Of Pseudomonas Aeruginosa Mccb 123 and Their Applications
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Microbial Enzymes and Their Applications in Industries and Medicine
BioMed Research International Microbial Enzymes and Their Applications in Industries and Medicine Guest Editors: Periasamy Anbu, Subash C. B. Gopinath, Arzu Coleri Cihan, and Bidur Prasad Chaulagain Microbial Enzymes and Their Applications in Industries and Medicine BioMed Research International Microbial Enzymes and Their Applications in Industries and Medicine Guest Editors: Periasamy Anbu, Subash C. B. Gopinath, Arzu Coleri Cihan, and Bidur Prasad Chaulagain Copyright © 2013 Hindawi Publishing Corporation. All rights reserved. This is a special issue published in “BioMed Research International.” All articles are open access articles distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Contents Microbial Enzymes and Their Applications in Industries and Medicine,PeriasamyAnbu, Subash C. B. Gopinath, Arzu Coleri Cihan, and Bidur Prasad Chaulagain Volume 2013, Article ID 204014, 2 pages Effect of C/N Ratio and Media Optimization through Response Surface Methodology on Simultaneous Productions of Intra- and Extracellular Inulinase and Invertase from Aspergillus niger ATCC 20611, Mojdeh Dinarvand, Malahat Rezaee, Malihe Masomian, Seyed Davoud Jazayeri, Mohsen Zareian, Sahar Abbasi, and Arbakariya B. Ariff Volume 2013, Article ID 508968, 13 pages A Broader View: Microbial Enzymes and Their Relevance in Industries, Medicine, and Beyond, Neelam Gurung, Sumanta Ray, Sutapa Bose, and Vivek Rai Volume 2013, Article -
Amyloid-Degrading Ability of Nattokinase from Bacillus Subtilis Natto
J. Agric. Food Chem. 2009, 57, 503–508 503 Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto †,‡ § § † RUEI-LIN HSU, KUNG-TA LEE, JUNG-HAO WANG, LILY Y.-L. LEE, AND ,†,‡ RITA P.-Y. CHEN* Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan, R. O. C., Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan, R. O. C., and Department of Biochemical Science and Technology, National Taiwan University, Taipei 106, Taiwan, R. O. C. More than 20 unrelated proteins can form amyloid fibrils in vivo which are related to various diseases, such as Alzheimer’s disease, prion disease, and systematic amyloidosis. Amyloid fibrils are an ordered protein aggregate with a lamellar cross- structure. Enhancing amyloid clearance is one of the targets of the therapy of these amyloid-related diseases. Although there is debate on whether the toxicity is due to amyloids or their precursors, research on the degradation of amyloids may help prevent or alleviate these diseases. In this study, we explored the amyloid-degrading ability of nattokinase, a fibrinolytic subtilisin-like serine protease, and determined the optimal conditions for amyloid hydrolysis. This ability is shared by proteinase K and subtilisin Carlsberg, but not by trypsin or plasmin. KEYWORDS: Nattokinase; amyloid; natto; subtilisin NAT; amyloid degradation; fibril; amyloidosis INTRODUCTION of cardiovascular disease. Dietary supplementation with natto Natto, a fermented food made from boiled soybeans, has suppresses the intimal thickening of arteries and leads to the been eaten for more than 1000 years in Asia. The fermenta- lysis of mural thrombi seen after endothelial injury (12). tion microbe isolated from natto is the Gram-positive Other clinically thrombolytic agents, such as urokinase and endospore-forming bacterium Bacillus subtilis natto (formerly streptokinase, are costly and unstable in the intestinal tract designated Bacillus natto)(1). -
Identification and Phylogenetic Analysis of Keratinase Producing Bacteria SNP1 from Poultry Field
