Engineering Properties of Sweet Potato Starch for Industrial Applications by Biotechnological Techniques Including Genome Editing
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Product Guide
www.megazyme.com es at dr hy o rb a C • s e t a r t s b u S e m y z n E • s e m y z n E • s t i K y a s s A Plant Cell Wall & Biofuels Product Guide 1 Megazyme Test Kits and Reagents Purity. Quality. Innovation. Barry V. McCleary, PhD, DScAgr Innovative test methods with exceptional technical support and customer service. The Megazyme Promise. Megazyme was founded in 1988 with the We demonstrate this through the services specific aim of developing and supplying we offer, above and beyond the products we innovative test kits and reagents for supply. We offer worldwide express delivery the cereals, food, feed and fermentation on all our shipments. In general, technical industries. There is a clear need for good, queries are answered within 48 hours. To validated methods for the measurement of make information immediately available to the polysaccharides and enzymes that affect our customers, we established a website in the quality of plant products from the farm 1994, and this is continually updated. Today, it gate to the final food. acts as the source of a wealth of information on Megazyme products, but also is the hub The commitment of Megazyme to “Setting of our commercial activities. It offers the New Standards in Test Technology” has been possibility to purchase and pay on-line, to continually recognised over the years, with view order history, to track shipments, and Megazyme and myself receiving a number many other features to support customer of business and scientific awards. -
Characterisation of Streptococcus Pneumoniae Opacity Phase Variation
Characterisation of Streptococcus pneumoniae Opacity Phase Variation Melissa Hui Chieh Chai, BBiomedSc (Hon), MSc A thesis submitted in fulfilment of the requirements for the degree of Doctor of Philosophy from the University of Adelaide February 2016 Research Centre for Infectious Diseases Department of Molecular and Cellular Biology The University of Adelaide Adelaide, S.A., Australia Table of Contents Chapter 1: INTRODUCTION ........................................................................... 1 1.1 The Pneumococcus ....................................................................................................... 1 1.1.1 Burden of Disease .................................................................................................. 1 1.1.2 Antimicrobial resistance ........................................................................................ 3 1.2 Pneumococcal Vaccines ............................................................................................... 4 1.3 Pathogenesis of Pneumococcal Disease ....................................................................... 7 1.3.1 Pneumococcal colonisation.................................................................................... 7 1.3.2 Progression to disease .......................................................................................... 10 1.4 S. pneumoniae Virulence Factors ............................................................................... 11 1.4.1 Pneumococcal capsule ........................................................................................ -
Mechanism of Nucleotide Flipping by Human Alkyladenine DNA Glycosylase
Mechanism of Nucleotide Flipping by Human Alkyladenine DNA Glycosylase by Jenna M. Hendershot A dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy (Biological Chemistry) in the University of Michigan 2014 Doctoral Committee: Associate Professor Patrick J. O’Brien, Chair Professor Hashim M. Al-Hashimi, Duke University Professor Carol A. Fierke Associate Professor Bruce A. Palfey Associate Professor Raymond C. Trievel © Jenna M. Hendershot 2014 Table of Contents List of Figures.………………….…………………………………………………………………………………………… iii List of Tables.……………………………………………………………………………………………………………….. vi List of Appendices.…….....…………………………………………………………………………………………….. vii List of Abbreviations..………………………………………………………………………………………………….. viii Abstract...…………………………………………………………………………………………………………………….. xi Chapter (1) Introduction…………………………………………………………………………………………………. 1 (2) Substitution of Active Site Tyrosines with Tryptophan Alters the Free Energy for Nucleotide Flipping by Human Alkyladenine DNA Glycosylase.………..……. 18 (3) Critical Role of DNA Intercalation in Enzyme-Catalyzed Nucleotide Flipping… 58 (4) Evidence for Early Intercalation during the Search for DNA Damage by Human Alkyladenine DNA Glycosylase………………………………..………………………. 94 (5) Structure/Function Analysis of Intercalation and Nucleotide Flipping in Human Alkyladenine DNA Glycosylase….…………………………………………………….. 124 (6) Conclusions and Future Directions……….………………………………………………………. 155 ii List of Figures Figure 1.1: Nucleotide flipping……………………………………………………………………………………… -
