acuminosidase in Glycosyl Hydrolase Family 1." Journal of Biological Chemistry 279, no. 22 (2004): 23405–14. http://dx.doi.org/10.1074/jbc.m311379200.

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12

Koizumi, Hideyo, Kazuhide Totani, Noriyuki Kitamoto, Shota Sato, Tetsuo Ohmachi, and Takashi Yoshida. "Fungal Cellulases of Glycosyl Hydrolase Family 7 Catalyze Lactose Condensation." Journal of Applied Glycoscience 57, no. 4 (2010): 239–43. http://dx.doi.org/10.5458/jag.57.239.

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13

Cheng, Chih-Yu, Chu-Han Chang, Yue-Jin Wu, and Yaw-Kuen Li. "Exploration of Glycosyl Hydrolase Family 75, a Chitosanase fromAspergillus fumigatus." Journal of Biological Chemistry 281, no. 6 (2005): 3137–44. http://dx.doi.org/10.1074/jbc.m512506200.

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14

Aronson, Nathan N., Christopher J. Blanchard, and Jeffry D. Madura. "Homology Modeling of Glycosyl Hydrolase Family 18 Enzymes and Proteins." Journal of Chemical Information and Computer Sciences 37, no. 6 (1997): 999–1005. http://dx.doi.org/10.1021/ci970236v.

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15

Li, Kun-Lung, Keisuke Nakashima, Jun Inoue, and Noriyuki Satoh. "Phylogenetic Analyses of Glycosyl Hydrolase Family 6 Genes in Tunicates: Possible Horizontal Transfer." Genes 11, no. 8 (2020): 937. http://dx.doi.org/10.3390/genes11080937.

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Horizontal gene transfer (HGT) is the movement of genetic material between different species. Although HGT is less frequent in eukaryotes than in bacteria, several instances of HGT have apparently shaped animal evolution. One well-known example is the tunicate cellulose synthase gene, CesA, in which a gene, probably transferred from bacteria, greatly impacted tunicate evolution. A Glycosyl Hydrolase Family 6 (GH6) hydrolase-like domain exists at the C-terminus of tunicate CesA, but not in cellulose synthases of other organisms. The recent discovery of another GH6 hydrolase-like gene (GH6-1) in

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16

Michlmayr, Herbert, Walter Brandes, Reinhard Eder, Christina Schümann, Andrés M. del Hierro та Klaus D. Kulbe. "Characterization of Two Distinct Glycosyl Hydrolase Family 78 α-l-Rhamnosidases from Pediococcus acidilactici". Applied and Environmental Microbiology 77, № 18 (2011): 6524–30. http://dx.doi.org/10.1128/aem.05317-11.

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ABSTRACTα-l-Rhamnosidases play an important role in the hydrolysis of glycosylated aroma compounds (especially terpenes) from wine. Although several authors have demonstrated the enological importance of fungal rhamnosidases, the information on bacterial enzymes in this context is still limited. In order to fill this important gap, two putative rhamnosidase genes (ramandram2) fromPediococcus acidilacticiDSM 20284 were heterologously expressed, and the respective gene products were characterized. In combination with a bacterial β-glucosidase, both enzymes released the monoterpenes linalool andc

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17

Attigani, Ayman, Lifang Sun, Qing Wang, et al. "The crystal structure of the endoglucanase Cel10, a family 8 glycosyl hydrolase fromKlebsiella pneumoniae." Acta Crystallographica Section F Structural Biology Communications 72, no. 12 (2016): 870–76. http://dx.doi.org/10.1107/s2053230x16017891.

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Cellulases are produced by microorganisms that grow on cellulose biomass. Here, a cellulase, Cel10, was identified in a strain ofKlebsiella pneumoniaeisolated from Chinese bamboo rat gut. Analysis of substrate specificity showed that Cel10 is able to hydrolyze amorphous carboxymethyl cellulose (CMC) and crystalline forms of cellulose (Avicel and xylan) but is unable to hydrolyzep-nitrophenol β-D-glucopyranoside (p-NPG), proving that Cel10 is an endoglucanase. A phylogenetic tree analysis indicates that Cel10 belongs to the glycoside hydrolase 8 (GH8) subfamily. In order to further understandin

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18

Kim, Dong-Jin, Jong-Min Baek, Pedro Uribe, Charles Kenerley, and Douglas Cook. "Cloning and characterization of multiple glycosyl hydrolase genes from Trichoderma virens." Current Genetics 40, no. 6 (2002): 374–84. http://dx.doi.org/10.1007/s00294-001-0267-6.

