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- W2078396098 abstract "The mechanism of irreversible thermoinactivation of α-chymotrypsin in buffer medium, dimethylformamide, dimethylsulfoxide/buffer and reverse micelles was studied. Experiments for the enzyme thermoinactivation in the different systems were accompanied by studies on protein structure alterations. The formation of free SH groups was followed during the stability tests. This formation is due to the cleavage of the enzyme primary structure which leads to small peptides. These were identified by SDS-PAGE, in the case of the buffer medium, and also by HPLC in the three other systems. An increase of SH groups with the residence time of the enzyme in the buffer and organic solvent/buffer system was observed. This was corroborated by the disappearance of the electrophoresis bands of the protein and also by HPLC analysis. In the latter technique, the peaks corresponding to α-chymotrypsin disappeared with the concomitant appearance of small peaks in the chromatogram. For the enzyme encapsulated in reverse micelles, the formation of free SH groups was not detected and the HPLC analysis revealed that the protein peak stayed intact during the residence time in this system. The thermoinactivation of chemically modified α-chymotrypsin by the introduction of dianhydride pyromellitic on the Lys residues of the protein was also studied in some of the systems. The results showed that the chemical modification stabilized the enzyme when the system used was buffer or organic solvent mixed with buffer being this stabilization partially due to a slower process of cysteine bond cleavage." @default.
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- W2078396098 date "1999-09-01" @default.
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- W2078396098 title "Irreversible thermoinactivation of α-chymotrypsin in buffer and water miscible organic solvent. Comparison with a reverse micellar system" @default.
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- W2078396098 doi "https://doi.org/10.1016/s1381-1177(99)00029-6" @default.
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