The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds

2002 ◽  
Vol 363 (2) ◽  
pp. 377-386 ◽  
Author(s):  
Ronald P. de VRIES ◽  
Patricia A. vanKUYK ◽  
Harry C.M. KESTER ◽  
Jaap VISSER
Keyword(s):  
Aspergillus Niger ◽  
Sugar Beet ◽  
Aromatic Compounds ◽  
Plant Cell Wall ◽  
Sequence Similarity ◽  
Feruloyl Esterase ◽  
Cell Wall Polysaccharides ◽  
Gene Encoding ◽  
Reading Frame ◽  
Wheat Arabinoxylan

The faeB gene encoding a second feruloyl esterase from Aspergillus niger has been cloned and characterized. It consists of an open reading frame of 1644bp containing one intron. The gene encodes a protein of 521 amino acids that has sequence similarity to that of an Aspergillus oryzae tannase. However, the encoded enzyme, feruloyl esterase B (FAEB), does not have tannase activity. Comparison of the physical characteristics and substrate specificity of FAEB with those of a cinnamoyl esterase from A. niger [Kroon, Faulds and Williamson (1996) Biotechnol. Appl. Biochem. 23, 255–262] suggests that they are in fact the same enzyme. The expression of faeB is specifically induced in the presence of certain aromatic compounds, but not in the presence of other constituents present in plant-cell-wall polysaccharides such as arabinoxylan or pectin. The expression profile of faeB in the presence of aromatic compounds was compared with the expression of A. nigerfaeA, encoding feruloyl esterase A (FAEA), and A. nigerbphA, the gene encoding a benzoate-p-hydroxylase. All three genes have different subsets of aromatic compounds that induce their expression, indicating the presence of different transcription activating systems in A. niger that respond to aromatic compounds. Comparison of the activity of FAEA and FAEB on sugar-beet pectin and wheat arabinoxylan demonstrated that they are both involved in the degradation of both polysaccharides, but have opposite preferences for these substrates. FAEA is more active than FAEB towards wheat arabinoxylan, whereas FAEB is more active than FAEA towards sugar-beet pectin.

scholarly journals Regulation of the Feruloyl Esterase (faeA) Gene from Aspergillus niger

1999 ◽  
Vol 65 (12) ◽  
pp. 5500-5503 ◽  
Author(s):  
Ronald P. de Vries ◽  
Jaap Visser
Keyword(s):  
Cell Wall ◽  
Aspergillus Niger ◽  
Ferulic Acid ◽  
Methoxy Group ◽  
Plant Cell Wall ◽  
Ring Structure ◽  
Feruloyl Esterase ◽  
Cell Wall Polysaccharides ◽  
Aromatic Residues ◽  
Encoding Gene

ABSTRACT Feruloyl esterases can remove aromatic residues (e.g., ferulic acid) from plant cell wall polysaccharides (xylan, pectin) and are essential for complete degradation of these polysaccharides. Expression of the feruloyl esterase-encoding gene (faeA) fromAspergillus niger depends on d-xylose (expression is mediated by XlnR, the xylanolytic transcriptional activator) and on a second system that responds to aromatic compounds with a defined ring structure, such as ferulic acid and vanillic acid. Several compounds were tested, and all of the inducing compounds contained a benzene ring which had a methoxy group at C-3 and a hydroxy group at C-4 but was not substituted at C-5. Various aliphatic groups occurred at C-1. faeA expression in the presence of xylose or ferulic acid was repressed by glucose. faeA expression in the presence of ferulic acid and xylose was greater thanfaeA expression in the presence of either compound alone. The various inducing systems allow A. niger to produce feruloyl esterase not only during growth on xylan but also during growth on other ferulic acid-containing cell wall polysaccharides, such as pectin.

scholarly journals Characterization of the gene celD and its encoded product 1,4-β-d-glucan glucohydrolase D from Pseudomonas fluorescens subsp. cellulosa

