By Yutaka Kawarabayasi Ph.D. (auth.), Pratyoosh Shukla, Brett I. Pletschke (eds.)
Enzyme know-how is one the main promising disciplines in smooth biotechnology. during this ebook, the purposes of a wide selection of enzymes are highlighted. present reports in enzyme expertise are centred in the direction of the invention of novel enzymes (termed “bio-discovery” or “bio-prospecting”) and the id and elucidation of novel pathways of those novel enzymes with emphasis on their business relevance. With the advance of molecular ideas and different bioinformatics instruments, the time to combine this topic with different fields within the existence sciences has arrived. A fast enlargement of the data base within the box of enzyme biotechnology has happened over the last few years. a lot of this enlargement has been pushed by means of the bio-discovery of many new enzymes from a variety of environments, a few severe in nature, through next protein (enzyme) engineering. those enzymes have discovered a variety of purposes, starting from bioremediation, bio-monitoring, biosensor improvement, bioconversion to biofuels and different biotechnologically vital value-added items. Hydrolases represent an incredible section of the worldwide annual profit generated by way of business enzymes and the emphasis has accordingly been put on those enzymes and their functions. With the gigantic curiosity of researchers lively during this quarter, this booklet will serve to supply details on present features during this box of analysis. within the present variation, the contributions of many different themes in the direction of constructing new instructions of study within the region of enzyme biotechnology are defined. This ebook serves to supply a distinct resource of data to undergraduates, publish graduates and doctoral classes in microbiology and biotechnology in addition to allied existence sciences. the current variation of the publication covers all vital components of enzyme biotechnology i.e. the big variety of enzymes within the box of enzyme biotechnology and their business purposes, new tools and cutting-edge info on glossy tools of enzyme discovery. This booklet will act nearly as good source on many of the present elements of enzyme expertise for all scholars engaged in bioengineering and biotechnology.
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Additional resources for Advances in Enzyme Biotechnology
However, 3 On the Enzyme Specificity for the Synthesis of Prebiotic Galactooligosaccharides more structure-function studies (in vitro and in vivo) assaying different GOS are required to determine the target molecules to be synthesized. Acknowledgements We thank Ramiro Martínez (Novozymes A/S, Madrid, Spain) for supplying Lactozym and for useful suggestions. We thank DSM Food Specialties for supplying Maxilact LGX 5000. Projects BIO2010-20508-C04-01 and BIO2010-20508-C04-04 from Spanish Ministry of Science and Innovation supported this research.
Process Biochem 37:267–274 Freitas FF, Marquez LDS, Ribeiro GP, Brandao GC, Cardoso VL, Ribeiro EJ (2011) A comparison of the kinetic properties of free and immobilized Aspergillus oryzae β-galactosidase. Biochem Eng J 58–59:33–38 Fujimoto H, Miyasato M, Ito Y, Sasaki T, Ajisaka K (1998) Purification and properties of recombinant β-galactosidase from Bacillus circulans. Glycoconj J 15:155–160 Gaur R, Pant H, Jain R, Khare SK (2006) Galactooligosaccharide synthesis by immobilized Aspergillus oryzae beta-galactosidase.
Maximum GOS production for any particular enzyme depends basically on the relative rates of the transgalactosylation and hydrolysis reactions. As the lactose is consumed, the concentration of GOS increases until it reaches a maximum. At this point, the rate of synthesis of GOS products equals its rate of 27 3 On the Enzyme Specificity for the Synthesis of Prebiotic Galactooligosaccharides a OH OH 6'' HO OH HO 3''' OH O 2''' 2' 3' O 1''' HO 3'' OH 2 3 OH O 1 OH O 5'' 4'' 1' 5 O HO OH 6'' OH 4 O 5' 4' OH 6 HO 5''' 4''' 6' 1'' OH 6''' OH O 2'' 3'' b O 5'' 4'' OH O 2'' 6' 1'' OH HO 3' 4 O 5' 4' OH 6 2' 1' OH 5 O HO 3 O 2 1 OH OH Fig.