Characterization of the Relationship Between Measles Virus Fusion
University of Massachusetts Medical School eScholarship@UMMS GSBS Dissertations and Theses Graduate School of Biomedical Sciences 2006-05-17 Characterization of the Relationship Between Measles Virus Fusion, Receptor Binding, and the Virus-Specific Interaction Between the Hemagglutinin and Fusion Glycoproteins: a Dissertation Elizabeth Ann Corey University of Massachusetts Medical School Let us know how access to this document benefits ou.y Follow this and additional works at: https://escholarship.umassmed.edu/gsbs_diss Part of the Amino Acids, Peptides, and Proteins Commons, Cells Commons, Chemical Actions and Uses Commons, Lipids Commons, and the Virus Diseases Commons Repository Citation Corey EA. (2006). Characterization of the Relationship Between Measles Virus Fusion, Receptor Binding, and the Virus-Specific Interaction Between the Hemagglutinin and Fusion Glycoproteins: a Dissertation. GSBS Dissertations and Theses. https://doi.org/10.13028/hg2y-0r35. Retrieved from https://escholarship.umassmed.edu/gsbs_diss/221 This material is brought to you by eScholarship@UMMS. It has been accepted for inclusion in GSBS Dissertations and Theses by an authorized administrator of eScholarship@UMMS. For more information, please contact [email protected]. CHARACTERIZATION OF THE RELATIONSHIP BETWEEN MEASLES VIRUS FUSION , RECEPTOR BINDING , AND THE VIRUS-SPECIFIC INTERACTION BETWEEN THE HEMAGGLUTININ AND FUSION GL YCOPROTEINS A Dissertation Presented Elizabeth Anne Corey Submitted to the Faculty of the University of Massachusetts Graduate -
Function and Structure Studies of GH Family 31 and 97 \Alpha
110610 (RV-17) Biosci. Biotechnol. Biochem., 75 (12), 110610-1–9, 2011 Award Review Function and Structure Studies of GH Family 31 and 97 -Glycosidases Masayuki OKUYAMA Research Faculty of Agriculture, Hokkaido University, Kita-9, Nishi-9, Kita-ku, Sapporo 060-8589, Japan Online Publication, December 7, 2011 [doi:10.1271/bbb.110610] A huge number of glycoside hydrolases are classified an evolutionary relationship of proteins in the family, into the glycoside hydrolase family (GH family) based from which it is often possible to extract information on on their amino-acid sequence similarity. The glycoside function and structure.3) Classification in a GH family hydrolases acting on -glucosidic linkage are in GH has, accordingly, become indispensable for research on family 4, 13, 15, 31, 63, 97, and 122. This review deals glycoside hydrolases. Glycoside hydrolases are also mainly with findings on GH family 31 and 97 enzymes. divided into two mechanistic classes, inverting and Research on two GH family 31 enzymes is described: retaining enzymes: with inversion or net retention of clarification of the substrate recognition of Escherichia anomeric configuration during the catalytic reaction.4) coli -xylosidase, and glycosynthase derived from Schiz- The stereochemical outcome is generally conserved in a osaccharomyces pombe -glucosidase. GH family 97 is GH family. The inverting mechanism proceeds via a an aberrant GH family, containing inverting and simple single displacement. Two functional groups, retainingAdvance glycoside hydrolases. The inverting View enzyme usually carboxyl groups, act as general acid and general in GH family 97 displays significant similarity to base catalysts. The general acid catalyst donates a proton retaining -glycosidases, including GH family 97 retain- to the departure aglycon, and the general base catalyst ing -glycosidase, but the inverting enzyme has no simultaneously deprotonates the incoming water mole- catalytic nucleophile residue. -
Letters to Nature
letters to nature Received 7 July; accepted 21 September 1998. 26. Tronrud, D. E. Conjugate-direction minimization: an improved method for the re®nement of macromolecules. Acta Crystallogr. A 48, 912±916 (1992). 1. Dalbey, R. E., Lively, M. O., Bron, S. & van Dijl, J. M. The chemistry and enzymology of the type 1 27. Wolfe, P. B., Wickner, W. & Goodman, J. M. Sequence of the leader peptidase gene of Escherichia coli signal peptidases. Protein Sci. 6, 1129±1138 (1997). and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258, 12073±12080 2. Kuo, D. W. et al. Escherichia coli leader peptidase: production of an active form lacking a requirement (1983). for detergent and development of peptide substrates. Arch. Biochem. Biophys. 303, 274±280 (1993). 28. Kraulis, P.G. Molscript: a program to produce both detailed and schematic plots of protein structures. 3. Tschantz, W. R. et al. Characterization of a soluble, catalytically active form of Escherichia coli leader J. Appl. Crystallogr. 24, 946±950 (1991). peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry 34, 3935±3941 29. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and (1995). the thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281±296 (1991). 4. Allsop, A. E. et al.inAnti-Infectives, Recent Advances in Chemistry and Structure-Activity Relationships 30. Meritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505± (eds Bently, P. H. & O'Hanlon, P. J.) 61±72 (R. Soc. Chem., Cambridge, 1997). -
