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METACYC ID Description A0AR23 GO:0004842 (Ubiquitin-Protein Ligase
Electronic Supplementary Material (ESI) for Integrative Biology This journal is © The Royal Society of Chemistry 2012 Heat Stress Responsive Zostera marina Genes, Southern Population (α=0. -
Increasing the Amylose Content of Durum Wheat Through Silencing of the Sbeiia Genes
Sestili et al. BMC Plant Biology 2010, 10:144 http://www.biomedcentral.com/1471-2229/10/144 RESEARCH ARTICLE Open Access IncreasingResearch article the amylose content of durum wheat through silencing of the SBEIIa genes Francesco Sestili1, Michela Janni1, Angela Doherty2, Ermelinda Botticella1, Renato D'Ovidio1, Stefania Masci1, Huw D Jones2 and Domenico Lafiandra*1 Abstract Background: High amylose starch has attracted particular interest because of its correlation with the amount of Resistant Starch (RS) in food. RS plays a role similar to fibre with beneficial effects for human health, providing protection from several diseases such as colon cancer, diabetes, obesity, osteoporosis and cardiovascular diseases. Amylose content can be modified by a targeted manipulation of the starch biosynthetic pathway. In particular, the inactivation of the enzymes involved in amylopectin synthesis can lead to the increase of amylose content. In this work, genes encoding starch branching enzymes of class II (SBEIIa) were silenced using the RNA interference (RNAi) technique in two cultivars of durum wheat, using two different methods of transformation (biolistic and Agrobacterium). Expression of RNAi transcripts was targeted to the seed endosperm using a tissue-specific promoter. Results: Amylose content was markedly increased in the durum wheat transgenic lines exhibiting SBEIIa gene silencing. Moreover the starch granules in these lines were deformed, possessing an irregular and deflated shape and being smaller than those present in the untransformed controls. Two novel granule bound proteins, identified by SDS- PAGE in SBEIIa RNAi lines, were investigated by mass spectrometry and shown to have strong homologies to the waxy proteins. RVA analysis showed new pasting properties associated with high amylose lines in comparison with untransformed controls. -
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. -
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. -
Studies of Barley Limit Dextrinase I I
b ¡\il i: ilq.5l¡Tt-!iÈ' ta. S.S LIBRARY STUDIES OF BARLEY LIMIT DEXTRINASE I I I I by I l I ¡ I Michael John Sissons ì B.Ag.Sc. (University of Adelaide)' I I M.Ag.Sc. (La Trobe UniversitY) i l A thesis submitted to the University of Adelaide for the degree of Doctor of Philosophy Departnent of Plant Science, Waite Agricultural Resea¡ch Institute, Glen Osmond, South Australia October, 1991 LIST OF CONTENTS Contents Page No. Summary i-ü Statement of originality and consent for photocopy or loan lU Acknowledgements iv List of publications v Chapter 1: LITERATURE REVIEW 1.1 Introduction I 1.2 Properties of limit dextrinase 2 t.2.r Purification 2 1.2.2 Enzyme properties 3 t.2.3 Effect of inhibitors 3 r.2.4 Polymorphism 7 t.2.5 Substrate specificity 7 1.2.5.1 Action of limit dextrinase on oligosaccharides 7 t.2.5.2 Polysaccharides 7 1.3 Methods of Assay 9 1.3.1 Detection of Limit Dextrinase Activity in Electrophoretic Gels 10 t.4 Synthesis of limit dextrinase t2 1.4.1 Mechanism of Increase in Limit Dextrinase Activity during Germination 13 1.5 Effect of Barley Genotype and Environment on Limit Dextrinase ActivitY 15 1.6 Limit dextrinase - Role in Malting and Brewing 16 1.6.1 Effect of Kilning on Limit Dextrinase Activity 18 r.6.2 Effect of Mashing on Limit Dextrinase Activity 18 1.6.3 Limit 0extrinase-Role in Speciality Brewing, Distiling and Related Iridustries 2l 1.6.4 Relationship beween Limit Dextrinase Activity, Wort Fermentability and Alcohol Production 22 r.7 Role of Limit Dextrinase in Starch Degradation 23 1.8 Conclusions 24 Chapter -
Evaluation of Saccharifying Methods for Alcoholic Fermentation of Starchy Substrates Alice Lee Iowa State College