International Journal of Biotechnology and Biochemistry ISSN 0973-2691 Volume 15, Number 1 (2019) pp. 39-51 © Research India Publications http://www.ripublication.com Identification and Phylogenetic Analysis of Keratinase Producing Bacteria SNP1 from Poultry Field Divya Balakrishnan and Nithadas Sathyadas Padmanabhan Department of Biotechnology, Sree Narayana College, Kollam-691001, Kerala, India. (*Corresponding author) Abstract The study was conduct to select the best promising keratinolytic bacterial strain. A keratinase positive bacterial strain was isolated from the soil samples of poultry field, Attingal, Thiruvananthapuram. Each sample was plated on skim milk agar and feather meal agar plates containing 5 g feather. The well grown isolates which produced the largest clear zone on skimmed milk plate were selected for keratinase assays. Out of 26 bacterial isolates, 7 isolates were selected. Among the selected strain, the best keratinase producing bacterium SNP1was selected for further analysis. The SNP1 potential strain was later confirmed as Bacillus haynessi based on molecular and phylogenetic analysis. The medium components and culture conditions were optimized to enhance keratinase production through optimization. Keratin and feather powder (10g/l) were identified as good substrates for the highest keratinase production. The strain SNP1 resulted maximum enzyme production at 96h of incubation at 37°C and pH 8 under 120 rpm. Therefore, Bacillus hayneisi might be used for large scale production of keratinase for industrial purposes. Keywords: Keratinase, Bacillus sp., Optimization, Enzyme activity, 16SrRNA Keratin is a hard-degrading fibrous and recalcitrant structural protein, which forms the third most abundant polymer in nature after cellulose and chitin (Lene et al ., 2016). In the native state, the feather keratin resists the degradation by proteolytic enzymes such as trypsin and pepsin due to tightpeptide-chains held together by disulfide bridges by means of cysteine residues (Weeranut, 2017; Korniłłowicz-Kowalska and Bohacz, 2011). -
The Role of Streptococcal and Staphylococcal Exotoxins and Proteases in Human Necrotizing Soft Tissue Infections
toxins Review The Role of Streptococcal and Staphylococcal Exotoxins and Proteases in Human Necrotizing Soft Tissue Infections Patience Shumba 1, Srikanth Mairpady Shambat 2 and Nikolai Siemens 1,* 1 Center for Functional Genomics of Microbes, Department of Molecular Genetics and Infection Biology, University of Greifswald, D-17489 Greifswald, Germany; [email protected] 2 Division of Infectious Diseases and Hospital Epidemiology, University Hospital Zurich, University of Zurich, CH-8091 Zurich, Switzerland; [email protected] * Correspondence: [email protected]; Tel.: +49-3834-420-5711 Received: 20 May 2019; Accepted: 10 June 2019; Published: 11 June 2019 Abstract: Necrotizing soft tissue infections (NSTIs) are critical clinical conditions characterized by extensive necrosis of any layer of the soft tissue and systemic toxicity. Group A streptococci (GAS) and Staphylococcus aureus are two major pathogens associated with monomicrobial NSTIs. In the tissue environment, both Gram-positive bacteria secrete a variety of molecules, including pore-forming exotoxins, superantigens, and proteases with cytolytic and immunomodulatory functions. The present review summarizes the current knowledge about streptococcal and staphylococcal toxins in NSTIs with a special focus on their contribution to disease progression, tissue pathology, and immune evasion strategies. Keywords: Streptococcus pyogenes; group A streptococcus; Staphylococcus aureus; skin infections; necrotizing soft tissue infections; pore-forming toxins; superantigens; immunomodulatory proteases; immune responses Key Contribution: Group A streptococcal and Staphylococcus aureus toxins manipulate host physiological and immunological responses to promote disease severity and progression. 1. Introduction Necrotizing soft tissue infections (NSTIs) are rare and represent a more severe rapidly progressing form of soft tissue infections that account for significant morbidity and mortality [1]. -
(12) United States Patent (10) Patent No.: US 6,395,889 B1 Robison (45) Date of Patent: May 28, 2002
