13 results match your criteria Biotechnology And Bioprocess Engineering[Journal]

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Anti-cariogenic Characteristics of Rubusoside.

Biotechnol Bioprocess Eng 2019 18;24(2):282-287. Epub 2019 May 18.

1Graduate School of International Agricultural Technology and Institutes of Green Bioscience & Technology, Seoul National University, Seoul, Pyeongchang, 25354 Korea.

plays an important role in the development of dental caries in humans by synthesizing adhesive insoluble glucans from sucrose by mutansucrase activity. To explore the anti-cariogenic characteristics of rubusoside (Ru), a natural sweetener component in (Rosaceae), we investigated the inhibitory effect of Ru against the activity of mutansucrase and the growth of Ru (50 mM) showed 97% inhibitory activity against 0.1 U/mL mutansucrase of with 500 mM sucrose. Read More

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http://dx.doi.org/10.1007/s12257-018-0408-0DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090897PMC

Improvement in the Reproducibility of a Paper-based Analytical Device (PAD) Using Stable Covalent Binding between Proteins and Cellulose Paper.

Biotechnol Bioprocess Eng 2018 17;23(6):686-692. Epub 2019 Jan 17.

1Department of Chemical Engineering and Applied Chemistry, Chungnam National University, Seoul, Korea.

Paper-based analytical devices (PADs) have been widely used in many fields because they are affordable and portable. For reproducible quantitative analysis, it is crucial to strongly immobilize proteins on PADs. Conventional techniques for immobilizing proteins on PADs are based on physical adsorption, but proteins can be easily removed by weak physical forces. Read More

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http://dx.doi.org/10.1007/s12257-018-0430-2DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090440PMC
January 2019

A rapidly new-typed detection of norovirus based on FF-ATPase molecular motor biosensor.

Biotechnol Bioprocess Eng 2016 18;21(1):128-133. Epub 2016 Mar 18.

4Weifang people's hospital of high-tech industrial development zone, Weifang, 261-205 China.

In order to adapt port rapid detection of food borne norovirus, presently we developed a new typed detection method based on FF-ATPase molecular motor biosensor. A specific probe was encompassed the conservative region of norovirus and FF-ATPase within chromatophore was constructed as a molecular motor biosensor through the "ε-subunit antibody-streptomycin-biotin-probe" system. Norovirus was captured based on probe-RNA specific binding. Read More

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http://dx.doi.org/10.1007/s12257-015-0384-6DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7091097PMC

Temperature sensing using red fluorescent protein.

Biotechnol Bioprocess Eng 2015 18;20(1):67-72. Epub 2015 Mar 18.

2Department of Bioscience and Biotechnology, Konkuk University, Seoul, 143-701 Korea.

Genetically encoded fluorescent proteins are extensively utilized for labeling and imaging proteins, organelles, cell tissues, and whole organisms. In this study, we explored the feasibility of mRFP1 and its variants for measuring intracellular temperature. A linear relationship was observed between the temperature and fluorescence intensity of mRFP1 and its variants. Read More

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http://dx.doi.org/10.1007/s12257-014-0456-zDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090752PMC

Inhibition effect of flavonoid compounds against neuraminidase expressed in .

Biotechnol Bioprocess Eng 2014 11;19(1):70-75. Epub 2014 Mar 11.

1Department of Biotechnology and Bioengineering, and Research Institute for Catalysis, College of Engineering, Chonnam National University, Gwangju, 500-757 Korea.

Neuraminidase (NA) is one of the two glycoproteins on the surface of influenza virus, which cleaves terminal sialic acid residues and facilitates the release of virions from infected cells. The recombinant NA from H5N1 influenza virus strain A/Vietnam/1203/04 was expressed in X33 as a 45 kDa protein that displayed a of 9.96 ± 1. Read More

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http://dx.doi.org/10.1007/s12257-013-0599-3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7091146PMC

Recent development of highly sensitive protease assay methods: Signal amplification through enzyme cascades.

Biotechnol Bioprocess Eng 2012 4;17(6):1113-1119. Epub 2013 Jan 4.

1Department of Molecular Science and Technology, Ajou University, Suwon, 443-749 Korea.

Proteases are involved in almost all biological processes, and therefore, aberrant activity of many of these enzymes is an important indicator of disease. Various methods have been developed to analyze protease activity, among which, protease assays based on resonance energy transfer are currently used most widely. However, quantitative methods with relatively higher sensitivity are needed, especially for disease diagnosis at early stages. Read More

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http://dx.doi.org/10.1007/s12257-012-0545-9DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090753PMC
January 2013

Inhibitory effects of epigallocatechin gallate and its glucoside on the human intestinal maltase inhibition.

Biotechnol Bioprocess Eng 2012 24;17(5):966-971. Epub 2012 Oct 24.

1School of Biological Sciences and Technology and Research Institute for Catalysis, Chonnam National University, Gwangju, 500-757 Korea.

Human intestinal maltase (HMA) is an α-glucosidase responsible for the hydrolysis of α-1,4-linkages from the non-reducing end of malto-oligosaccharides. HMA has become an important target in the treatment of type-2 diabetes. In this study, epigallocatechin gallate (EGCG) and EGCG glucoside (EGCG-G1) were identified as inhibitors of HMA by an assay with IC of 20 ± 1. Read More

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http://dx.doi.org/10.1007/s12257-012-0242-8DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7091073PMC
October 2012

Iso-migrastatin Titer Improvement in the Engineered Streptomyces lividans SB11002 Strain by Optimization of Fermentation Conditions.