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19

Abdul Manas, Nor Hasmaliana, Rosli Md. Illias, and Nor Muhammad Mahadi. "Strategy in manipulating transglycosylation activity of glycosyl hydrolase for oligosaccharide production." Critical Reviews in Biotechnology 38, no. 2 (2017): 272–93. http://dx.doi.org/10.1080/07388551.2017.1339664.

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20

De Ranter, C., S. Sansen, K. Gebruers, et al. "Detecting the structural determinants of glycosyl hydrolase family 11 xylanase inhibition." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (2005): c197. http://dx.doi.org/10.1107/s0108767305091622.

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21

Vandermarliere, E., S. Sansen, A. Rabijns, and S. V. Strelkov. "A glycosyl hydrolase family 11 xylanase with an extended thumb region." Acta Crystallographica Section A Foundations of Crystallography 62, a1 (2006): s155. http://dx.doi.org/10.1107/s0108767306096905.

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22

Bartosiak-Jentys, Jeremy, Ali H. Hussein, Claire J. Lewis, and David J. Leak. "Modular system for assessment of glycosyl hydrolase secretion in Geobacillus thermoglucosidasius." Microbiology 159, Pt_7 (2013): 1267–75. http://dx.doi.org/10.1099/mic.0.066332-0.

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23

St John, Franz J., Jason C. Hurlbert, John D. Rice, James F. Preston, and Edwin Pozharski. "Ligand Bound Structures of a Glycosyl Hydrolase Family 30 Glucuronoxylan Xylanohydrolase." Journal of Molecular Biology 407, no. 1 (2011): 92–109. http://dx.doi.org/10.1016/j.jmb.2011.01.010.

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24

Costanzo, Stefano, M. D. Ospina-Giraldo, K. L. Deahl, C. J. Baker, and Richard W. Jones. "Gene duplication event in family 12 glycosyl hydrolase from Phytophthora spp." Fungal Genetics and Biology 43, no. 10 (2006): 707–14. http://dx.doi.org/10.1016/j.fgb.2006.04.006.

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25

Seon Park, Jae, James B. Russell, and David B. Wilson. "Characterization of a family 45 glycosyl hydrolase from Fibrobacter succinogenes S85." Anaerobe 13, no. 2 (2007): 83–88. http://dx.doi.org/10.1016/j.anaerobe.2006.12.003.

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26

Faure, Denis, Jos Desair, Veerle Keijers та ін. "Growth of Azospirillum irakense KBC1 on the Aryl β-Glucoside Salicin Requires either salA or salB". Journal of Bacteriology 181, № 10 (1999): 3003–9. http://dx.doi.org/10.1128/jb.181.10.3003-3009.1999.

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ABSTRACT The rhizosphere nitrogen-fixing bacteriumAzospirillum irakense KBC1 is able to grow on pectin and β-glucosides such as cellobiose, arbutin, and salicin. Two adjacent genes, salA and salB, conferring β-glucosidase activity to Escherichia coli, have been identified in a cosmid library of A. irakense DNA. The SalA and SalB enzymes preferentially hydrolyzed aryl β-glucosides. A Δ(salA-salB) A. irakense mutant was not able to grow on salicin but could still utilize arbutin, cellobiose, and glucose for growth. This mutant could be complemented by either salA or salB, suggesting functional r

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27

Enkhbaatar, Bolormaa, Uyangaa Temuujin, Ju-Hyeon Lim, Won-Jae Chi, Yong-Keun Chang, and Soon-Kwang Hong. "Identification and Characterization of a Xyloglucan-Specific Family 74 Glycosyl Hydrolase from Streptomyces coelicolor A3(2)." Applied and Environmental Microbiology 78, no. 2 (2011): 607–11. http://dx.doi.org/10.1128/aem.06482-11.