Immunobiologicals Purified Proteins
Immunobiologicals i Cat. No. Enzyme Quantity PURIFIED PROTEINS 321731 Pullalanase, Crude Form 500 mg 835001 Superoxide Dismutase 25 mg 835002 100 mg Purified Enzymes 835011 Superoxide Dismutase 1 mg Cat. No. Enzyme Quantity 835012 5 mg 321241 β-N-Acetylhexosaminidase 0.5 U 321351 Thermolysin 250 mg 320941 N-Acetylmuramidase 10 mg 360941 Yeast LyticEnzyme,70,000u/mg 500mg 364841 Alkaline Phosphatase, Labeling Grade 5 KU 360942 1 g µ 360943 2 g 194966 Carboxypeptidase P, Excision Grade 20 g 360944 5 g 321271 Carboxypeptidase W 1 mg 360951 Yeast LyticEnzyme,5,000u/mg 5g 320961 Cellulase Y-C 10 g 360952 10 g 150 320301 Chondroitinase ABC Lyase, Protease Free 4x1 U 360953 25 g 320211 Chondroitinase ABC Lyase 4x5 U 360954 100 g Purified Proteins 320221 Chondroitinase AC-II Lyase 4x5 U 320921 Zymolyase 20T 1 g 320311 Chondroitinase AC-I 4x1 U 320932 Zymolyase 100T 250 mg 970551 Chondroitin Sulfate C 100 mg 320931 500 mg 970571 Chondroitin Sulfate D 10 mg 320231 Chondro-4-sulfatase 4x1.6 U 320241 Chondro-6-sulfatase 4x2.5 U 362001 Collagenase, Type 300C 300 KU Blood Proteins 321601 Dextranase 10 mg 321321 Endo-β-galactosidase 0.1 U ALBUMIN, BOVINE 321281 Endoglycosidase D 0.1 U Cat. No. Description Quantity 321282 0.5 U 810012 Crystalline 5 g 391311 Endoglycosidase H 0.2 U 810013 10 g 391312 2 U 810014 100 g 320182 Glucoamylase 2 KU 810032 Fraction V Powder, pH7.0 50 g 321291 Glycopeptidase A 1 mU 810033 100 g 321051 Glycosidases, Mixed 1 g 810034 500 g 321052 5 g 810035 1 kg 810036 5 kg 321001 Glycosidase 1 g 810532 Fraction V Powder, pH5.2 -
A Soluble Starch Synthase I Gene, Ibssi, Alters the Content, Composition, Granule Size and Structure of Starch in Transgenic
www.nature.com/scientificreports OPEN A soluble starch synthase I gene, IbSSI, alters the content, composition, granule size and Received: 23 January 2017 Accepted: 11 April 2017 structure of starch in transgenic Published: xx xx xxxx sweet potato Yannan Wang, Yan Li, Huan Zhang, Hong Zhai, Qingchang Liu & Shaozhen He Soluble starch synthase I (SSI) is a key enzyme in the biosynthesis of plant amylopectin. In this study, the gene named IbSSI, was cloned from sweet potato, an important starch crop. A high expression level of IbSSI was detected in the leaves and storage roots of the sweet potato. Its overexpression significantly increased the content and granule size of starch and the proportion of amylopectin by up- regulating starch biosynthetic genes in the transgenic plants compared with wild-type plants (WT) and RNA interference plants. The frequency of chains with degree of polymerization (DP) 5–8 decreased in the amylopectin fraction of starch, whereas the proportion of chains with DP 9–25 increased in the IbSSI-overexpressing plants compared with WT plants. Further analysis demonstrated that IbSSI was responsible for the synthesis of chains with DP ranging from 9 to 17, which represents a different chain length spectrum in vivo from its counterparts in rice and wheat. These findings suggest that theIbSSI gene plays important roles in determining the content, composition, granule size and structure of starch in sweet potato. This gene may be utilized to improve the content and quality of starch in sweet potato and other plants. In plants, starch consists of amylose and amylopectin. Amylose mainly comprises linear chains that are linked by α-1, 4 O-glycosidic bonds, whereas amylopectin is highly branched and contains 5–6% α-1,6 O-glycosidic bonds to generate glucan branches of various lengths1. -
Characterization of Starch Debranching Enzymes of Maize Endosperm Afroza Rahman Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1998 Characterization of starch debranching enzymes of maize endosperm Afroza Rahman Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons, Molecular Biology Commons, and the Plant Sciences Commons Recommended Citation Rahman, Afroza, "Characterization of starch debranching enzymes of maize endosperm " (1998). Retrospective Theses and Dissertations. 12519. https://lib.dr.iastate.edu/rtd/12519 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps. -
3-Methyladenine DNA Glycosylases: Structure, Function, and Biological Importance Michael D