USOO6395889B1 (12) United States Patent (10) Patent No.: US 6,395,889 B1 Robison (45) Date of Patent: May 28, 2002 (54) NUCLEIC ACID MOLECULES ENCODING WO WO-98/56804 A1 * 12/1998 ........... CO7H/21/02 HUMAN PROTEASE HOMOLOGS WO WO-99/0785.0 A1 * 2/1999 ... C12N/15/12 WO WO-99/37660 A1 * 7/1999 ........... CO7H/21/04 (75) Inventor: fish E. Robison, Wilmington, MA OTHER PUBLICATIONS Vazquez, F., et al., 1999, “METH-1, a human ortholog of (73) Assignee: Millennium Pharmaceuticals, Inc., ADAMTS-1, and METH-2 are members of a new family of Cambridge, MA (US) proteins with angio-inhibitory activity', The Journal of c: - 0 Biological Chemistry, vol. 274, No. 33, pp. 23349–23357.* (*) Notice: Subject to any disclaimer, the term of this Descriptors of Protease Classes in Prosite and Pfam Data patent is extended or adjusted under 35 bases. U.S.C. 154(b) by 0 days. * cited by examiner (21) Appl. No.: 09/392, 184 Primary Examiner Ponnathapu Achutamurthy (22) Filed: Sep. 9, 1999 ASSistant Examiner William W. Moore (51) Int. Cl." C12N 15/57; C12N 15/12; (74) Attorney, Agent, or Firm-Alston & Bird LLP C12N 9/64; C12N 15/79 (57) ABSTRACT (52) U.S. Cl. .................... 536/23.2; 536/23.5; 435/69.1; 435/252.3; 435/320.1 The invention relates to polynucleotides encoding newly (58) Field of Search ............................... 536,232,235. identified protease homologs. The invention also relates to 435/6, 226, 69.1, 252.3 the proteases. The invention further relates to methods using s s s/ - - -us the protease polypeptides and polynucleotides as a target for (56) References Cited diagnosis and treatment in protease-mediated disorders. -
Structure of Human Aspartyl Aminopeptidase Complexed With
Chaikuad et al. BMC Structural Biology 2012, 12:14 http://www.biomedcentral.com/1472-6807/12/14 RESEARCH ARTICLE Open Access Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family Apirat Chaikuad1, Ewa S Pilka1, Antonio De Riso2, Frank von Delft1, Kathryn L Kavanagh1, Catherine Vénien-Bryan2, Udo Oppermann1,3 and Wyatt W Yue1* Abstract Backround: Aspartyl aminopeptidase (DNPEP), with specificity towards an acidic amino acid at the N-terminus, is the only mammalian member among the poorly understood M18 peptidases. DNPEP has implicated roles in protein and peptide metabolism, as well as the renin-angiotensin system in blood pressure regulation. Despite previous enzyme and substrate characterization, structural details of DNPEP regarding ligand recognition and catalytic mechanism remain to be delineated. Results: The crystal structure of human DNPEP complexed with zinc and a substrate analogue aspartate-β- hydroxamate reveals a dodecameric machinery built by domain-swapped dimers, in agreement with electron microscopy data. A structural comparison with bacterial homologues identifies unifying catalytic features among the poorly understood M18 enzymes. The bound ligands in the active site also reveal the coordination mode of the binuclear zinc centre and a substrate specificity pocket for acidic amino acids. Conclusions: The DNPEP structure provides a molecular framework to understand its catalysis that is mediated by active site loop swapping, a mechanism likely adopted in other M18 and M42 metallopeptidases that form dodecameric complexes as a self-compartmentalization strategy. Small differences in the substrate binding pocket such as shape and positive charges, the latter conferred by a basic lysine residue, further provide the key to distinguishing substrate preference. -
Molecular Markers of Serine Protease Evolution
The EMBO Journal Vol. 20 No. 12 pp. 3036±3045, 2001 Molecular markers of serine protease evolution Maxwell M.Krem and Enrico Di Cera1 ment and specialization of the catalytic architecture should correspond to signi®cant evolutionary transitions in the Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Box 8231, St Louis, history of protease clans. Evolutionary markers encoun- MO 63110-1093, USA tered in the sequences contributing to the catalytic apparatus would thus give an account of the history of 1Corresponding author e-mail: [email protected] an enzyme family or clan and provide for comparative analysis