Biotechnol Bioprocess Eng 2010 Aug;15(4):664-669

Institute of Biochemistry, Zhejiang Sci-Tech University, Hangzhou 310-018, China.

The heterologous production of iso-migrastatin (iso-MGS) was successfully demonstrated in an engineered S. lividans SB11002 strain, which was derived from S. lividans K4-114, following introduction of pBS11001, which harbored the entire mgs biosynthetic gene cluster. Read More

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http://dx.doi.org/10.1007/s12257-009-3129-6DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3100776PMC
August 2010
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Production of a heat-labile enterotoxin B subunit-porcine epidemic diarrhea virus-neutralizing epitope fusion protein in transgenic lettuce ().

Biotechnol Bioprocess Eng 2009 14;14(6):731-737. Epub 2010 Jan 14.

Division of Biological Sciences and the Research Center for Bioactive Materials, Chonbuk National University, Jeonju, 561-756 Korea.

Plant-based vaccines have been produced in transgenic plants including tobacco, potatoes, corn, and rice. However, these plants are not suitable for administration without cooking. To overcome this obstacle, a fusion gene encoding the synthetic enterotoxigenic heat-labile enterotoxin B subunit genetically fused with a synthetic neutralizing epitope of porcine epidemic diarrhea virus (sLTB-sCOE) was introduced into lettuce cells () by -mediated transformation methods. Read More

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http://dx.doi.org/10.1007/s12257-009-3012-5DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7091058PMC
January 2010

Simultaneous extraction and separation of liquiritin, glycyrrhizic acid, and glabridin from licorice root with analytical and preparative chromatography.

Biotechnol Bioprocess Eng 2008 3;13(6):671-676. Epub 2009 Feb 3.

Center for Advanced Bioseparation Technology, Department of Chemical Engineering, Inha University, Incheon, 402-751 Korea.

Simultaneous extraction and separation of liquiritin, glycyrrhizic acid, and glabridin from licorice were developed by liquidliquid extraction with liquid chromatography separation. By utilizing different extraction solvents, procedures, and times, the optimum extraction conditions were established. The extracts of licorice were separated and determined using a C column with a mobile phase consisting of acetonitrile-water (containing 1. Read More

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http://dx.doi.org/10.1007/s12257-008-0019-2DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090988PMC
February 2009

Surface displayed expression of a neutralizing epitope of spike protein from a Korean strain of porcine epidemic diarrhea virus.

Biotechnol Bioprocess Eng 2007 ;12(6):690-695

1Institute for Molecular Biology and Genetics, Research Center of Bioactive Materials, Chonbuk National University, 561-756 Jeonju, Korea.

The neutralizing epitope (K-COE) of the spike protein from a Korean strain of porcine epidemic diarrhea virus (PEDV) has been shown to prevent and foster an immune response to PED, when orally adjusted. The cell surface of the budding yeast,, was engineered to anchor the K-COE on the outer layer of the cell, and consequently, the altered yeast was applied as a dietary complement for animal feed, with immunogenic functions. In this study, the K-COE gene () of the Korean strain of PEDV with the signal peptide of rice amylase 1A (), was fused with the gene encoding the carboxyterminal half (320 amino acid residues from the C terminus) of yeast α-agglutinin, a mating associated protein that is anchored covalently to the cell wall. Read More

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http://dx.doi.org/10.1007/BF02931087DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090475PMC
January 2007

Engineering blood cells and proteins as blood substitutes: A short review.

Authors:
Hae Won Kim

Biotechnol Bioprocess Eng 2007 ;12(1):43

1Brown University Medical School and The Miriam Hospital, 164 Summit Avenue, 02906 Providence, Rhode Island USA.

In this brief review, basic principles and recent progresses on the development of therapeutic substitutes for major blood components are briefly discussed with primary focus on the red cell substitutes. Read More

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http://dx.doi.org/10.1007/BF02931802DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090951PMC
January 2007

Polyhydroxyalkanoate chip for the specific immobilization of recombinant proteins and its applications in immunodiagnostics.

Biotechnol Bioprocess Eng 2006 ;11(2):173

1Department of Chemical and Biomolecular Engineering, Bioprocess Engineering Research Center, Center for Ultramicrochemical Process Systems, Korea Advanced Institute of Science and Technology, 305-701 Daejeon, Korea.

In this study, a novel strategy was developed for the highly selective immobilization of proteins, using the polyhydroxyalkanoate (PHA) depolymerase substrate binding domain (SBD) as an active binding domain. In order to determine the appropriacy of this method for immunodiagnostic assays, the single-chain antibody (ScFv) against the hepatitis B virus (HBV) preS2 surface protein and the severe acute respiratory syndrome coronavirus (SARS-CoV) envelope protein (SCVe) were fused to the SBD, then directly immobilized on PHA-coated slides via microspotting. The fluorescence-labeled HBV antigen and the antibody against SCVe were then utilized to examine specific interactions on the PHA-coated surfaces. Read More

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http://dx.doi.org/10.1007/BF02931904DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090861PMC
January 2006
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