Isolation and Properties of Alginate Lyase from the Mid-Gut Gland of Wreath ShellTurbo cornutus
- 1 October 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 41 (10) , 1939-1946
- https://doi.org/10.1080/00021369.1977.10862789
Abstract
Alginate lyase [EC 4.2.2.3] has been purified from mid-gut gland of wreath shell. The enzyme was homogeneous as judged by SDS-polyacrylamide gel electrophoresis. A molecular weight of 32,000 was estimated by SDS-polyacrylamide gel electrophoresis. Absorption spectra of the reaction products indicated that the enzyme had lyase activity. The enzyme was most active at a pH range of about 8.8 to 9.2 and most stable at pH 5 to 6. Phosphate showed strong stabilizing and enhancing effects on the enzyme activity. Divalent cations behaved differently toward alginic acid and propylene glycol alginate, suggesting requirements for free carboxyl groups and a single glycosidic chain in the enzyme action.This publication has 7 references indexed in Scilit:
- Multiple Components of Endo-polyguluronide Lyase of Pseudomonas sp.The Journal of Biochemistry, 1977
- Substrate Specificity of Endo-polyguluronide Lyases from Pseudomonoas sp. on the Basis of Their Kinetic PropertiesThe Journal of Biochemistry, 1977
- Fine Structure of SMG Alginate Fragment in the Light of Its Degradation by Alginate Lyases of Pseudomonas sp.The Journal of Biochemistry, 1977
- Purification and properties of an alginate lyase from a marine bacteriumBiochemical Journal, 1976
- Alginic Acid Degradation by Eliminases from Abalone HepatopancreasJournal of Biological Chemistry, 1967
- Neutral Salts: The Generality of Their Effects on the Stability of Macromolecular ConformationsScience, 1964
- ALGINIC ACID METABOLISM IN BACTERIA .1. ENZYMATIC FORMATION OF UNSATURATED OLIGOSACCHARIDES AND 4-DEOXY-L-ERYTHRO-5-HEXOSEULOSE URONIC ACID1962