with other families and clans. Therefore, the use The evolutionary history of serine proteases can be of sequence markers associated with active site structure accounted for by highly conserved amino acids that generates a model for protease evolution with broad form crucial structural and chemical elements of applicability and potential for extension to other classes of the catalytic apparatus. These residues display non- enzymes. random dichotomies in either amino acid choice or The ®rst report of a sequence marker associated with serine codon usage and serve as discrete markers for active site chemistry was the observation that both AGY tracking changes in the active site environment and and TCN codons were used to encode active site serines in supporting structures. These markers categorize a variety of enzyme families (Brenner, 1988). Since serine proteases of the chymotrypsin-like, subtilisin- AGY®TCN interconversion is an uncommon event, it like and a/b-hydrolase fold clans according to phylo- was reasoned that enzymes within the same family genetic lineages, and indicate the relative ages and utilizing different active site codons belonged to different order of appearance of those lineages. -
Human LDLR / LDL Receptor Protein (His Tag)
Human LDLR / LDL Receptor Protein (His Tag) Catalog Number: 10231-H08H General Information SDS-PAGE: Gene Name Synonym: FH; FHC; LDL R; LDL Receptor; LDLCQ2 Protein Construction: A DNA sequence encoding the extracellular domain of human LDLR (NP_000518.1) precursor (Met 1-Arg 788) was expressed with a C-terminal polyhistidine tag. Source: Human Expression Host: HEK293 Cells QC Testing Purity: > 85 % as determined by SDS-PAGE Bio Activity: Protein Description Measure by its ability to bind with human PCSK9 in a functional ELISA. LDL Receptor, also known as LDLR, is a mosaic protein which belongs to 1. Immobilized human PCSK9 at 10 μg/ml (100 μl/well) can bind the Low density lipoprotein receptor gene family. The low density lipoprotein biotinylated recombinant human LDLR. The EC of biotinylated human 50 receptor (LDLR) gene family consists of cell surface proteins involved in LDLR is 0.61 μg/ml. receptor-mediated endocytosis of specific ligands. LDL Receptor consists of 2. Immobilized mouse PCSK9 at 10 μg/ml (100 μl/well) can bind 84 amino acids (after removal of signal peptide) and mediates the biotinylated recombinant human LDLR. The EC50 of biotinylated human endocytosis of cholesterol-rich LDL. Low density lipoprotein (LDL) is LDLR is 0.12 μg/ml. normally bound at the cell membrane and taken into the cell ending up in Endotoxin: lysosomes where the protein is degraded and the cholesterol is made available for repression of microsomal enzyme 3-hydroxy-3-methylglutaryl < 1.0 EU per μg of the protein as determined by the LAL method coenzyme A (HMG CoA) reductase, the rate-limiting step in cholesterol synthesis. -
Misc Thesisdb Bythesissuperv
Honors Theses 2006 to August 2020 These records are for reference only and should not be used for an official record or count by major or thesis advisor. Contact the Honors office for official records. Honors Year of Student Student's Honors Major Thesis Title (with link to Digital Commons where available) Thesis Supervisor Thesis Supervisor's Department Graduation Accounting for Intangible Assets: Analysis of Policy Changes and Current Matthew Cesca 2010 Accounting Biggs,Stanley Accounting Reporting Breaking the Barrier- An Examination into the Current State of Professional Rebecca Curtis 2014 Accounting Biggs,Stanley Accounting Skepticism Implementation of IFRS Worldwide: Lessons Learned and Strategies for Helen Gunn 2011 Accounting Biggs,Stanley Accounting Success Jonathan Lukianuk 2012 Accounting The Impact of Disallowing the LIFO Inventory Method Biggs,Stanley Accounting Charles Price 2019 Accounting The Impact of Blockchain Technology on the Audit Process Brown,Stephen Accounting Rebecca Harms 2013 Accounting An Examination of Rollforward Differences in Tax Reserves Dunbar,Amy Accounting An