Download Carbohydrate-active enzymes: structure, function and by Kwan-Hwa Park (ed.) PDF

By Kwan-Hwa Park (ed.)

Fresh advances in biochemistry and biotechnology have enabled major growth in uncomplicated study on carbohydrate-active enzymes and advances of their powerful program. The mechanism of catalytic response of carbohydrate-active enzymes isn't absolutely understood, although, as they typically express strange substrate specificity and modes of motion. This complete assortment summarises one of the most very important learn within the box of carbohydrate-active enzymes, targeting the enzymatic response mechanism, structure-function courting and position within the dwelling organism The e-book relies on papers awarded within the 2008 Agricultural Biotechnology Symposium Carbohydrate-active enzymes: constitution, functionality and functions hung on September 26th-27th 2008 in Seoul nationwide college, Korea. This symposium used to be equipped through the heart for Agricultural Biomaterials, Seoul nationwide college, Korea, which has prepared symposia on agricultural biotechnology each year seeing that 1990. Many vital effects on new different types of carbohydrate-active enzymes and their purposes were stated at those conferences. Papers partially one in every of this assortment specialize in structure-function relationships of carbohydrate-active enzymes. Papers partly speak about capabilities and purposes of carbohydrate-active enzymes, resembling enzymes for grain processing and glycosidases and their mutants as beneficial instruments for glycoside synthesis. With its unique editor and foreign workforce of participants, Carbohydrate-active enzymes: constitution, functionality and functions is a necessary reference for study scientists, post-graduate scholars and people within the foodstuff with an curiosity in enzymes.

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Additional resources for Carbohydrate-active enzymes: structure, function and applications

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MacGregor A W, Donald L J , MacGregor E A, and Duckworth H W (2003), ' Stoichiometry of the complex formed by barley limit dextrinase with its endogenous inhibitor. Determination by electrospray time-of-flight mass spectrometry' J Cereal Sci, 37, 357-3 62. MacGregor E A, Jespersen H M, and Svensson B ( 1 996), 'A circularly permuted a­ amylase-type alP-barre l in glucan-synthesizing glucosyltransferases' , FEBS Lett, 3 78, 263-266. MacGregor E A, Janecek S , and Svensson B (200 1 ), ' Relationship of sequence and structure to specificity in the a-amylase family of enzymes' , Biochim Biophys Acta, 1 546, 1 -20.

30 Beier L, Svendsen A, Andersen C, Frandsen T P, Borchert T V, and Cherry J R (2000 ) , ' Conversion of the maltogenic a-amylase Novamyl into a CGTase' , Protein Eng, 1 3 , 509-5 1 3 . Blennow A , Engelsen S B , Nielsen T H , Baunsgaard L , and Mikkelsen R (2002) , ' Starch phosphorylation - a new front line in starch research' , Trends in Plant Sci, 7, 445-450. Boraston A B, Bolam D N, Gilbert H J, and Davies G J (2004) , ' Carbohydrate-binding modules : fine-tuning polysaccharide recognition', Biochem J, 3 82, 769-78 1 .

Certain enzymes carry auxiliary tools facilitating contact with supramolecular substrate structures. org/) and secondary carbohydrate binding sites situated on the surface of the integral enzyme structure. A variety of enzyme isoforms can furthermore display distinctly different functional and stability properties. A regulatory point resides in the specificity of proteinaceous inhibitors directed towards individual enzymes. A wide range of approaches including site-directed mutagenesis, domain fusion, and formation of chimeras have been applied to investigate structure/function relationships in starch­ degrading enzymes with focus on features engaged in polysaccharide processing.

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