Enzymes in Food Technology - Introduction

Enzymes in Food Technology: Second Edition

Volumn , Issue , 2009, Pages 1-17

  van Oort, Maarten ^a  

^a AB Mauri   (Netherlands)

Author keywords

Enzyme (protease) fermentation of Bacillus licheniformis; Enzyme function in nature; Enzyme kinetics describing, predicting and calculating how enzymes bind substrates; Enzyme workings lowering activation energy in reactions; Enzymes proteins enhancing or accelerating chemical reactions; Enzymes exhibiting absolute specificity; Factors affecting enzyme activity; Industrial success of enzymes benefits offerred in comparison with chemicals; International Union of Biochemistry (IUB); Nomenclature of enzymes

Indexed keywords

ACTIVATION ENERGY; BACTERIOLOGY; CALCIFICATION (BIOCHEMISTRY); ENZYME KINETICS; INDICATORS (CHEMICAL); INDUSTRIAL CHEMICALS;

BACILLUS LICHENIFORMIS; ENZYME FUNCTIONS; INTERNATIONAL UNION OF BIOCHEMISTRY (IUB); TECHNOLOGY INTRODUCTIONS;

ENZYME ACTIVITY;

EID: 84902217910     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781444309935.ch1     Document Type: Editorial

References (19)

1. Smith, A.D., Datta, S.P., Smith, G.H., Campbell, P.N., Bentley, R. and McKenzie, H.A. (eds) (1997) Oxford Dictionary of Biochemistry and Molecular Biology. Oxford University Press, Oxford.
2. Lilley, D. (2005). Structure, folding and mechanisms of ribozymes. Current Opinion in Structural Biology 15(3), 313-323.
3. IUB homepage, http://www.chem.qmul.ac.uk/iubmb/
4. Hunter, T. (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80(2), 225-236.
5. Berg, J.S., Powell, B.C. and Cheney, R.E. (2001) A millennial myosin census. Molecular Biology of the Cell 12(4), 780-794.
6. Mackie, R.I. and White, B.A. (1990) Recent advances in rumen microbial ecology and metabolism: potential impact on nutrient output. Journal of Dairy Science 73(10), 2971-2995.
7. Anfinsen, C.B. (1973) Principles that govern the folding of protein chains. Science 181(96), 223-230.
8. Jaeger, K.E. and Eggert, T. (2004) Enantioselective biocatalysis optimized by directed evolution. Current Opinion in Biotechnology 15(4), 305-313.
9. Fischer, E. (1894) Einfluss der configuration auf die wirkung der enzyme. Berichte der Deutschen Chemischen Gesellschaft 27, 2985-2993.
10. Koshland, D.E. (1958) Application of a theory of enzyme specificity to protein synthesis. Proceedings of the National Academy of Sciences of the United States of America 44(2), 98-104.
11. Vasella, A., Davies, G.J. and Bohm, M. (2002) Glycosidase mechanisms. Current Opinion in Chemical Biology 6(5), 619-629.
12. Boyer, R. (2002) Concepts in Biochemistry, 2nd edn (in English). John Wiley & Sons, Inc., New York, pp. 137-138.
13. Arrhenius, S. (1899) On the theory of chemical reaction velocity. Zeitschrift für Physikalische Chemie 28, 317.
14. Henri, V. (1902) Theorie generale de l'action de quelques diastases. Comptes Rendus Hebdomadaires Academie de Sciences de Paris 135, 916-919.
15. Sørensen, P.L. (1909) Enzymstudien II. Über die Messung und Bedeutung der Wasserstoffionenkonzentration bei enzymatischen Prozessen. Biochemische Zeitschrift 21, 131-304.
16. Michaelis, L. and Menten, M. (1913) Die Kinetik der Invertinwirkung. Biochemische Zeitschrift 49, 333-369.
17. Briggs, G.E. and Haldane, J.B.S. (1925) A note on the kinetics of enzyme action. Biochemical Journal 19, 338-339.
18. Wagner, A.F. and Folkers, K.A. (1975) Vitamins and Coenzymes. Interscience Publishers, New York.
19. BRENDA Enzyme Information Database, http://www.brenda-enzymes.info/