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Substrate Specifity Of Porcine Pancreatic Lipase Studied In Terms Of The Steady-State Kinetics Binding And Rate Constants

Valmsen, Karin
; 
Lookene, Aivar
; 
Sikk, Peeter
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Issue Date
1991
Submitted date
2024-03-20
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Abstract
The steady-state kinetics binding constants have been rarely determined for emulsified lipase substrates since the apparent Michaelis constant has the dimension of the emulsion surface area in this case [1,2] which typically could not be determined precisely. On the other hand, only a combination of binding and rate parameters could be determined in experiments with substrate monolayers [3,4], and the range of suitable substratesis strictly limited in these experiments due to requirements on the stability of monolayers, productsolubility, etc. [4]. In this paper we review data on the substrate specificity of porcine pancreatic lipase on emulsified triacylglycerolsubstrates studied in terms of the steady-state binding and rate constants in the assay system lipase/colipase/micellar NaTDC'/-triacylglycerol emulsion’.
Citation
Lipases : structure, mechanism and genetic engineering, 173 - 181
Affiliation
Institute of Chemical Physics and Biophysics of the Estonian Academy of Siences P.O. Box 670, 200026 Tallinn, Estonia / USSR
Publisher
GBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweig
Journal
Lipases : structure, mechanism and genetic engineering, 1991
URI
http://hdl.handle.net/10033/623714
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Book chapter
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International
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