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Glycoside hydrolase

José Munoz-Munoz, Alan Cartmell, Nicolas Terrapon, Arnaud Baslé, Bernard Henrissat, Harry J Gilbert
The human gut microbiota utilizes complex carbohydrates as major nutrients. The requirement for efficient glycan degrading systems exerts a major selective selection pressure on this microbial community. Thus, we propose that this microbial ecosystem represents a substantial resource for discovering novel carbohydrate active enzymes. To test this hypothesis we screened the potential enzymatic functions of hypothetical proteins encoded by genes of Bacteroides thetaiotaomicron that were upregulated by arabinogalactan arabinogalactan proteins or AGPs...
June 21, 2017: Journal of Biological Chemistry
Lijuan Wei, Hongju Jian, Kun Lu, Nengwen Yin, Jia Wang, Xiujian Duan, Wei Li, Liezhao Liu, Xinfu Xu, Rui Wang, Andrew H Paterson, Jiana Li
Candidate genes associated with lignin and lodging traits were identified by combining phenotypic, genotypic, and gene expression data in B. napus. Brassica napus is one of the world's most important oilseed crops, but its yield can be dramatically reduced by lodging, bending, and falling of its vertical stems. Lignin has been shown to contribute to stem mechanical strength. In this study, we found that the syringyl/guaiacyl (S/G) monolignol ratio exhibits a significant negative correlation with disease and lodging resistance...
June 20, 2017: TAG. Theoretical and Applied Genetics. Theoretische und Angewandte Genetik
Xueyan Gao, Congyan Wang, Wei Dai, Shenrong Ren, Fang Tao, Xingbing He, Guomin Han, Wei Wang
A recent algicidal mode indicates that fungal mycelia can wrap and eliminate almost all co-cultivated algal cells within a short time span. However, the underlying molecular mechanism is rarely understood. We applied proteomic analysis to investigate the algicidal process of Trametes versicolor F21a and identified 3,754 fungal proteins. Of these, 30 fungal enzymes with endo- or exoglycosidase activities such as β-1,3-glucanase, α-galactosidase, α-glucosidase, alginate lyase and chondroitin lyase were significantly up-regulated...
June 20, 2017: Scientific Reports
Brendan D Snarr, Perrin Baker, Natalie C Bamford, Yukiko Sato, Hong Liu, Mélanie Lehoux, Fabrice N Gravelat, Hanna Ostapska, Shane R Baistrocchi, Robert P Cerone, Elan E Filler, Matthew R Parsek, Scott G Filler, P Lynne Howell, Donald C Sheppard
Galactosaminogalactan and Pel are cationic heteropolysaccharides produced by the opportunistic pathogens Aspergillus fumigatus and Pseudomonas aeruginosa, respectively. These exopolysaccharides both contain 1,4-linked N-acetyl-d-galactosamine and play an important role in biofilm formation by these organisms. Proteins containing glycoside hydrolase domains have recently been identified within the biosynthetic pathway of each exopolysaccharide. Recombinant hydrolase domains from these proteins (Sph3h from A...
June 20, 2017: Proceedings of the National Academy of Sciences of the United States of America
Jie Zhou, Zhoukun Li, Jiale Wu, Lifeng Li, Ding Li, Xianfeng Ye, Xue Luo, Yan Huang, Zhongli Cui, Hui Cao
A novel β-(1,3)-glucanase gene designated lamC, cloned from Corallococcus sp. EGB, contains a fascin-like module and a glycoside hydrolase family 16 (GH16) catalytic module. LamC displays broad hydrolytic activity toward various polysaccharides. Analysis of the hydrolytic products revealed that LamC is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan and xylan substrates. Site-directed mutagenesis of conserved catalytic Glu residues (E304A and E309A) demonstrated that these activities were derived from the same active site...
June 16, 2017: Applied and Environmental Microbiology
Nandita Pasari, Nidhi Adlakha, Mayank Gupta, Zeenat Bashir, Girish H Rajacharya, Garima Verma, Manoj Munde, Rakesh Bhatnagar, Syed Shams Yazdani
Cellulolytic enzymes capable of hydrolyzing plant biomass are secreted by microbial cells specifically in response to the carbon substrate present in the environment. These enzymes consist of a catalytic domain, generally appended to one or more non-catalytic Carbohydrate Binding Module (CBM), which enhances their activity towards recalcitrant biomass. In the present study, the genome of a cellulolytic microbe Paenibacillus polymyxa A18 was annotated for the presence of CBMs and analyzed their expression in response to the plant biomass and model polysaccharides Avicel, CMC and xylan using quantitative PCR...
June 16, 2017: Scientific Reports
Yi-Rui Yin, Zhao-Hui Meng, Qing-Wen Hu, Zhao Jiang, Wen-Dong Xian, Lin-Hua Li, Wei Hu, Feng Zhang, En-Min Zhou, Xiao-Yang Zhi, Wen-Jun Li
Thermoactinospora rubra YIM 77501(T) is an aerobic, Gram-positive, spore-forming and cellulose degrading thermophilic actinomycete isolated from a sandy soil sample of a volcano. Its growth temperature range is 28-60°C. The genomic sequence of this strain revealed that there are 27 cellulase genes belonging to six glycoside hydrolase families. To understand the strategy that this strain uses to utilize carbon sources such as cellulose at different temperatures, comparative transcriptomics analysis of T. rubra YIM 77501(T) was performed by growing it with cellulose (CMC) and without cellulose (replaced with glucose) at 30, 40, and 50°C, respectively...