1992 ◽  
Vol 285 (3) ◽  
pp. 947-955 ◽  
Author(s):  
J E Rixon ◽  
L M A Ferreira ◽  
A J Durrant ◽  
J I Laurie ◽  
G P Hazlewood ◽  
...  
Keyword(s):  
Pseudomonas Fluorescens ◽  
Plant Cell Wall ◽  
Genomic Library ◽  
Cell Envelope ◽  
Sequence Similarity ◽  
Significant Proportion ◽  
Structural Similarity ◽  
Reading Frame ◽  
E Coli ◽  
Beta Glucosidase

A genomic library of Pseudomonas fluorescens subsp. cellulosa DNA constructed in pUC18 and expressed in Escherichia coli was screened for recombinants expressing 4-methylumbelliferyl beta-D-glucoside hydrolysing activity (MUGase). A single MUGase-positive clone was isolated. The MUGase hydrolysed cellobiose, cellotriose, cellotetraose, cellopentaose and cellohexaose to glucose, by sequentially cleaving glucose residues from the non-reducing end of the cello-oligosaccharides. The Km values for cellobiose and cellohexaose hydrolysis were 1.2 mM and 28 microM respectively. The enzyme exhibited no activity against soluble or insoluble cellulose, xylan and xylobiose. Thus the MUGase is classified as a 1,4-beta-D-glucan glucohydrolase (EC 3.2.1.74) and is designated 1,4-beta-D-glucan glucohydrolase D (CELD). When expressed by E. coli, CELD was located in the cell-envelope fraction; a significant proportion of the native enzyme was also associated with the cell envelope when synthesized by its endogenous host. The nucleotide sequence of the gene, celD, which encodes CELD, revealed an open reading frame of 2607 bp, encoding a protein of M(r) 92,000. The deduced primary structure of CELD was confirmed by the M(r) of CELD (85,000) expressed by E. coli and P. fluorescens subsp. cellulosa, and by the experimentally determined N-terminus of the enzyme purified from E. coli, which showed identity with residues 52-67 of the celD translated sequence. The structure of the N-terminal region of full-length CELD was similar to the signal peptides of P. fluorescens subsp. cellulosa plant-cell-wall hydrolases. Deletion of the N-terminal 47 residues of CELD solubilized MUGase activity in E. coli. CELD exhibited sequence similarity with beta-glucosidase B of Clostridium thermocellum, particularly in the vicinity of the active-site aspartate residue, but did not display structural similarity with the mature forms of cellulases and xylanases expressed by P. fluorescens subsp. cellulosa.

Identification of a bacterial di-haem cytochrome c peroxidase from Methylomicrobium album BG8

Microbiology ◽  
2010 ◽  
Vol 156 (9) ◽  
pp. 2682-2690 ◽  
Author(s):  
O. A. Karlsen ◽  
Ø. Larsen ◽  
H. B. Jensen
Keyword(s):  
Copper Ions ◽  
Sequence Similarity ◽  
Physiological Role ◽  
Growth Conditions ◽  
Inverse Pcr ◽  
Restriction Enzyme Digestion ◽  
Methylococcus Capsulatus ◽  
Gene Encoding ◽  
Reading Frame ◽  
Methylomicrobium Album

The nucleotide sequence of an open reading frame (corB) downstream of the copper-repressible CorA-encoding gene of the methanotrophic bacterium Methylomicrobium album BG8 was obtained by restriction enzyme digestion and inverse PCR. The amino acid sequence deduced from this gene showed significant sequence similarity to the surface-associated di-haem cytochrome c peroxidase (SACCP) previously isolated from Methylococcus capsulatus (Bath), including both c-type haem-binding motifs. Homology analysis placed this protein, phylogenetically, within the subfamily containing the M. capsulatus SACCP of the bacterial di-haem cytochrome c peroxidase (BCCP) family of proteins. Immunospecific recognition confirmed synthesis of the M. album CorB as a protein non-covalently associated with the outer membrane and exposed to the periplasm. corB expression is regulated by the availability of copper ions during growth and the protein is most abundant in M. album when grown at a low copper-to-biomass ratio, indicating an important physiological role of CorB under these growth conditions. corB was co-transcribed with the gene encoding CorA, constituting a copper-responding operon, which appears to be under the control of a σ 54-dependent promoter. M. album CorB is the second isolated member of the recently described subfamily of the BCCP family of proteins. So far, these proteins have only been described in methanotrophic bacteria.