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ABSTRACTThesco6545gene ofStreptomyces coelicolorA3(2) was nominated as a putative cellulase with 863 mature-form amino acids (90.58 kDa). We overexpressed and purified Sco6545 and demonstrated that the protein is not a cellulase but a xyloglucan-specific glycosyl hydrolase which cleaves xyloglucan at unbranched glucose residues.

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28

Hossain, Md Anowar, and Hairul Azman Roslan. "Molecular Phylogeny and Predicted 3D Structure of Plantbeta-D-N-Acetylhexosaminidase." Scientific World Journal 2014 (2014): 1–14. http://dx.doi.org/10.1155/2014/186029.

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beta-D-N-Acetylhexosaminidase, a family 20 glycosyl hydrolase, catalyzes the removal ofβ-1,4-linkedN-acetylhexosamine residues from oligosaccharides and their conjugates. We constructed phylogenetic tree ofβ-hexosaminidases to analyze the evolutionary history and predicted functions of plant hexosaminidases. Phylogenetic analysis reveals the complex history of evolution of plantβ-hexosaminidase that can be described by gene duplication events. The 3D structure of tomatoβ-hexosaminidase (β-Hex-Sl) was predicted by homology modeling using 1now as a template. Structural conformity studies of the

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29

FERNANDES, Ana C., Carlos M. G. A. FONTES, Harry J. GILBERT, Geoffrey P. HAZLEWOOD, Tito H. FERNANDES, and Luis M. A. FERREIRA. "Homologous xylanases from Clostridium thermocellum: evidence for bi-functional activity, synergism between xylanase catalytic modules and the presence of xylan-binding domains in enzyme complexes." Biochemical Journal 342, no. 1 (1999): 105–10. http://dx.doi.org/10.1042/bj3420105.

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Clostridium thermocellum produces a consortium of plant-cell-wall hydrolases that form a cell-bound multi-enzyme complex called the cellulosome. In the present study two similar xylanase genes, xynU and xynV, were cloned from C. thermocellum strain YS and sequenced. The deduced primary structures of both xylanases, xylanase U (XylU) and xylanase V (XylV), were homologous with the previously characterized xylanases from C. thermocellum strain F1. Truncated derivatives of XylV were produced and their biochemical properties were characterized. The xylanases were shown to be remarkably thermostabl

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30

Kang, Young-Min, Tae-Ho Kang, Han-Dae Yun та Kye-Man Cho. "Enhancing the Enzymatic Activity of the Multifunctional β-Glycosyl Hydrolase (Cel44C-Man26AP558) from Paenibacillus polymyxa GS01 Using DNA Shuffling". Korean Journal of Microbiology 48, № 2 (2012): 73–78. http://dx.doi.org/10.7845/kjm.2012.48.2.073.

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31

Arul, Loganathan, George Benita, Duraialagaraja Sudhakar, Balsamy Thayumanavan and Ponnusamy Balasubramanian та Ponnusamy Balasubramanian. "β-glucuronidase of family-2 glycosyl hydrolase: A missing member in plants". Bioinformation 3, № 5 (2008): 194–97. http://dx.doi.org/10.6026/97320630003194.

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32

Do, Thi Tuyen, Dinh Thi Quyen, Thi Nuong Nguyen, and Van Thuat Nguyen. "Molecular characterization of a glycosyl hydrolase family 10 xylanase from Aspergillus niger." Protein Expression and Purification 92, no. 2 (2013): 196–202. http://dx.doi.org/10.1016/j.pep.2013.09.011.

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33

Tamayo-Ramos, Juan, and Margarita Orejas. "Enhanced glycosyl hydrolase production in Aspergillus nidulans using transcription factor engineering approaches." Biotechnology for Biofuels 7, no. 1 (2014): 103. http://dx.doi.org/10.1186/1754-6834-7-103.

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34

Thomas, Bruce R., Gabriel O. Romero, Donald J. Nevins, and Raymond L. Rodriguez. "New perspectives on the endo-beta-glucanases of glycosyl hydrolase Family 17." International Journal of Biological Macromolecules 27, no. 2 (2000): 139–44. http://dx.doi.org/10.1016/s0141-8130(00)00109-4.

