Download Advances in Textile Biotechnology by Artur Cavaco-Paulo, V. A. Nierstrasz Vincent Nierstrasz PDF

By Artur Cavaco-Paulo, V. A. Nierstrasz Vincent Nierstrasz

Biotechnology has impacted the textiles during the improvement of extra effective and environmentally pleasant production methods, in addition to permitting the layout of stronger fabric fabrics. This e-book will supply an intensive assessment of present and destiny focuses of biotechnology within the fiber and cloth undefined. half one of many e-book opens with a assessment of applied sciences enthusiastic about cloth biotechnology. Chapters discover the layout and engineering of novel enzymes for fabric purposes and advancements in strategies and gear for enzymatic fabric remedies. half investigates the amendment of specific fibers by using biotechnology. Key subject matters comprise the remedy of wool and silk fibers and the enzymatic remedy as opposed to traditional processing of cotton. With specialist contributions from leaders of their fields, Advances in fabric Biotechnology will function a finished consultant for these within the fabric and fiber undefined, in addition to specialists within the biology, chemical and environmental engineering industries.

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Araújo r, casal m and cavaco-paulo a (2008b), ‘Application of enzymes for textile fibres processing’, Biocatal Biotransfor, 26(5), 332–349. 1080/ 10242420802390457. araújo r, cavaco-paulo a and casal m (2008a), ‘Strategies towards the functionalization of Bacillus subtilis subtilisin E for wool finishing applications’, Eng Life Sci, 8(3), 238–249. 1002/elsc. 200700056. araújo r, silva c, machado r, casal m, cunha a m, rodriguez-cabello j c and cavaco-paulo a (2009), ‘Proteolytic enzyme engineering: a tool for wool’, Biomacromolecules, 10, 1655–1661.

Introduction of a lysine, an asparagine, or an alanine at position 357 and of a lysine or an asparagine at position 354 resulted in © Woodhead Publishing Limited, 2010 Design and engineering of novel enzymes for textile applications 19 calcium-independent variants. Although the Asp357Lys, Asp357Asn, and Asp357Ala variants did not bind calcium, at elevated temperatures these calcium-independent mutants showed a reduced activity. Over the whole temperature range the activities of the Asp354Lys and Asp354Asn variants are significantly lower than the wild-type enzyme in the presence of calcium.

Ben ali m, khemakhem b, robert x, haser r and bejar s (2006), ‘Thermostability enhancement and change in starch hydrolysis profile of the maltohexaoseforming amylase of Bacillus stearothermophilus US100 strain’, Biochem J, 394, 51–56. 1042/BJ20050726. ben ali m, mhiri s, mezghani m and bejar s (2001), ‘Purification and sequence analysis of the atypical maltohexaose-forming α-amylase of the B. stearothermophilus US100’, Enzyme Microb Technol, 28(6), 537–542. 1016/S01410229(01)00294-0. berry m j, davis p j and gidley m j (2001), ‘Conjugated polysaccharide fabric detergent and conditioning products’, United States Patent 6225462.

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