Examination of Microsoft and Hewlett Packard Tax Avoidance Strategies Anne Jensen 2013 Accounting Dunbar,Amy Accounting and Related Financial Statement Disclosures Measuring Tax Aggressiveness after FIN 48: The Effect of Multinational Status, Audrey Manning 2012 Accounting Dunbar,Amy Accounting Multinational Size, and Disclosures Chelsey Nalaboff 2015 Accounting Tax Inversions: Comparing Corporate Characteristics of Inverted Firms Dunbar,Amy Accounting Jeffrey Peterson 2018 Accounting The Tax Implications of Owning a Professional Sports Franchise Dunbar,Amy Accounting Brittany Rogan 2015 Accounting A Creative Fix: The Persistent Inversion Problem Dunbar,Amy Accounting Foreign Account Tax Compliance Act: The Most Revolutionary Piece of Tax Szwakob Alexander 2015D Accounting Dunbar,Amy Accounting Legislation Since the Introduction of the Income Tax Prasant Venimadhavan 2011 Accounting A Proposal Against Book-Tax Conformity in the U.S. -
(12) United States Patent (10) Patent No.: US 8,603,824 B2 Ramseier Et Al
USOO8603824B2 (12) United States Patent (10) Patent No.: US 8,603,824 B2 Ramseier et al. (45) Date of Patent: Dec. 10, 2013 (54) PROCESS FOR IMPROVED PROTEIN 5,399,684 A 3, 1995 Davie et al. EXPRESSION BY STRAIN ENGINEERING 5,418, 155 A 5/1995 Cormier et al. 5,441,934 A 8/1995 Krapcho et al. (75) Inventors: Thomas M. Ramseier, Poway, CA 5,508,192 A * 4/1996 Georgiou et al. .......... 435/252.3 (US); Hongfan Jin, San Diego, CA 5,527,883 A 6/1996 Thompson et al. (US); Charles H. Squires, Poway, CA 5,558,862 A 9, 1996 Corbinet al. 5,559,015 A 9/1996 Capage et al. (US) 5,571,694 A 11/1996 Makoff et al. (73) Assignee: Pfenex, Inc., San Diego, CA (US) 5,595,898 A 1/1997 Robinson et al. 5,610,044 A 3, 1997 Lam et al. (*) Notice: Subject to any disclaimer, the term of this 5,621,074 A 4/1997 Bjorn et al. patent is extended or adjusted under 35 5,622,846 A 4/1997 Kiener et al. 5,641,671 A 6/1997 Bos et al. U.S.C. 154(b) by 471 days. 5,641,870 A 6/1997 Rinderknecht et al. 5,643,774 A 7/1997 Ligon et al. (21) Appl. No.: 11/189,375 5,662,898 A 9/1997 Ligon et al. (22) Filed: Jul. 26, 2005 5,677,127 A 10/1997 Hogan et al. 5,683,888 A 1 1/1997 Campbell (65) Prior Publication Data 5,686,282 A 11/1997 Lam et al. -
Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants. -
Feather Protein Lysate Optimization and Feather Meal Formation Using
www.nature.com/scientificreports OPEN Feather protein lysate optimization and feather meal formation using YNDH protease with keratinolytic activity afterward enzyme partial purifcation and characterization Doaa A. Goda1*, Ahmad R. Bassiouny2, Nihad M. Abdel Monem2, Nadia A. Soliman1 & Yasser R. Abdel‑Fattah1 Incubation parameters used for the creation of a protein lysate from enzymatically degraded waste feathers using crude keratinase produced by the Laceyella sacchari strain YNDH were optimized using the Response Surface Methodology (RSM); amino acids quantifcation was also estimated. The optimization elevated the total protein to 2089.5 µg/ml through the application of the following optimal conditions: a time of 20.2 h, a feather concentration (conc.) of 3 g%, a keratinase activity of 24.5 U/100 ml, a pH of 10, and a cultivation temperature of 50 °C. The produced Feather Protein Lysate (FPL) was found to be enriched with essential and rare amino acids. Additionally, this YNDH enzyme group was partially purifed, and some of its characteristics were studied. Crude enzymes were frst concentrated with an Amicon Ultra 10‑k centrifugal flter, and then concentrated proteins were applied to a "Q FF" strong anion column chromatography. The partially purifed enzyme has an estimated molecular masses ranging from 6 to 10 kDa. The maximum enzyme activity was observed at 70 °C and for a pH of 10.4. Most characteristics of this protease/keratinase group were found to be nearly the same when the activity was measured with both casein and keratin‑azure as substrates, suggesting that these three protein bands work together in order to degrade the keratin macromolecule.