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35

Thiery, Emilie, Jérémy Reniers, Johan Wouters, and Stéphane P. Vincent. "Stereoselective Synthesis of Boat-Locked Glycosides Designed as Glycosyl Hydrolase Conformational Probes." European Journal of Organic Chemistry 2015, no. 7 (2015): 1472–84. http://dx.doi.org/10.1002/ejoc.201403363.

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36

ARONSON, N. N., C. J. BLANCHARD, and J. D. MADURA. "ChemInform Abstract: Homology Modeling of Glycosyl Hydrolase Family 18 Enzymes and Proteins." ChemInform 29, no. 12 (2010): no. http://dx.doi.org/10.1002/chin.199812244.

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37

Bajwa, Paramjit K., Sean Harrington, Mehdi Dashtban та Hung Lee. "Expression and Characterization of Glycosyl Hydrolase Family 115 α-Glucuronidase fromScheffersomyces stipitis". Industrial Biotechnology 12, № 2 (2016): 98–104. http://dx.doi.org/10.1089/ind.2015.0031.

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38

Uno, Yuichi, Sae Hashidume, Osamu Kurita, Takayuki Fujiwara та Keiichi Nomura. "Dioscorea opposita Thunb. α-mannosidase belongs to the glycosyl hydrolase family 38". Acta Physiologiae Plantarum 32, № 4 (2010): 713–18. http://dx.doi.org/10.1007/s11738-009-0452-7.

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39

Attanasio, Francesco, Maurizio Bruschi, Giovanni Candiano, et al. "Analytical titration curves of glycosyl hydrolase Cel45 by combined isoelectric focusing — electrophoresis." Electrophoresis 20, no. 7 (1999): 1403–11. http://dx.doi.org/10.1002/(sici)1522-2683(19990601)20:7<1403::aid-elps1403>3.0.co;2-6.

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40

Tsai, Li-Chu, Imamaddin Amiraslanov, Hung-Ren Chen, et al. "Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage." Acta Crystallographica Section F Structural Biology Communications 71, no. 10 (2015): 1264–72. http://dx.doi.org/10.1107/s2053230x15015915.

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Exoglucanase/cellobiohydrolase (EC 3.2.1.176) hydrolyzes a β-1,4-glycosidic bond from the reducing end of cellulose and releases cellobiose as the major product. Three complex crystal structures of the glycosyl hydrolase 48 (GH48) cellobiohydrolase S (ExgS) from Clostridium cellulovorans with cellobiose, cellotetraose and triethylene glycol molecules were solved. The product cellobiose occupies subsites +1 and +2 in the open active-site cleft of the enzyme–cellotetraose complex structure, indicating an enzymatic hydrolysis function. Moreover, three triethylene glycol molecules and one pentaeth

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41

St John, Franz J., Javier M. González, and Edwin Pozharski. "Consolidation of glycosyl hydrolase family 30: A dual domain 4/7 hydrolase family consisting of two structurally distinct groups." FEBS Letters 584, no. 21 (2010): 4435–41. http://dx.doi.org/10.1016/j.febslet.2010.09.051.

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42

McKIE, Vincent A., Gary W. BLACK, Sarah J. MILLWARD-SADLER, Geoffrey P. HAZLEWOOD, Judith I. LAURIE, and Harry J. GILBERT. "Arabinanase A from Pseudomonas fluorescens subsp. cellulosa exhibits both an endo- and an exo- mode of action." Biochemical Journal 323, no. 2 (1997): 547–55. http://dx.doi.org/10.1042/bj3230547.

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Pseudomonas fluorescens subsp. cellulosa expressed arabinanase activity when grown on media supplemented with arabinan or arabinose. Arabinanase activity was not induced by the inclusion of other plant structural polysaccharides, and was repressed by the addition of glucose. The majority of the Pseudomonas arabinanase activity was extracellular. Screening of a genomic library of P. fluorescens subsp. cellulosa DNA constructed in Lambda ZAPII, for recombinants that hydrolysed Red-dyed arabinan, identified five arabinan-degrading plaques. Each of the phage contained the same Pseudomonas arabinan

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43

Nghi, Do Huu, Britta Bittner, Harald Kellner та ін. "The Wood Rot Ascomycete Xylaria polymorpha Produces a Novel GH78 Glycoside Hydrolase That Exhibits α-l-Rhamnosidase and Feruloyl Esterase Activities and Releases Hydroxycinnamic Acids from Lignocelluloses". Applied and Environmental Microbiology 78, № 14 (2012): 4893–901. http://dx.doi.org/10.1128/aem.07588-11.

