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Renewable Resources for Functional Polymers and Biomaterials: Polysaccharides, Proteins and Polyesters: Volume 1
Author(s): Peter A Williams
- Publisher: Royal Society of Chemistry
- Publication Date: 9 Sept. 2011
- Edition: 1st
- Language: English
- Print length: 456 pages
- ISBN-10: 1849732450
- ISBN-13: 9781849732451
Book Description
Covers polysaccharides and Other Other Contributor important biomacromolecules, detailing their source, production, structures, properties, and current and potential application in biotechnology and medicine.
Editorial Reviews
Review
From the Back Cover
The importance of renewable based materials has lead to a renaissance in the chemistry of biomacromolecules and their expansive functional properties. This book covers the source, production, structures and properties of some of the most important biomacromolecules with applications in the fields of biotechnology and medicine. Particular attention is given to polysaccharides obtained from botanical, algal, animal and microbial sources; microbial polyesters; the glycoproteins fibronectin and laminin as well as an introduction to nucleic acid polymers and genetic engineering.
Aimed at both the biomedical and wider materials science communities, the overview of biopolymers at the graduate and post graduate level will appeal to both academic and industrial scientists who are involved in research and development activities.
About the Author
Excerpt. © Reprinted by permission. All rights reserved.
Renewable Resources for Functional Polymers and Biomaterials
By Peter A. Williams
The Royal Society of Chemistry
Copyright © 2011 Royal Society of Chemistry
All rights reserved.
ISBN: 978-1-84973-245-1
Contents
Chapter 1 Natural Polymers: Introduction and Overview Peter A. Williams,
Chapter 2 Natural Polymer Resources: Isolation, Separation and Characterization Werner Praznik, Renate Löppert and Anton Huber,
Chapter 3 Cellulose and Its Derivatives in Medical Use Tohru Shibata,
Chapter 4 Xylan and Xylan Derivatives – Basis of Functional Polymers for the Future Thomas Heinze and Stephan Daus,
Chapter 5 Starch and its Derived Products: Biotechnological and Biomedical Applications John F. Kennedy, Charles J. Knill, Liu Liu and Parmjit S. Panesar,
Chapter 6 Gum Arabic and other Exudate Gums Glyn O. Phillips and Aled O. Phillips,
Chapter 7 Alginates: Existing and Potential Biotechnological and Medical Applications Kurt I. Draget and Gudmund Skjåk-Bræk,
Chapter 8 Pectins: Production, Properties and Applications H.U. Endress,
Chapter 9 Hyaluronan: a Simple Molecule with Complex Character Koen P. Vercruysse,
Chapter 10 Chitin and Chitosan: Sources, Production and Medical Applications Thomas Kean and Maya Thanou,
Chapter 11 β-Glucans Steve W. Cui, Qi Wang and Mei Zhang,
Chapter 12 Microbial Polyesters: Biosynthesis, Properties, Biodegradation and Applications Chang-Sik Ha and Won-Ki Lee,
Chapter 13 Glycoproteins and Adhesion Ligands: Properties and Biomedical Applications B.K. Mann and S.D. Turner,
Chapter 14 Nucleic Acid Polymers and Applications of Recombinant DNA Technology Ian Holt and Y. Chan N. Pham,
Subject Index,
CHAPTER 1
Natural Polymers: Introduction and Overview
PETER A. WILLIAMS
Glyndwr University, Plas Coch, Mold Road, Wrexham LL11 2AW, UK
1.1 Introduction to Biopolymers
Proteins and polysaccharides are found abundantly in nature and are major constituents of plants, animals and micro-organisms serving a number of important functions. Proteins are composed of amino acids and although there are hundreds of different proteins they all consist of linear chains of the same twenty L-a-amino acids which are linked through peptide bonds formed by a condensation reaction. Each amino acid contains an amino group and carboxylic acid group with the general formula:
[FORMULA NOT REPRODUCIBLE IN ASCII]
The R group differs for the various amino acids and can impart polar, non-polar, anionic or cationic characteristics. The amino acid units are linked together through a peptide bond to form a polypeptide chain as illustrated below:
[FORMULA NOT REPRODUCIBLE IN ASCII]
Proteins consisting of between 15 and 10 000 amino acids are known. Since proteins contain both cationic and anionic charges due to the presence of ionisable groups, notably amine and carboxyl, they have a characteristic isoelectric point which corresponds to the pH at which the molecules have a net zero charge.
There are various levels of protein structure. The protein primary structure is defined by the characteristic sequence of amino acids of the polypeptide chain. Certain amino acids within the chain give rise to local secondary structures such as the a helix and the pleated sheet. There is a tendency for the more hydrophobic amino acids present to reside within the core of the molecule so that they are less exposed to the aqueous environment, and the overall shape of the protein that is formed (the tertiary structure) is stabilised by a range of interactions