scholarly journals Enzymic and molecular characterization of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC 7942: resistance of the enzyme to hydrogen peroxide

1996 ◽  
Vol 316 (2) ◽  
pp. 685-690 ◽  
Author(s):  
Masahiro TAMOI ◽  
Takahiro ISHIKAWA ◽  
Toru TAKEDA ◽  
Shigeru SHIGEOKA
Keyword(s):  
Amino Acid ◽  
Molecular Mass ◽  
Higher Plants ◽  
Sequence Similarity ◽  
Native Enzyme ◽  
Chromosomal Dna ◽  
Gene Encoding ◽  
Reading Frame ◽  
Synechococcus Pcc 7942 ◽  
Pcc 7942

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been purified to electrophoretic homogeneity from Synechococcus PCC 7942 cells. The native enzyme had a molecular mass of 160 kDa and consisted of four subunits with a molecular mass of 41 kDa. The activity was 6-fold higher with NADPH than with NADH; the apparent Km values for NADPH and NADH were 62±4.5 and 420±10.5 μM respectively. The gene encoding NADP-dependent GAPDH was cloned from the chromosomal DNA of Synechococcus 7942. A 1140 bp open reading frame, encoding an enzyme of 380 amino acid residues (approx. molecular mass of 41.3 kDa) was observed. The deduced amino acid sequence of the gene had a greater sequence similarity to the NADP-dependent and chloroplastic form than to the NAD-dependent and cytosolic form. The Synechococcus 7942 enzyme lacked one of the cysteines involved in the light-dependent regulation of the chloroplast enzymes of higher plants. The recombinant enzyme expressed in Escherichia coli as well as the native enzyme purified from Synechococcus 7942 cells were resistant to 1 mM H2O2.

scholarly journals Trichloroethene Reductive Dehalogenase fromDehalococcoides ethenogenes: Sequence of tceA and Substrate Range Characterization

2000 ◽  
Vol 66 (12) ◽  
pp. 5141-5147 ◽  
Author(s):  
Jon K. Magnuson ◽  
Margaret F. Romine ◽  
David R. Burris ◽  
Mark T. Kingsley
Keyword(s):  
Signal Sequence ◽  
Sequence Similarity ◽  
Inverse Pcr ◽  
Binding Motif ◽  
Gene Encoding ◽  
Sequence Comparisons ◽  
Reading Frame ◽  
Reductive Dehalogenase ◽  
Dehalococcoides Ethenogenes ◽  
Range Characterization

ABSTRACT The anaerobic bacterium Dehalococcoides ethenogenes is the only known organism that can completely dechlorinate tetrachloroethene or trichloroethene (TCE) to ethene via dehalorespiration. One of two corrinoid-containing enzymes responsible for this pathway, TCE reductive dehalogenase (TCE-RDase) catalyzes the dechlorination of TCE to ethene. TCE-RDase dehalogenated 1,2-dichloroethane and 1,2-dibromoethane to ethene at rates of 7.5 and 30 μmol/min/mg, respectively, similar to the rates for TCE,cis-dichloroethene (DCE), and 1,1-DCE. A variety of other haloalkanes and haloalkenes containing three to five carbon atoms were dehalogenated at lower rates. The gene encoding TCE-RDase,tceA, was cloned and sequenced via an inverse PCR approach. Sequence comparisons of tceA to proteins in the public databases revealed weak sequence similarity confined to the C-terminal region, which contains the eight-iron ferredoxin cluster binding motif, (CXXCXXCXXXCP)2. Direct N-terminal sequencing of the mature enzyme indicated that the first 42 amino acids constitute a signal sequence containing the twin-arginine motif, RRXFXK, associated with the Sec-independent membrane translocation system. This information coupled with membrane localization studies indicated that TCE-RDase is located on the exterior of the cytoplasmic membrane. Like the case for the two other RDases that have been cloned and sequenced, a small open reading frame, tceB, is proposed to be involved with membrane association of TCE-RDase and is predicted to be cotranscribed with tceA.

