scholarly journals Heterologous, Expression, and Characterization of Thermostable Glucoamylase Derived fromAspergillus flavusNSH9 inPichia pastoris

2016 ◽  
Vol 2016 ◽  
pp. 1-10 ◽  
Author(s):  
Kazi Muhammad Rezaul Karim ◽  
Ahmad Husaini ◽  
Md. Anowar Hossain ◽  
Ngieng Ngui Sing ◽  
Fazia Mohd Sinang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Pichia Pastoris ◽  
Aspergillus Flavus ◽  
Residual Activity ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Higher Temperature ◽  
Positive Effect

A novel thermostable glucoamylase cDNA without starch binding domain (SBD) ofAspergillus flavusNSH9 was successfully identified, isolated, and overexpressed inPichia pastorisGS115. The complete open reading frame of glucoamylase fromAspergillus flavusNSH9 was identified by employing PCR that encodes 493 amino acids lacking in the SBD. The first 17 amino acids were presumed to be a signal peptide. The cDNA was cloned intoPichia pastorisand the highest expression of recombinant glucoamylase (rGA) was observed after 8 days of incubation period with 1% methanol. The molecular weight of the purified rGA was about 78 kDa and exhibited optimum catalytic activity at pH 5.0 and temperature of 70°C. The enzyme was stable at higher temperature with 50% of residual activity observed after 20 min at 90°C and 100°C. Low concentration of metal (Mg++, Fe++, Zn++, Cu++, and Pb++) had positive effect on rGA activity. This rGA has the potential for use and application in the saccharification steps, due to its thermostability, in the starch processing industries.

Characterization of an atypical antigen from Sarcoptes scabiei containing an MADF domain

Parasitology ◽  
2005 ◽  
Vol 132 (1) ◽  
pp. 117-126 ◽  
Author(s):  
E. L. LJUNGGREN ◽  
K. BERGSTRÖM ◽  
D. A. MORRISON ◽  
J. G. MATTSSON
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Sequence Analysis ◽  
Sarcoptes Scabiei ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Sequence Complexity ◽  
N Terminus ◽  
Inside Wall

We have cloned a cDNA encoding a novel antigen from a Sarcoptes scabiei (Acari) cDNA library by immunoscreening with sera from S. scabiei-infected dogs. The antigen is encoded by a 2157 bp mRNA with a predicted open reading frame of 719 amino acids (molecular weight 79 kDa). Our sequence analysis identified the presence of a MADF domain in the N-terminus, and downstream of this domain there was a region of low sequence complexity. This latter region contained several blocks of triplets and quadruplets of polar amino acids (Asn, Gln and Ser), and these 3 amino acids represented 39·7% of all amino acids. The antigen was named Atypical Sarcoptes Antigen 1 (ASA1) since the MADF domain normally is found in proteins involved in transcriptional regulation. In addition, 15 out of 62 S. scabiei-infected dogs reacted with a purified recombinant version of ASA1 in Western blot analysis. With immunohistochemistry we could show that ASA1 is expressed throughout the parasite, and that IgG specific for ASA1 binds to the inside wall of the mite's burrow. To our knowledge, this is the first description of an antigen containing an MADF domain.

scholarly journals Cloning, Nucleotide Sequence, and Expression of the Gene Encoding the Bacteriocin Boticin B from Clostridium botulinum Strain 213B

2000 ◽  
Vol 66 (12) ◽  
pp. 5480-5483 ◽  
Author(s):  
Sean S. Dineen ◽  
Marite Bradshaw ◽  
Eric A. Johnson
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Clostridium Botulinum ◽  
Shuttle Vector ◽  
Open Reading Frame ◽  
Gene Encoding ◽  
Reading Frame ◽  
Heat Stable ◽  
Group I