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1955 Evaluation of saccharifying methods for alcoholic fermentation of starchy substrates Alice Lee Iowa State College Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons Recommended Citation Lee, Alice, "Evaluation of saccharifying methods for alcoholic fermentation of starchy substrates " (1955). Retrospective Theses and Dissertations. 13626. https://lib.dr.iastate.edu/rtd/13626 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]. NOTE TO USERS This reproduction is the best copy available. ® UMI EVALUATION OF SACCHARIFYING METHODS FOR ALCOHOLIC FERMENTATION OF STARCHY SUBSTRATES by Alice Lee A Dlseertatlon Submitted to the Graduate Faculty In Partial Fulfillment of The RequirementB for the Degree of DOCTOR OF PHILOSOPHY Major Subjects Blochensletry Approved: Signature was redacted for privacy. In Charge of Major Work Signature was redacted for privacy. Head of Major Department Signature was redacted for privacy. Dean of Graduate College Iowa State College 1955 UMI Number: DP12815 INFORMATION TO USERS 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 bleed-through, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. -
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. -
Source: the Arabidopsis Information Resource (TAIR);
Table S1 List of targeted loci and information about their function in Arabidopsis thaliana (source: The Arabidopsis Information Resource (TAIR); https://www.arabidopsis.org/tools/bulk/genes/index.jsp). Locus Gene Model Gene Model Description Gene Model Primary Gene Symbol All Gene Symbols Identifier Name Type AT1G78800 AT1G78800.1 UDP-Glycosyltransferase superfamily protein_coding protein;(source:Araport11) AT5G06830 AT5G06830.1 hypothetical protein;(source:Araport11) protein_coding AT2G31740 AT2G31740.1 S-adenosyl-L-methionine-dependent methyltransferases protein_coding superfamily protein;(source:Araport11) AT5G11960 AT5G11960.1 magnesium transporter, putative protein_coding (DUF803);(source:Araport11) AT4G00560 AT4G00560.4 NAD(P)-binding Rossmann-fold superfamily protein_coding protein;(source:Araport11) AT1G80510 AT1G80510.1 Encodes a close relative of the amino acid transporter ANT1 protein_coding (AT3G11900). AT2G21250 AT2G21250.1 NAD(P)-linked oxidoreductase superfamily protein_coding protein;(source:Araport11) AT5G04420 AT5G04420.1 Galactose oxidase/kelch repeat superfamily protein_coding protein;(source:Araport11) AT4G34910 AT4G34910.1 P-loop containing nucleoside triphosphate hydrolases protein_coding superfamily protein;(source:Araport11) AT5G66120 AT5G66120.2 3-dehydroquinate synthase;(source:Araport11) protein_coding AT1G45110 AT1G45110.1 Tetrapyrrole (Corrin/Porphyrin) protein_coding Methylase;(source:Araport11) AT1G67420 AT1G67420.2 Zn-dependent exopeptidases superfamily protein_coding protein;(source:Araport11) AT3G62370 -
Structure of the Starch-Debranching Enzyme Barley Limit Dextrinase Reveals Homology of the N-Terminal Domain to CBM21
View metadata,Downloaded citation and from similar orbit.dtu.dk papers on:at core.ac.uk Dec 20, 2017 brought to you by CORE provided by Online Research Database In Technology Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21 Møller, Marie Sofie; Abou Hachem, Maher ; Svensson, Birte; Henriksen, Anette Published in: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online Link to article, DOI: 10.1107/S1744309112031004 Publication date: 2012 Document Version Publisher's PDF, also known as Version of record Link back to DTU Orbit Citation (APA): Møller, M. S., Abou Hachem, M., Svensson, B., & Henriksen, A. (2012). Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 68(Pt 9), 1008-1012. DOI: 10.1107/S1744309112031004 General rights Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights. • Users may download and print one copy of any publication from the public portal for the purpose of private study or research. • You may not further distribute the material or use it for any profit-making activity or commercial gain • You may freely distribute the URL identifying the publication in the public portal If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.