scholarly journals Molecular Cloning and Expression Analysis of the Rhodobacter capsulatus sodB Gene, Encoding an Iron Superoxide Dismutase

1998 ◽  
Vol 180 (20) ◽  
pp. 5413-5420 ◽  
Author(s):  
Néstor Cortez ◽  
Néstor Carrillo ◽  
Cécile Pasternak ◽  
Angelika Balzer ◽  
Gabriele Klug
Keyword(s):  
Superoxide Dismutase ◽  
Rhodobacter Capsulatus ◽  
Sequence Similarity ◽  
Bacterial Species ◽  
Polyacrylamide Gel Electrophoresis ◽  
Selection Procedure ◽  
Cloning And Expression ◽  
Gene Encoding ◽  
Reading Frame ◽  
Species Activity

ABSTRACT Genetic complementation of a sodA sodB Escherichia colimutant strain was used to clone Rhodobacter capsulatusgenes involved in detoxification of superoxide radicals. After sequence analysis, 1 of the 16 identical clones obtained by this selection procedure was shown to contain an open reading frame with sequence similarity to that coding for Fe-containing superoxide dismutases (SodB). The R. capsulatus sodB gene was expressed inE. coli, and the nature of the metal ligand was confirmed by inhibitor sensitivity assays with lysates from both bacterial species. Activity staining of cleared Rhodobacter lysates resolved by polyacrylamide gel electrophoresis indicated that SodB was the only superoxide dismutase present in this phototrophic organism. The sodB gene was expressed at low levels in R. capsulatus cells grown under anaerobic or semiaerobic conditions, but expression was strongly induced upon exposure of the bacteria to air or to methyl viologen. Attempts to construct a sodBmutant in this organism by allelic exchange of the chromosomal copy of the gene with a suicide plasmid containing a mutated sodBgene were unsuccessful, strongly suggesting that the encoded superoxide dismutase is essential for viability of R. capsulatus in aerobic cultures.

scholarly journals Differential Expression of Three α-Galactosidase Genes and a Single β-Galactosidase Gene from Aspergillus niger

1999 ◽  
Vol 65 (6) ◽  
pp. 2453-2460 ◽  
Author(s):  
Ronald P. de Vries ◽  
Hetty C. van den Broeck ◽  
Ester Dekkers ◽  
Paloma Manzanares ◽  
Leo H. de Graaff ◽  
...  
Keyword(s):  
Amino Acids ◽  
Aspergillus Niger ◽  
Signal Sequence ◽  
Expression Patterns ◽  
Carbon Sources ◽  
Gene Encoding ◽  
Calculated Molecular Mass ◽  
Reading Frame ◽  
Polymeric Compounds ◽  
Elevated Expression

