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When faced with a shortage of oxygen, many bacterial species use nitrate to support respiration via the process of denitrification. This takes place extensively in nitrogen-rich soils and generates the gaseous products nitric oxide (NO), nitrous oxide (N2O) and dinitrogen (N2). The denitrifying bacteria protect themselves from the endogenous cytotoxic NO produced by converting it to N2O, which can be released into the atmosphere. However, N2O is a potent greenhouse gas and hence the activity of the enzyme that breaks down N2O has a crucial role in restricting its atmospheric levels. Here, we review the current understanding of the process by which N2O is produced and destroyed and discuss the potential for feeding this into new approaches for combating N2O release.

This second edition integrates many new findings into the underlying enzymatic mechanisms and the catalytic machinery for building the varied and complex end product metabolites. This text will serve as a reference point for chemists of every subdiscipline, including synthetic organic chemists and medicinal chemists.

Alkaline phosphatases (APases) are commonly used as nonradioactive markers for detecting specific proteins or DNA targets in clinical medicine and molecular biology. However, their applications in the biotechnology industry require thermostability and storage stability. Our preliminary study revealed that APase from Thermus sp. NTU-237 (TsAPase) is thermostable and exhibits high activity. Therefore, it is desirable to establish the optimal conditions for its application. To characterize APase from thermophile Thermus sp. NTU-237 and to evaluate its potential applications. The APase gene of Thermus sp. NTU-237 was cloned and expressed in Escherichia coli. Subsequently, the effects of buffer, glycerol, sodium dodecyl sulfate (SDS), NaCl, and temperature on enzyme activity were studied to establish the optimal conditions for TsAPase assays. In addition, the potential for application of TsAPase was evaluated using the 5-bromo-4-chloro-3-indolyl phosphate/nitro blue tetrazolium (BCIP/NBT) active staining method. Recombinant TsAPase was identified as having a dimeric structure and a molecular mass of 109 kDa. Sequence alignment analysis of known thermophilic APases with TsAPase and E. coli APase revealed that catalytic and binding residues were highly conserved. This finding suggested that the catalytic mechanism of TsAPase is the same as that of other APases. TsAPase activity was inhibited by glycerol and SDS but enhanced by NaCl and Tris-HCl buffer. The kinetic parameters Km, kcat, and Vmax were determined to be 81 µM, 6.08 s-1, and 6.76 U.mg-1, respectively. The optimum temperature of TsAPase was 80 °C, and TsAPase was stable at room temperature for more than 10 days. Moreover, TsAPase could catalyze the dephosphorylation of BCIP and could elicit blue color development by the BCIP/NBT reaction kit at room temperature. These results illustrate that TsAPase has potential for application in medical or basic research.

This textbook describes the types of natural products, the biosynthetic pathways that enable the production of these molecules, and an update on the discovery of novel products in the post-genomic era.

The biochemistry of food is the foundation on which the research and development advances in food biotechnology are built. In Food Biochemistry and Food Processing, Second Edition, the editors have brought together more than fifty acclaimed academicians and industry professionals from around the world to create this fully revised and updated edition. This book is an indispensable reference and text on food biochemistry and the ever increasing developments in the biotechnology of food processing. Beginning with sections on the essential principles of food biochemistry, enzymology, and food processing, the book then takes the reader on commodity-by-commodity discussions of biochemistry of raw materials and product processing. Chapters in this second edition have been revised to include safety considerations and the chemical changes induced by processing in the biomolecules of the selected foodstuffs. This edition also includes a new section on health and functional foods, as well as ten new chapters including those on thermally and minimally processed foods, separation technology in food processing, and food allergens. Food Biochemistry and Food Processing, second edition fully develops and explains the biochemical aspects of food processing, and brings together timely and relevant topics in food science and technology in one package. This book is an invaluable reference tool for professional food scientists, researchers and technologists in the food industry, as well as faculty and students in food science, food technology and food engineering programs. The Editor Dr. Benjamin K. Simpson, Department of Food Science and Agricultural Chemistry, McGill University, Quebec, Canada Associate Editors Professor Leo Nollet, Department of Applied Engineering Sciences, Hogeschool Ghent, Belgium Professor Fidel Toldrá, Instituto de Agroquímica y Tecnología de Alimentos (CSIC), Valencia, Spain Professor Soottawat Benjakul, Department of Food Technology, Prince of Songkla University, Songkhla, Thailand Professor Gopinadhan Paliyath, Department of Plant Agriculture, University of Guelph, Ontario, Canada Dr. Y. H. Hui, Consultant to the Food Industry, West Sacramento, California, USA.

This popular account of the history of ferment takes the reader on a fascinating journey from its obscure origins in medieval medicine and alchemy to the modern concept of the enzyme. During the 19th century, the question of the nature of the ferment led to a long and bitter conflict between those that believed in a vital force peculiar to the living cell and those that looked for a more chemical explanation. The book takes an in-depth look at the events of 1897 when Eduard Buchner demonstrated that cell-free extracts of yeast could catalyze alcoholic fermentation, putting an end to “vitalism” and at the same time earning him a Nobel Prize, the first to be awarded for purely biochemical work.

Cet ouvrage est l'unique adaptation française du célèbre Fundamentals of Enzyme Kinetics d'Athel Cornish-Bowden. Il donne une description des principes de base des phénomènes d'inhibition et d'activation, de la régulation allostérique et de la coopérativité. Il aborde les systèmes enzymatiques, le contrôle métabolique et en analyse en détail les applications pratiques.