In this study, the Box-Behnken experimental planning was used to optimize the extraction of polysaccharides from the cell wall of Rhizopus microspore var. oligosporus, with analysis of the quantitative effects of parameters pH, temperature and extraction time for polysaccharide yield. The optimal conditions for extraction were determined by the regression equation and evaluation of the response surface graphs, which indicated: pH 13, temperature of 120ºC and time of 60 min, with maximum yield around 18.5%. Fourier transform infrared spectroscopy analysis indicated typical polysaccharide signals. Nuclear magnetic resonance spectroscopy and monosaccharide analysis indicated a β(1,3) β(1,6) glucogalactan. The polysaccharide exhibited an average molecular weight of 120 kDa and a polymerization degree of 741. Antioxidant assays in vitro revealed the potential of polysaccharide in elimination of ABTS+ radical and hydroxyl radicals. EC50 values for free radical elimination were 7.69 and 17.8 mg/mL, for ABTS+ and hydroxyls, respectively. The polysaccharides showed potential for α-amylase inhibition with an EC50 of 1.66 mg/mL. The results suggest that β(1,3) β(1,6) glucogalactan from Rhizopus microsporus var. oligosporus can be used in biotechnological applications.
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http://dx.doi.org/10.1590/0001-3765202420230073 | DOI Listing |
Microbiol Resour Announc
January 2020
Department of Life Science and Biotechnology, Bioproduction Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki, Japan
We isolated strains AA2-13 and AA3-38 from Arima Onsen, a hot spring in Japan, and sequenced their genomes. The average nucleotide identity between their genomes was 99.2%, and that with the genome of strain DSM 4252 (isolated from Iceland) was ∼95.
View Article and Find Full Text PDFSheng Wu Gong Cheng Xue Bao
March 2009
National Diagnostic Center for Exotic Animal Diseases, China Animal Health and Epidemiology Center, Qingdao 266032, China.
Binding sites of five monoclonal antibodies were obtained by reinforceable method of overlapping recombinant prion protein and synthetic peptide. Overlapping peptides of PrP core were expressed in Escherichia coli by insertion of serial PCR amplicons of ovine PrP gene fragments into pET32a. The expressed fusion peptides were then tested for the binding activity to PrP monoclonal antibodies in Western blotting.
View Article and Find Full Text PDFJ Gastroenterol
August 1998
Fourth Department of Internal Medicine, Teikyo University School of Medicine, Kawasaki, Japan.
Anti-liver-kidney microsome-1 (LKM-1), which reacts with cytochrome P450 IID6 (CYP2D6), is an autoantibody present in autoimmune hepatitis type II, which affects primarily young patients. Recently, it has been shown some adult patients with chronic hepatitis C are also positive for anti-LKM-1. Thus, anti-LKM-1-positive patients can be classified into two subgroups: (1) those with autoimmune hepatitis type II and (2) those with chronic hepatitis C.
View Article and Find Full Text PDFFEMS Microbiol Lett
July 1996
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
This study showed that the antigenicity of a malarial epitope increased with the length of the epitope when inserted at positions aa26 (amino acid position 26) and aa196, but not at aa213, of the Pseudomonas aeruginosa major outer membrane protein OprF (326 amino acids). Immunization studies showed that a 19-aa epitope was significantly more immunogenic than a 7-aa epitope when inserted at aa26 of OprF, while neither an 11- nor a 19-aa epitope fused to the C-terminus of glutathione S-transferase was immunogenic.
View Article and Find Full Text PDFGene
May 1995
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
OprF, the major outer membrane (OM) protein of Pseudomonas aeruginosa, has been proposed to be comprised of a series of beta-strands separated by periplasmic or surface-exposed loop regions. In this study, a simple malarial epitope was used to demonstrate that OprF can be used as an expression vector to present foreign peptide sequences, namely, the 4-amino-acid (aa) repeating epitope (Asn-Ala-Asn-Pro = NANP) of the circumsporozoite protein of the human malarial parasite Plasmodium falciparum. Eight permissive sites, that allowed the expression and surface exposure of the malarial epitope, were identified throughout OprF.
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