ABSTRACT A gene encoding a third α-galactosidase (AglB) fromAspergillus niger has been cloned and sequenced. The gene consists of an open reading frame of 1,750 bp containing six introns. The gene encodes a protein of 443 amino acids which contains a eukaryotic signal sequence of 16 amino acids and seven putative N-glycosylation sites. The mature protein has a calculated molecular mass of 48,835 Da and a predicted pI of 4.6. An alignment of the AglB amino acid sequence with those of other α-galactosidases revealed that it belongs to a subfamily of α-galactosidases that also includesA. niger AglA. A. niger AglC belongs to a different subfamily that consists mainly of prokaryotic α-galactosidases. The expression of aglA,aglB, aglC, and lacA, the latter of which encodes an A. niger β-galactosidase, has been studied by using a number of monomeric, oligomeric, and polymeric compounds as growth substrates. Expression of aglA is only detected on galactose and galactose-containing oligomers and polymers. The aglB gene is expressed on all of the carbon sources tested, including glucose. Elevated expression was observed on xylan, which could be assigned to regulation via XlnR, the xylanolytic transcriptional activator. Expression of aglC was only observed on glucose, fructose, and combinations of glucose with xylose and galactose. High expression of lacA was detected on arabinose, xylose, xylan, and pectin. Similar to aglB, the expression on xylose and xylan can be assigned to regulation via XlnR. All four genes have distinct expression patterns which seem to mirror the natural substrates of the encoded proteins.

scholarly journals Purification and Genetic Characterization of Enterocin I from Enterococcus faecium 6T1a, a Novel Antilisterial Plasmid-Encoded Bacteriocin Which Does Not Belong to the Pediocin Family of Bacteriocins

1998 ◽  
Vol 64 (12) ◽  
pp. 4883-4890 ◽  
Author(s):  
Belén Floriano ◽  
José L. Ruiz-Barba ◽  
Rufino Jiménez-Díaz
Keyword(s):  
Enterococcus Faecium ◽  
Pathogenic Bacteria ◽  
Specific Activity ◽  
Sequence Similarity ◽  
Fold Increase ◽  
Leader Peptide ◽  
Nucleotide Sequencing ◽  
Gene Encoding ◽  
Reading Frame ◽  
Fast Flow

ABSTRACT Enterocin I (ENTI) is a novel bacteriocin produced byEnterococcus faecium 6T1a, a strain originally isolated from a Spanish-style green olive fermentation. The bacteriocin is active against many olive spoilage and food-borne gram-positive pathogenic bacteria, including clostridia, propionibacteria, and Listeria monocytogenes. ENTI was purified to homogeneity by ammonium sulfate precipitation, binding to an SP-Sepharose fast-flow column, and phenyl-Sepharose CL-4B and C2/C18 reverse-phase chromatography. The purification procedure resulted in a final yield of 954% and a 170,000-fold increase in specific activity. The primary structure of ENTI was determined by amino acid and nucleotide sequencing. ENTI consists of 44 amino acids and does not show significant sequence similarity with any other previously described bacteriocin. Sequencing of the entI structural gene, which is located on the 23-kb plasmid pEF1 of E. faecium 6T1a, revealed the absence of a leader peptide at the N-terminal region of the gene product. A second open reading frame, ORF2, located downstream of entI, encodes a putative protein that is 72.7% identical to ENTI.entI and ORF2 appear to be cotranscribed, yielding an mRNA of ca. 0.35 kb. A gene encoding immunity to ENTI was not identified. However, curing experiments demonstrated that both enterocin production and immunity are conferred by pEF1.

scholarly journals Pengaruh Lama Peram Proses Fermentasi Kulit Kacang Tanah Amoniasi dengan Aspergillus niger terhadap Produksi VFA dan NH3 secara In vitro

2019 ◽  
Vol 17 (3) ◽  
pp. 69-72
Author(s):  
Ulfatul Laikha ◽  
Bim Tampubolon ◽  
A Subrata
Keyword(s):  
New York ◽  
Aspergillus Niger ◽  
Fermentation Process ◽  
Plant Cell Wall ◽  
Sprague Dawley ◽  
Cell Wall Polysaccharides ◽  
Fermentation Time ◽  
Randomized Design ◽  
Peanut Shells

