title: [Water binding of adsorptive immobilized lipases].
abstract: It is supposed that not only the total water content of lipase preparations but more their state of water binding is of technological importance in enzymatic interesterification reactions in systems nearly free from water. The isotherms at 65 degrees C of two microbial lipases immobilized on various adsorbents as well as different adsorbents themselves are shown. The water binding capacity in the range of water content of technological interest decreases from the anion exchange resin Amberlyst A 21 via nonpolar adsorbent Amberlite XAD-2 to kieselguhr Celite 545. It is demonstrated that water binding by lipases is depending on temperature but is also affected by adsorptive immobilization. Adsorptive immobilized lipases show hysteresis, which is very important for preparing a definite water content of the enzyme preparations.
authors.affiliation: Wissenschaftsbereich Lebensmittelchemie, Humboldt-Universität zu Berlin, DDR.
authors.forename: S
authors.initials: S
authors.lastname: Loose
authors.forename: D
authors.initials: D
authors.lastname: Meusel
authors.forename: A
authors.initials: A
authors.lastname: Muschter
authors.forename: B
authors.initials: B
authors.lastname: Ruthe
mesh_terms: D000327:Adsorption; D004800:Enzymes, Immobilized / Q000378:metabolism*; D008049:Lipase / Q000378:metabolism*; D009089:Mucor / Q000201:enzymology*; D012233:Rhizopus / Q000201:enzymology*; D013696:Temperature; D014867:Water / Q000378:metabolism*
chemical_list: D004800:Enzymes, Immobilized; D014867:Water; D008049:Lipase
vernacular_title: Zur Wasserbindung adsorptiv immobilisierter Lipasen.