2017: Frontiers in Microbiology
Moisés Martínez-Castillo, Rosa Elena Cárdenas-Guerra, Rossana Arroyo, Anjan Debnath, Mario Alberto Rodríguez, Myrna Sabanero, Fernando Flores-Sánchez, Fernando Navarro-Garcia, Jesús Serrano-Luna, Mineko Shibayama
AIM: The aim of this work was to identify, characterize and evaluate the pathogenic role of mucinolytic activity released by Naegleria fowleri. MATERIALS & METHODS: Zymograms, protease inhibitors, anion exchange chromatography, MALDI-TOF-MS, enzymatic assays, Western blot, and confocal microscopy were used to identify and characterize a secreted mucinase; inhibition assays using antibodies, dot-blots and mouse survival tests were used to evaluate the mucinase as a virulence factor...
June 13, 2017: Future Microbiology
Javier Iglesias-Fernández, Susan M Hancock, Seung Seo Lee, Maola Khan, Jo Kirkpatrick, Neil J Oldham, Katherine McAuley, Anthony Fordham-Skelton, Carme Rovira, Benjamin G Davis
SNi-like mechanisms, which involve front-face leaving group departure and nucleophile approach, have been observed experimentally and computationally in chemical and enzymatic substitution at α-glycosyl electrophiles. Since SNi-like, SN1 and SN2 substitution pathways can be energetically comparable, engineered switching could be feasible. Here, engineering of Sulfolobus solfataricus β-glycosidase, which originally catalyzed double SN2 substitution, changed its mode to SNi-like. Destruction of the first SN2 nucleophile through E387Y mutation created a β-stereoselective catalyst for glycoside synthesis from activated substrates, despite lacking a nucleophile...
June 12, 2017: Nature Chemical Biology
Narine Arabyan, Bihua C Huang, Bart C Weimer
Lysozyme enzymes hydrolyze the β-1,4-glycosidic bond in oligosaccharides. These enzymes are part of a broad group of glucoside hydrolases that are poorly characterized; however, they are important for growth and are being recognized as emerging virulence factors. This is the release of four lysozyme-encoding-gene-deletion mutants in Salmonella enterica serovar Typhimurium LT2.
June 8, 2017: Genome Announcements
Azucena Herrera-González, Gema Núñez-López, Sandrine Morel, Lorena Amaya-Delgado, Georgina Sandoval, Anne Gschaedler, Magali Remaud-Simeon, Javier Arrizon
Enzymatic fructosylation of organic acceptors other than sugar opens access to the production of new molecules that do not exist in nature. These new glycoconjugates may have improved physical-chemical and bioactive properties like solubility, stability, bioavailability, and bioactivity. This review focuses on different classes of acceptors including alkyl alcohols, aromatic alcohols, alkaloids, flavonoids, and xanthonoids, which were tested for the production of fructoderivatives using enzymes from the glycoside hydrolase (GH) families 32 and 68 that use sucrose as donor substrate...
June 8, 2017: Applied Microbiology and Biotechnology
Yan-Xiao Li, Ping Yi, Qiao-Juan Yan, Zhen Qin, Xue-Qiang Liu, Zheng-Qiang Jiang
BACKGROUND: β-Mannanase randomly cleaves the β-1,4-linked mannan backbone of hemicellulose, which plays the most important role in the enzymatic degradation of mannan. Although the industrial applications of β-mannanase have tremendously expanded in recent years, the wild-type β-mannanases are still defective for some industries. The glycoside hydrolase (GH) family 5 β-mannanase (RmMan5A) from Rhizomucor miehei shows many outstanding properties, such as high specific activity and hydrolysis property...
2017: Biotechnology for Biofuels
Mukil Maruthamuthu, Jan Dirk van Elsas
BACKGROUND: Enzyme discovery is a promising approach to aid in the deconstruction of recalcitrant plant biomass in an industrial process. Novel enzymes can be readily discovered by applying metagenomics on whole microbiomes. Our goal was to select, examine, and characterize eight novel glycoside hydrolases that were previously detected in metagenomic libraries, to serve biotechnological applications with high performance. RESULTS: Here, eight glycosyl hydrolase family candidate genes were selected from metagenomes of wheat straw-degrading microbial consortia using molecular cloning and subsequent gene expression studies in Escherichia coli...