The aim of this research was to examine the effect of fermentation time by Aspergillus niger on peanut shells ammoniated on VFA and NH3 production. The research was allocated in a completely randomized design with 4 treatments and 4 replications. The treatments  were fermentation process of 0 days (T0), 5 days (T1), 10 days (T2) and 15 days (T3). The results showed that fermentation process with A. niger on the ammoniated peanut shells increased (p<0.05) the VFA and NH3 production. In an incubation time of 15 days, the highest VFA and NH3 production waas obtained. The average production of VFA were T0=153; T1=188; T2=193 and T3=203 mM respectively. Average of NH3 production in this study were T0=2,89; T1=3,61; T2=3,74 dan T3=3,90 mM respectively. It was conclusded that the  fermentation process with A. niger on peanut shells ammoniated increased the VFA and NH3 production. The 15 days of fermentation process was the best time which produced the highest of  VFA and NH3 production. Key words:   Aspergillus niger, NH3, peanut shells, VFA DAFTAR PUSTAKA Badan Pusat Statistik. 2018. Provinsi Jawa Tengah dalam Angka. Semarang (ID): Badan Pusat Statistik Provinsi Jawa Tengah Basri E & Tambunan RD. 2016. Kajian pemanfaatan pakan berbasis bahan lokal yang berwawasan lingkungan untuk sapi potong di Lampung. Prosiding Seminar Nasional Inovasi Teknologi Pertanian Puslitbangtan. Banjar Baru (ID): Puslitbangtan Church DC& Pond WG. 1988. Basic Animal Nutrition and Feeding. 3rd edition. New York (US): John Wiley and Sons Danuarsa. 2006. Analisis proksimat dan asam lemak pada beberapa komunitas kacang-kacangan. Buletin Teknik Pertanian. 11(1): 1-9 DeVries &Visser J. 2001. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiology Molecular Biology Review. 65 (4): 497-522 Gunam IBWG, Buda K & Guna IMYS. 2010. Pengaruh perlakuan delignifikasi dengn larutan NaOH dan kosentrasi substrat jerami padi terhadap produksi enzim selulase dari Aspergillus niger. Jurnal Biologi. 15 (1): 55-61 Hastuti D, Shofia NA &. Tampoebolon BIM. 2010. Pengaruh perlakuan teknologi amofer (amoniasi fermentasi) pada hasil samping tongkol jagung sebagai alternative pakan berkualitas ternak ruminansia. Jurnal Mediagro. 7 (1): 55-65 Nurhaita, Definiati N & Suliasih. 2017. Pengolahan jerami padi sebagai pakan ternak sapi pada kelompok tani sido urip Desa Srikuncoro. Malang (ID): Prosiding Seminar Nasional dan Gelar Produk, UMM Prasetyo, H. 2014. Polimerisasi karet alam secara mekanis untuk bahan adiktif aspal. Jurnal Penelitian Karet. 32 (1): 81-87 Junior LKP, Swastini DA & Leliqia NPE. 2015. Pengaruh pemberian ekstrak etanol kulit kacang tanah dengan metode maserasi terhadap profil lipid pada tikus Sprague Dawley diet lemak tinggi. Jurnal Farmasi. 4 (1): 18-25 Komar, A. 1984. Teknologi Pengolahan Jerami sebagai Makanan Ternak. Bandung (ID): Yayasan Dian Grahita Indonesia Retnani Y, Permana IG, Kumalasari NR & Taryati. 2015. Teknik Membuat Biskuit Pakan Ternak dari Limbah Pertanian. Jakarta (ID): Penebar Swadaya Steel RGD & Torrie JH. 1991. Prinsip dan Prosedur Statistika. Terjemahan. Jakarta (ID): Gramedia Pustaka Utama, Jakart. Suhartati FM. 2005. Proteksi Protein Daun Lamtoro (Leucaena leucocephala) Menggunakan Tanin, Saponin, Minyak dan Pengaruhnya terhadap Ruminal Undegradable Protein (RUDP) dan Sintesis Protein Mikrobia Rumen. [skripsi] Purwokerto (ID): Fakultas Peternakan, Universitas Jenderal Soedirman Tillman, Harihartadi AD, Reksodiprojo S, Prawirokusumo S & Lebdosoekojo. 1998. Ilmu Makanan Ternak Dasar. Yogyakarta (ID): Gajah Mada University Press

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