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63 matches found in 28 documents. Search time: 0.002 seconds.
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Score: 10.00
Title: Characterization of beta-glucosidase from a strain of Penicillium purpurogenum KJS506 .
Literature: oryza Field: abstract Doc ID: pub20043150 Accession (PMID): 20043150
Abstract: A novel beta-glucosidase ( BGL ) -producing strain was isolated and identified as Penicillium purpurogenum KJS506 based on its morphology and internal transcribed spacer ( ITS ) rDNA gene sequence . When rice straw and corn steep powder were used as carbon and nitrogen sources , respectively , the maximal BGL activity of 12 . 3 U ml ( -1 ) , one of the highest levels among BGL-producing microorganisms was observed . The optimum temperature and pH for BGL production were 32 degrees C and 4 , respectively . An extracellular BGL was purified to homogeneity by sequential chromatography of P purpurogenum culture supernatants , and the purified BGL showed higher activity ( V ( max ) = 934 U mg protein ( -1 ) ) than most BGLs from other sources . The complete ORF of bgl3 was cloned from P purpurogenum by a modified thermal asymmetric interlaced polymerase chain reaction . The bgl3 gene consists of a 2 , 571-bp ORF and encodes a putative protein containing 856 amino acids with a calculated molecular mass of 89 , 624 Da . The putative gene product was identified as a member of glycoside hydrolase family 3 . The present results should contribute to improved industrial production of BGL by P purpurogenum KJS506 .
Score: 7.00
Title: Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition .
Literature: oryza Field: abstract Doc ID: pub22418094 Accession (PMID): 22418094
Abstract: The rice BGlu1 beta-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from alpha-d-glucopyranosyl fluoride ( GlcF ) donor and p-nitrophenyl ( pNP ) cellobioside ( Glc2-pNP ) or cello-oligosaccharide acceptors . When activity with other donors and acceptors was tested , the initial enzyme preparation cleaved pNP-beta-D-glucopyranoside ( Glc-pNP ) and pNP-beta-D-fucopyranoside ( Fuc-pNP ) to pNP and glucose and fucose , suggesting contamination with wild type BGlu1 beta-glucosidase . The products from reaction of GlcF and Fuc-pNP included Fuc-beta- ( 1-->3 ) -Fuc-pNP , Glc-beta- ( 1-->3 ) -Fuc-pNP , and Fuc-beta- ( 1-->4 ) -Glc-beta- ( 1-->3 ) -Fuc-pNP , suggesting the presence of both wild type BGlu1 and its glycosynthase . Inhibition of the BGlu1 beta-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1 . Rice BGlu1 E386G-2 , generated from a new construct designed to minimize back-mutation , showed glycosynthase activity without wild type hydrolytic or transglycosylation activity . E386G-2 catalyzed transfer of glycosyl residues from GlcF , alpha-L-arabinosyl fluoride , alpha-D-fucosyl fluoride , alpha-D-galactosyl fluoride , alpha-D-mannosyl fluoride , and alpha-D-xylosyl fluoride donors to Glc2-pNP acceptor . The synthetic products from the reactions of alpha-fucosyl fluoride and alpha-mannosyl fluoride donors were confirmed to result from addition of a beta- ( 1-->4 ) -linked glycosyl residue . Moreover , the E386G glycosynthase transferred glucose from GlcF donor to glucose , cellobiose , Glc-pNP , Fuc-pNP , pNP-beta-D-galactopyranoside , and pNP-beta-D-xylopyranoside acceptors , but little to pNP-beta-D-mannopyranoside . Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH . Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities .
Score: 6.00
Title: Complex arrangement of dispersed repeated DNA sequences in Oryza officinalis .
Literature: oryza Field: abstract Doc ID: pub8851805 Accession (PMID): 8851805
Abstract: A 525-bp BglII fragment was isolated from Oryza officinalis DNA ( accession W1278 ) and shown to correspond to a new dispersed repetitive DNA sequence with specificity restricted to a subset of the wild rice with a C genome . The sequence of the fragment was determined but it does not correspond to any sequence already present in databases . It contains several imperfect palindromes . Larger genomic clones ( 12-18 kbp ) were isolated and all contain sequences homologous to the BglII element . Analysis of these clones confirms that the BglII element is dispersed in the O officinalis genome . From one genomic clone , the sequences adjacent to the BglII element were subcloned and used as probes to demonstrate that the sequences flanking the BglII element are variable in different genomic clones and that some of them are also dispersed repetitive sequences . The genomic specificity of two of these dispersed repeats was evaluated and shown to be different from that of the initial BglII element . This analysis revealed a complex arrangement of various dispersed repeated sequences .
Score: 5.00
Title: Expression of thermostable bacterial beta-glucosidase ( BglB ) in transgenic tobacco plants .
Literature: oryza Field: abstract Doc ID: pub20427180 Accession (PMID): 20427180
Abstract: Transgenic tobacco plants expressing the hyperthermostable beta-glucosidase BglB of Thermotoga maritima were generated with the goal of cost-effective production of the enzyme for the application in bioconversion of lignocellulosic biomass . The enzyme was targeted to the cytosol and chloroplasts , where it accumulated to level of 4 . 5% and 5 . 8% of total soluble protein , respectively . The optimal temperature and pH of the plant-expressed BglB was 80 degrees C and 4 . 5 , respectively . BglB activity was preserved in leaves after lyophilization , but decreased by over 70% with drying at room temperature . When BglB was synergistically supplied in a 1% ( w/v ) rice straw with Cel5A for efficient cellulase conversion , a 37% increase in glucose was observed . This report demonstrates the potential of utilizing transgenic tobacco for mass production of BglB .
Score: 4.00
Title: Purification , crystallization and preliminary X-ray analysis of rice BGlu1 beta-glucosidase with and without 2-deoxy-2-fluoro-beta-D-glucoside .
Literature: oryza Field: abstract Doc ID: pub16880561 Accession (PMID): 16880561
Abstract: Rice ( Oryza sativa ) BGlu1 beta-glucosidase was expressed in Escherichia coli with N-terminal thioredoxin and hexahistidine tags and purified by immobilized metal-affinity chromatography ( IMAC ) . After removal of the N-terminal tags , cation-exchange and S-200 gel-filtration chromatography yielded a 50 kDa BGlu1 with >95% purity . The free enzyme and a complex with 2 , 4-dinitrophenyl-2-deoxy-2-fluoro-beta-D-glucopyranoside inhibitor were crystallized by microbatch and hanging-drop vapour diffusion . Small tetragonal crystals of BGlu1 with and without inhibitor grew in 18% ( w/v ) PEG 8000 with 0 . 1 M sodium cacodylate pH 6 . 5 and 0 . 2 M zinc acetate . Crystals of BGlu1 with inhibitor were streak-seeded into 23% ( w/v ) PEG MME 5000 , 0 . 2 M ammonium sulfate , 0 . 1 M MES pH 6 . 7 to yield larger crystals . Crystals with and without inhibitor diffracted to 2 . 15 and 2 . 75 angstroms resolution , respectively , and had isomorphous orthorhombic unit cells belonging to space group P2 ( 1 ) 2 ( 1 ) 2 ( 1 ) .

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