2017: Biotechnology for Biofuels
Hikmate Abriouel, Beatriz Pérez Montoro, Carlos S Casimiro-Soriguer, Antonio J Pérez Pulido, Charles W Knapp, Natacha Caballero Gómez, Sonia Castillo-Gutiérrez, María D Estudillo-Martínez, Antonio Gálvez, Nabil Benomar
Lactobacillus pentosus MP-10 is a potential probiotic lactic acid bacterium originally isolated from naturally fermented Aloreña green table olives. The entire genome sequence was annotated to in silico analyze the molecular mechanisms involved in the adaptation of L. pentosus MP-10 to the human gastrointestinal tract (GIT), such as carbohydrate metabolism (related with prebiotic utilization) and the proteins involved in bacteria-host interactions. We predicted an arsenal of genes coding for carbohydrate-modifying enzymes to modify oligo- and polysaccharides, such as glycoside hydrolases, glycoside transferases, and isomerases, and other enzymes involved in complex carbohydrate metabolism especially starch, raffinose, and levan...
2017: Frontiers in Microbiology
Darryl R Jones, Muhammed Salah Uddin, Robert J Gruninger, Thi Thanh My Pham, Dallas Thomas, Alisdair B Boraston, Jonathan Briggs, Benjamin Pluvinage, Tim A McAllister, Robert J Forster, Adrian Tsang, L Brent Selinger, D Wade Abbott
Enzyme activities that improve digestion of recalcitrant plant cell wall polysaccharides may offer solutions for sustainable industries. To this end, anaerobic fungi in the rumen have been identified as a promising source of novel carbohydrate active enzymes (CAZymes) that modify plant cell wall polysaccharides and other complex glycans. Many CAZymes share insufficient sequence identity to characterized proteins from other microbial ecosystems to infer their function; thus presenting challenges to their identification...
June 6, 2017: Journal of Biological Chemistry
Oscar Crasson, Gaston Courtade, Raphaël R Léonard, Finn Lillelund Aachmann, François Legrand, Raffaella Parente, Denis Baurain, Moreno Galleni, Morten Sørlie, Marylène Vandevenne
Chitin is an important structural component of numerous fungal pathogens and parasitic nematodes. The human macrophage chitotriosidase (HCHT) is a chitinase that hydrolyses glycosidic bonds between the N-acetyl-D-glucosamine units of this biopolymer. HCHT belongs to the Glycoside Hydrolase (GH) superfamily and contains a well-characterized catalytic domain appended to a chitin-binding domain (ChBDCHIT1). Although its precise biological function remains unclear, HCHT has been described to be involved in innate immunity...
June 5, 2017: Scientific Reports
Xueping Tian, Tao Yang, Jingzhong He, Qian Chu, Xiaojun Jia, Jun Huang
The fungal community and the population of 16S rRNA, 18S rRNA and cellulose-degrading genes during the 30-day composting process of Chinese medicinal herbal residues were investigated using Illumina MiSeq and quantitative real-time PCR. An obvious succession of fungal communities occurred during the composting process. Unidentified fungi predominated in the raw materials. As composting progressed, Ascomycota became the most dominant phylum, with Aspergillus being the most dominant genus, and Aspergillus fumigatus making up 99...
May 21, 2017: Bioresource Technology
M Saritha, Rameshwar Tiwari, Surender Singh, Pawan K S Nain, Sarika Rana, Anurup Adak, Anju Arora, Lata Nain
A successful lignocellulosic ethanol production process needs to address the technological impediments such as cost-competitiveness and sustainability of the process. Effective biomass utilization requires a repertoire of enzymes including various accessory enzymes. Developing an enzyme preparation with defined hydrolytic activities can circumvent the need for supplementing cellulases with accessory enzymes for enhanced hydrolysis. With this objective, mixture design approach was used in the present study to enhance glycoside hydrolase production of a fungal isolate, Aspergillus terreus CM20, by determining the proportion of different lignocellulosic components as enzyme inducers in the culture medium...
August 2016: Indian Journal of Experimental Biology
Xiao-Jun Fan, Chun Yang, Chang Zhang, Hui Ren, Jian-Dong Zhang
Chitinases are glycosyl hydrolases that catalyze the hydrolysis of β-(1,4)-glycosidic bonds in chitin, the major structural polysaccharide presented in the cuticle and gut peritrophic matrix of insects. Two aspartate residues (D143, D145) and one tryptophan (W146) in the Lymantria dispar chitinase are highly conserved residues observed within the second conserved motif of the family 18 chitinase catalytic region. In this study, a chitinase cDNA, LdCht5, was cloned from L. dispar, and the roles of the three residues were investigated using site-directed mutagenesis and substituting them with three other amino acids...
June 2, 2017: Applied Biochemistry and Biotechnology
Maria Elena Ortiz-Soto, Christian Possiel, Julian Görl, Andreas Vogel, Ramona Schmiedel, Jürgen Seibel
Bacterial levansucrases produce β(2,6)-linked levan-type polysaccharides using sucrose or sucrose analogues as donor/acceptor substrates. However, the dominant reaction of Bacillus megaterium levansucrase (Bm-LS) is hydrolysis. Single domain levansucrases from Gram-positive bacteria display a wide substrate-binding pocket with open access to water, challenging engineering for transfructosylation-efficient enzymes. We pursued a shift in reaction specificity by either modifying the water distribution in the active site or the coordination of the catalytic acid/base (E352) and the nucleophile (D95), thus affecting the fructosyl-transfer rate and allowing acceptors other than water to occupy the active site...
May 30, 2017: Glycobiology
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