Modeling of the simultaneous hydrolysis-ultrafiltration of whey permeate by a thermostable β-galactosidase from Aspergillus niger

Hatzinikolaou, DG; Katsifas, E; Mamma, D; Karagouni, AD; Christakopoulos, P; Kekos, D

dc.contributor.author	Hatzinikolaou, DG	en
dc.contributor.author	Katsifas, E	en
dc.contributor.author	Mamma, D	en
dc.contributor.author	Karagouni, AD	en
dc.contributor.author	Christakopoulos, P	en
dc.contributor.author	Kekos, D	en
dc.date.accessioned	2014-03-01T01:22:46Z
dc.date.available	2014-03-01T01:22:46Z
dc.date.issued	2005	en
dc.identifier.issn	1369-703X	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/16647
dc.subject	β-Galactosidase	en
dc.subject	Hydrolysis	en
dc.subject	Kinetic parameters	en
dc.subject	Modeling	en
dc.subject	Process integration	en
dc.subject	Ultrafiltration	en
dc.subject	Whey	en
dc.subject.classification	Biotechnology & Applied Microbiology	en
dc.subject.classification	Engineering, Chemical	en
dc.subject.other	Activation energy	en
dc.subject.other	Computer simulation	en
dc.subject.other	Glucose	en
dc.subject.other	Hydrolysis	en
dc.subject.other	pH effects	en
dc.subject.other	Plants (botany)	en
dc.subject.other	Purification	en
dc.subject.other	Ultrafiltration	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	Energy sources	en
dc.subject.other	Michaelis-Menten kinetics	en
dc.subject.other	Whey permeate	en
dc.subject.other	Enzyme kinetics	en
dc.subject.other	beta galactoside	en
dc.subject.other	fungal enzyme	en
dc.subject.other	galactose	en
dc.subject.other	lactose	en
dc.subject.other	article	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	computer simulation	en
dc.subject.other	controlled study	en
dc.subject.other	culture medium	en
dc.subject.other	enzyme inhibition	en
dc.subject.other	enzyme kinetics	en
dc.subject.other	enzyme stability	en
dc.subject.other	fungal strain	en
dc.subject.other	fungus growth	en
dc.subject.other	hydrolysis kinetics	en
dc.subject.other	mathematical model	en
dc.subject.other	Michaelis constant	en
dc.subject.other	nonhuman	en
dc.subject.other	pH measurement	en
dc.subject.other	priority journal	en
dc.subject.other	supernatant	en
dc.subject.other	thermostability	en
dc.subject.other	ultrafiltration	en
dc.subject.other	validation process	en
dc.subject.other	whey	en
dc.subject.other	wild type	en
dc.subject.other	Aspergillus niger	en
dc.subject.other	Triticum aestivum	en
dc.title	Modeling of the simultaneous hydrolysis-ultrafiltration of whey permeate by a thermostable β-galactosidase from Aspergillus niger	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.bej.2005.02.011	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.bej.2005.02.011	en
heal.language	English	en
heal.publicationDate	2005	en
heal.abstract	A wild type strain of Aspergillus niger, denoted as BTL, produced elevated levels of P-galactosidase when grown in a low cost medium that contained wheat bran as the sole carbon and energy source. The enzyme was collected, concentrated and partially purified from the culture supernatant. Its kinetic and stability properties were thoroughly examined towards its potential use for the hydrolysis of acid whey permeate lactose. The P-galactosidase of A. niger BTL showed increased pH and thermal stability, with activation energy for the first order deactivation constant equal to 180 kJ/mol at pH 3.5. Lactose hydrolysis by the enzyme was described by Michaelis-Menten kinetics with competitive inhibition only from galactose. An integrated process, concerning the simultaneous hydrolysis-ultrafiltration of whey lactose that incorporated the specific kinetic properties of the P-galactosidase was developed and modeled. The model proved very successful in predicting the behavior of a continuous laboratory hydrolysis-ultrafiltration set up, specifically designed for that purpose. The validated model was finally used in a number of computer simulations in order to investigate the effect of the various process parameters on the overall system performance. (c) 2005 Elsevier B.V. All rights reserved.	en
heal.publisher	ELSEVIER SCIENCE SA	en
heal.journalName	Biochemical Engineering Journal	en
dc.identifier.doi	10.1016/j.bej.2005.02.011	en
dc.identifier.isi	ISI:000229352600009	en
dc.identifier.volume	24	en
dc.identifier.issue	2	en
dc.identifier.spage	161	en
dc.identifier.epage	172	en