ABSTRACT Boticin B is a heat-stable bacteriocin produced byClostridium botulinum strain 213B that has inhibitory activity against various strains of C. botulinum and related clostridia. The gene encoding the bacteriocin was localized to a 3.0-kb HindIII fragment of an 18.8-kb plasmid, cloned, and sequenced. DNA sequencing revealed the boticin B structural gene,btcB, to be an open reading frame encoding 50 amino acids. A C. botulinum strain 62A transconjugant containing theHindIII fragment inserted into a clostridial shuttle vector expressed boticin B, although at much lower levels than those observed in C. botulinum 213B. To our knowledge, this is the first demonstration and characterization of a bacteriocin from toxigenic group I C. botulinum.

scholarly journals Genomic Characterization of an Echovirus 7 Isolate of Southeast Asian Ancestry Recovered from a Child in Nigeria with Acute Flaccid Paralysis

2019 ◽  
Vol 8 (33) ◽  
Author(s):  
T. O. C. Faleye ◽  
O. M. Adewumi ◽  
J. A. Adeniji
Keyword(s):  
Amino Acids ◽  
Acute Flaccid Paralysis ◽  
Southeast Asian ◽  
Open Reading Frame ◽  
Flaccid Paralysis ◽  
Reading Frame ◽  
Asian Ancestry ◽  
Genomic Characterization

Here, we describe the genome of an echovirus 7 (E7) isolate of Southeast Asian ancestry recovered from a child in Nigeria with acute flaccid paralysis (AFP). The genome has 7,295 nucleotides (nt) and an open reading frame (ORF) with 2,195 amino acids.

scholarly journals Characterization of the ToxB Gene from Pyrenophora tritici-repentis

2001 ◽  
Vol 14 (5) ◽  
pp. 675-677 ◽  
Author(s):  
J. Patrick Martinez ◽  
Sean A. Ottum ◽  
Shaukat Ali ◽  
Leonard J. Francl ◽  
Lynda M. Ciuffetti
Keyword(s):  
Amino Acid ◽  
Pichia Pastoris ◽  
Heterologous Expression ◽  
North Dakota ◽  
Signal Peptide ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Pyrenophora Tritici Repentis ◽  
Putative Signal Peptide

The ToxB gene was cloned and characterized from a race 5 isolate of Pyrenophora tritici-repentis from North Dakota. ToxB contains a 261-bp open reading frame that encodes a 23 amino acid putative signal peptide and a 64 amino acid host-selective toxin, Ptr ToxB. Analysis of Ptr ToxB from heterologous expression in Pichia pastoris confirms that ToxB encodes a host-selective toxin.

scholarly journals Sequence of the Structural Gene for Xanthine Dehydrogenase (rosy Locus) in Drosophila melanogaster

Genetics ◽  
1987 ◽  
Vol 116 (1) ◽  
pp. 67-73
Author(s):  
Tim P Keith ◽  
Margaret A Riley ◽  
Martin Kreitman ◽  
R C Lewontin ◽  
Daniel Curtis ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Structural Gene ◽  
Xanthine Dehydrogenase ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Eco Ri

ABSTRACT We determined the nucleotide sequence of a 4.6-kb Eco RI fragment containing 70% of the rosy locus. In combination with information on the 5′ sequence, the gene has been sequenced in entirety. rosy cDNAs have been isolated and intron/exon boundaries have been determined. We find an open reading frame which spans four exons and would encode a protein of 1335 amino acids. The molecular weight of the encoded protein (xanthine dehydrogenase), based on the amino acid translation, is 146,898 daltons which agrees well with earlier biophysical estimates. Characteristics of the protein are discussed.

Cloning and Characterization of Two Pyruvate Decarboxylase Genes from Pichia stipitis CBS 6054

1998 ◽  
Vol 64 (1) ◽  
pp. 94-97 ◽  
Author(s):  
Ping Lu ◽  
Brian P. Davis ◽  
Thomas W. Jeffries
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Pyruvate Decarboxylase ◽  
Pichia Stipitis ◽  
Open Reading Frame ◽  
Fermentable Sugars ◽  
Yeast Gene ◽  
Reading Frame ◽  
Hanseniaspora Uvarum