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ABSTRACTSoft rot (type II) fungi belonging to the family Xylariaceae are known to substantially degrade hardwood by means of their poorly understood lignocellulolytic system, which comprises various hydrolases, including feruloyl esterases and laccase. In the present study, several members of the Xylariaceae were found to exhibit high feruloyl esterase activity during growth on lignocellulosic materials such as wheat straw (up to 1,675 mU g−1) or beech wood (up to 80 mU g−1). Following the ester-cleaving activity toward methyl ferulate, a hydrolase ofXylaria polymorphawas produced in solid-sta

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44

Hakamada, Yoshihiro, Shoukan Arata, and Shinichi Ohashi. "Purification and Characterization of a Xyloglucan-specific Glycosyl Hydrolase from Aspergillus oryzae RIB40." Journal of Applied Glycoscience 58, no. 2 (2011): 47–51. http://dx.doi.org/10.5458/jag.jag.jag-2010_010.

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45

Serna, Sonia, María Ercibengoa, Jose María Marimón, and Niels-Christian Reichardt. "Measuring Bacterial Glycosyl Hydrolase Activity with a Soluble Capture Probe by Mass Spectrometry." Analytical Chemistry 90, no. 21 (2018): 12536–43. http://dx.doi.org/10.1021/acs.analchem.8b02434.

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46

Elifantz, Hila, Lisa A. Waidner, Vanessa K. Michelou, Matthew T. Cottrell, and David L. Kirchman. "Diversity and abundance of glycosyl hydrolase family 5 in the North Atlantic Ocean." FEMS Microbiology Ecology 63, no. 3 (2008): 316–27. http://dx.doi.org/10.1111/j.1574-6941.2007.00429.x.

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47

ITO, Akihiro, Taka-aki OKAMURA, Koichi UEGAKI, et al. "Mass Spectrometric Analysis Using Ruthenium (II)-Labeling for Identification of Glycosyl Hydrolase Product." Bioscience, Biotechnology, and Biochemistry 73, no. 2 (2009): 428–30. http://dx.doi.org/10.1271/bbb.80492.

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48

Yu, Shan, Tiantian Su, Huijun Wu, et al. "PslG, a self-produced glycosyl hydrolase, triggers biofilm disassembly by disrupting exopolysaccharide matrix." Cell Research 25, no. 12 (2015): 1352–67. http://dx.doi.org/10.1038/cr.2015.129.

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49

Ding, Shi-You, Edward A. Bayer, David Steiner, Yuval Shoham, and Raphael Lamed. "A Novel Cellulosomal Scaffoldin fromAcetivibrio cellulolyticus That Contains a Family 9 Glycosyl Hydrolase." Journal of Bacteriology 181, no. 21 (1999): 6720–29. http://dx.doi.org/10.1128/jb.181.21.6720-6729.1999.

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ABSTRACT A novel cellulosomal scaffoldin gene, termed cipV, was identified and sequenced from the mesophilic cellulolytic anaerobeAcetivibrio cellulolyticus. Initial identification of the protein was based on a combination of properties, including its high molecular weight, cellulose-binding activity, glycoprotein nature, and immuno-cross-reactivity with the cellulosomal scaffoldin ofClostridium thermocellum. The cipV gene is 5,748 bp in length and encodes a 1,915-residue polypeptide with a calculated molecular weight of 199,496. CipV contains an N-terminal signal peptide, seven type I cohesin

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Sathya, T. A., and Mahejibin Khan. "Diversity of Glycosyl Hydrolase Enzymes from Metagenome and Their Application in Food Industry." Journal of Food Science 79, no. 11 (2014): R2149—R2156. http://dx.doi.org/10.1111/1750-3841.12677.

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