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CRYSTALLIZATION AND CHARACTERIZATION OF CANDIDA RUGOSA LIPASE
Rubin, Byron Jamison, Penny Harrison, David
Rubin, Byron
Jamison, Penny
Harrison, David
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Issue Date
1991
Submitted date
2024-03-13
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Abstract
A lipase isolated from the fungus Candida rugosahas beenpurified and crystallized in a form suitable for X-ray crystallographic structure determination. Several proteins with lipolytic activity having isoelectric points from 4.2 to 5.8 were separated by ion exchange chromatography.The protein having the lowestisoelectric point was crystallized from 2-methy]-2,4-pentandiol in MES bufferin the presenceof calcium (II) salts. The crystals with cell dimensions a=64.9(1) 7 b=97.2(1) A and b=175.8(2)A, grow as large colorless plates often exceeding 0.7 mm in each of two dimensions. From the diffraction pattern the apparent crystal symmetry is C222,. Experimental density determination suggests one 60,000 M,. molecule in the asymmetric unit and approximately 50% solvent by volume. Theratio unit cell volume to the molecular weightof the contents of the unit cell, Vj, is 2.3 A3/d. Diffraction is strong to a resolution of 2 A resolution and work is underway to determine the three dimensional structure of this enzyme.
Citation
Lipases : structure, mechanism and genetic engineering, 63 - 66
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Type
Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International