References
- Aleshin A, Golubev A, Firsov LM, Honzatko RB. Crystal structure of glucoamylases from Aspergillus awamori var. X100 to 2.2 Å resolution. J Bio Chem 1992; 267: 19291–19298
- Ashikari T, Nakamura N, Tanaka Y, Kiuchi N, Shibano Y, Tanaka T, Amachi T, Yoshizumi H. Rhizopus raw-starch-degrading glucoamylase: Its cloning and expression in yeast. Agric Biol Chem 1986; 50: 957–964
- Chiba, S. 1995. “Enzyme chemistry and molecular biology of amylase and related enzymes,”, ed. by The Amylase Research Society of Japan. Boca Raton, Ann Arbor,. London, Tokyo: CRC Press. 68–82.
- Chiba S. Molecular mechanism in α-glucosidase and glucoamylase. Biosci Biotech Biochem 1997; 61: 1233–1239
- Coutinho PM, Reilly PJ. Glucoamylase structural, functional, and evolutionary relationships. Protein Stru Func Gene 1997; 29: 334–347
- Goto M, Tanigava K, Kanlayakrit W, Hayashida S. The molecular mechanism of binding of glucoamylases I from Aspergillus awamori var. kawachi to cyclodextrin and raw starch. Biosci Biotech Biochem 1994; 58: 49–54
- Hiromi K, Ohnishi M, Tanaka A. Subsite structure and ligand binding mechanism of glucoamylase. Mol Cell Biochem 1983; 51: 79–95
- Janssen AEM, Sjursnes BJ, Vakurov AV, Halling PJ. Kinetics of lipase-catalysed esterification in organic media: correct model and solvent effects on parameters. Enzym Microbiol Technol 1999; 24: 463–470
- Kiran KR, Divakar S. Enzyme inhibition by p-cresol and lactic acid in lipase-mediated synthesis of p-cresyl acetate and steroyl lactic acid: a kinetic study. World J Microb Biotechnol 2002; 18: 707–712
- Laroute V, Willemot RM. Glucoside synthesis by glucoamylase or β-glucosidase in organic solvents. Biotechnol Lett 1992; 14: 169–174
- Marty A, Chulalaksananukul W, Willemot RM, Condoret JS. Kinetics of lipase-catalysed esterification in supercritical CO2. Biotechnol Bioeng 1992; 39: 273–280
- Ohnishi M, Hiromi K. Binding of maltose to Rhizopus niveus glucoamylases in the pH range where the catalytic carboxyl groups are ionized. Carbohydr Res 1989; 195: 138–144
- Segel IH. Enzyme kinetics-behavior and analysis of rapid equilibrium and steady-state enzyme systems. A Wiley–Interscience Publication. ISBN 1993; 0-471-30309-7: 826–829
- Sierks MR, Ford C, Reilly PJ, Svensson B. Catalytic mechanism of fungal glucoamylases as defined by mutagenesis of Asp 176, Glu179, and Glu180 in the enzyme from Aspergillus awamori. Protein Engg 1990; 3: 193–198
- Stoffer B, Aleshin AE, Firsov LM, Svensson B, Honzatko RB. Refined structure for the complex of D-gluco-dihydroacarbose with glucoamylases from Aspergillus awamori var. X100 to 2.2 Å resolution: dual conformation for extended inhibitors bound to the active site of glucoamylases. FEBS Lett 1995; 358: 57–61
- Sumner JB, Sisler EB. A simple method for blood sugar. Arch Biochem 1944; 4: 333–336
- Svensson B, Clarke AJ, Svendsen I, Moller H. Identification of carboxylic acid residues in glucoamylases G2 from Aspergillus niger that participate in catalysis and substrate binding. Eur J Biochem 1990; 188: 29–38
- Tanaka A, Yamashita T, Ohnishi M, Hiromi K. Steady-state and transient kinetic studies on the binding of maltooligosaccharides to glucoamylases. J Biochem 1983; 93: 1037–1043
- Yadav GD, Lathi PS. Synthesis of citronellol laurate in organic media catalyzed by immobilized lipases: kinetic studies. J Mol Catal B: Enzym 2004; 27: 113–119