ABSTRACT In Pichia stipitis, fermentative and pyruvate decarboxylase (PDC) activities increase with diminished oxygen rather than in response to fermentable sugars. To better characterizePDC expression and regulation, two genes for PDC (PsPDC1 and PsPDC2) were cloned and sequenced from P. stipitis CBS 6054. Aside from Saccharomyces cerevisiae, from which three PDC genes have been characterized,P. stipitis is the only organism from which multiple genes for PDC have been identified and characterized. PsPDC1 andPsPDC2 have diverged almost as far from one another as they have from the next most closely related known yeast gene.PsPDC1 contains an open reading frame of 1,791 nucleotides encoding 597 amino acids. PsPDC2 contains a reading frame of 1,710 nucleotides encoding 570 amino acids. An 81-nucleotide segment in the middle of the β domain of PsPDC1 codes for a unique segment of 27 amino acids, which may play a role in allosteric regulation. The 5′ regions of both P. stipitis genes include two putative TATA elements that make them similar to the PDC genes from S. cerevisiae, Kluyveromyces marxianus, and Hanseniaspora uvarum.

scholarly journals Genomic Characterization of an Echovirus 7 Isolate of South-East Asian Ancestry Recovered from a Child with AFP in Nigeria

2018 ◽  
Author(s):  
Temitope Faleye ◽  
Moses Olubusuyi Adewumi ◽  
Johnson Adekunle Adeniji
Keyword(s):  
Amino Acids ◽  
Acute Flaccid Paralysis ◽  
East Asian ◽  
Open Reading Frame ◽  
Flaccid Paralysis ◽  
Reading Frame ◽  
Asian Ancestry ◽  
Genomic Characterization ◽  
East Asian Ancestry

Here we describe the genome of an Echovirus 7 isolate of South-East Asian ancestry recovered from a child with acute flaccid paralysis (AFP) in Nigeria. The genome has 7,295nt and an open reading frame with 2,195 amino acids.

CHARACTERIZATION OF THE WHEAT cDNA ENCODING THE β SUBUNIT OF THE MITOCHONDRIAL ATP SYNTHASE

1996 ◽  
Vol 44 (2-3) ◽  
pp. 77-88 ◽  
Author(s):  
Suzy Abulafia ◽  
Dan Graur ◽  
Katrien Devos ◽  
Adina Breiman
Keyword(s):  
Amino Acids ◽  
Phylogenetic Analysis ◽  
Amino Acid ◽  
Open Reading Frame ◽  
Β Subunit ◽  
Reading Frame ◽  
Mitochondrial Atp Synthase ◽  
Group 1 Chromosomes ◽  
Group 1

A wheat cDNA encoding an open reading frame of 553 amino acids with a deduced amino acid sequence corresponding to the mitochondrial β subunit of the synthase was isolated. The expression of the β ATPase was investigated in leaves of 7-day-old wheat plants, and a decrease in the abundance of transcripts along the leaf was observed. The cDNA of the β ATPase was mapped on the group 1 chromosomes of wheat. Phylogenetic analysis of the mitochondrial β subunit of the ATPase complex is described.

scholarly journals Characterization of the plasmidic beta-lactamase CMY-2, which is responsible for cephamycin resistance.

1996 ◽  
Vol 40 (1) ◽  
pp. 221-224 ◽  
Author(s):  
A Bauernfeind ◽  
I Stemplinger ◽  
R Jungwirth ◽  
H Giamarellou
Keyword(s):  
Amino Acids ◽  
Klebsiella Pneumoniae ◽  
Open Reading Frame ◽  
Its Sequence ◽  
Citrobacter Freundii ◽  
Beta Lactamase ◽  
Reading Frame ◽  
Class C

The phenotype of Klebsiella pneumoniae HEL-1 indicates a plasmidic cephamycinase gene (blaCMY-2). Its sequence shows one open reading frame coding for a protein of 381 amino acids. CMY-2 is classified as class C beta-lactamase that is closely related to the plasmidic enzymes BIL-1 and LAT-1 and the chromosomal AmpC of Citrobacter freundii. The blaCMY-2 gene possibly was translocated onto a plasmid of C. freundii which spread to K. pneumoniae.

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