The decay of the fluorescence anisotropy of tryptophan residues in fungal lipase fromHumicola lanuginosa |
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Authors: | A Stobiecka S Wysocki |
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Institution: | (1) The Institute of General Food Chemistry, Technical University, Stefanowskiego 4/10, 90-924 Ęódź, Poland |
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Abstract: | Pulse nanosecond fluorescence anisotropy decay has been used to study the mobility of tryptophan residues within fungal lipase
fromHumicola lanuginosa. The decay of emission anisotropy of protein in native, inhibited and mutated form has been investigated in buffered water
and 50% v/v glycerol solutions. The rotational motions of the lipase were analyzed in terms of two different kinetic models.
It was found that the fluorescence emission anisotropy decay can best be desribed with two rotational correlation times: 0.63
and 5.45 ns in water and 0.98 and 10.70 ns and in 50% v/v glycerol solution. Using the same experimental conditions the decay
of inhibited and mutatedH. lanuginosa lipase showed a similar biexponential character. These results are interpreted in terms of local or segmental motion arising
from a mass of about 1083 daltons which corresponds to the ‘lid’-helix fragment of the enzyme. |
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