Review articles 3-Methyladenine DNA glycosylases: structure, function, and biological importance Michael D. Wyatt,1 James M. Allan,1 Albert Y. Lau,2 Tom E. Ellenberger,2 and Leona D. Samson1* Summary The genome continuously suffers damage due to its reactivity with chemical and physical agents. Finding such damage in genomes (that can be several million to several billion nucleotide base pairs in size) is a seemingly daunting task. 3-Methyladenine DNA glycosylases can initiate the base excision repair (BER) of an extraordinarily wide range of substrate bases. The advantage of such broad substrate recognition is that these enzymes provide resistance to a wide variety of DNA damaging agents; however, under certain circumstances, the eclectic nature of these enzymes can confer some biological disadvantages. Solving the X-ray crystal struc- tures of two 3-methyladenine DNA glycosylases, and creating cells and animals altered for this activity, contributes to our understanding of their enzyme mechanism and how such enzymes influence the biological response of organisms to several different types of DNA damage. BioEssays 21:668–676, 1999. 1999 John Wiley & Sons, Inc. Introduction ately interpreted by DNA-processing enzymes. Unfortunately, DNA carries life’s genetic information encoded in the arrange- these bases are also chemically reactive, and the inevitable ment of bases along the length of the DNA molecule. Each base modifications produce a variety of biological outcomes, DNA base has a distinct chemical structure that is appropri- depending on how a cell recognizes and responds to the modification. Cellular DNA repair mechanisms target these inappropriate DNA structures, and play a vital role in maintain- 1Department of Cancer Cell Biology, Harvard School of Public Health, ing genomic integrity. -
Understanding Starch Metabolism in Pea Seeds Towards Tailoring Functionality for Value-Added Utilization
International Journal of Molecular Sciences Review Understanding Starch Metabolism in Pea Seeds towards Tailoring Functionality for Value-Added Utilization Bianyun Yu 1,*, Daoquan Xiang 1 , Humaira Mahfuz 1,2, Nii Patterson 1 and Dengjin Bing 3 1 Aquatic and Crop Resource Development Research Centre, National Research Council Canada, 110 Gymnasium Place, Saskatoon, SK S7N 0W9, Canada; [email protected] (D.X.); [email protected] (H.M.); [email protected] (N.P.) 2 Department of Biology, Faculty of Science, University of Ottawa, 30 Marie Curie, Ottawa, ON K1N 6N5, Canada 3 Lacombe Research and Development Centre, Agriculture and Agri-Food Canada, 6000 C and E Trail, Lacombe, AB T4L 1W1, Canada; [email protected] * Correspondence: [email protected] Abstract: Starch is the most abundant storage carbohydrate and a major component in pea seeds, accounting for about 50% of dry seed weight. As a by-product of pea protein processing, current uses for pea starch are limited to low-value, commodity markets. The globally growing demand for pea protein poses a great challenge for the pea fractionation industry to develop new markets for starch valorization. However, there exist gaps in our understanding of the genetic mechanism underlying starch metabolism, and its relationship with physicochemical and functional properties, which is a prerequisite for targeted tailoring functionality and innovative applications of starch. This review Citation: Yu, B.; Xiang, D.; outlines the understanding of starch metabolism with a particular focus on peas and highlights Mahfuz, H.; Patterson, N.; Bing, D. the knowledge of pea starch granule structure and its relationship with functional properties, and Understanding Starch Metabolism in industrial applications. -
STUDY of STARCH DEBRANCHING ENZYMES in DEVELOPING WHEAT KERNELS a Thesis Submitted to the College of Graduate Studies and Resear
STUDY OF STARCH DEBRANCHING ENZYMES IN DEVELOPING WHEAT KERNELS A Thesis Submitted to the College of Graduate Studies and Research in Partial Fulfilment of the Requirements for the Degree of Doctor of Philosophy in the Department of Biochemistry University of Saskatchewan Saskatoon By Supatcharee Netrphan Spring 2002 © Copyright Supatcharee Netrphan, 2002. All rights reserved. PERMISSION TO USE In presenting this thesis in partial fulfilment of the requirements for a Postgraduate degree from the University of Saskatchewan, I agree that the Libraries of this University may make it freely available for inspection. I further agree that permission for copying of this thesis in any manner, in whole or in part, for scholarly purposes may be granted by the professor or professors who supervised my thesis work or, in their absence, by the Head of the Department or the Dean of the College in which my thesis work was done. It is understood that any copying or publication or use of this thesis or parts thereof for financial gain shall not be allowed without my written permission. It is also understood that due recognition shall be given to me and to the University of Saskatchewan in any scholarly use which may be made of any material in my thesis. Requests for permission to copy or to make other use of material in this thesis in whole or in part should be addressed to: Head of the Department of Biochemistry University of Saskatchewan 107 Wiggins Road Saskatoon, Saskatchewan S7N 5E5 i ABSTRACT Starch debranching enzymes, which specifically hydrolyse a-1,6 glucosidic bonds in glucans containing both a-1,4 and a-1,6 linkages, are classified into two types: isoamylase (EC.