Thermostabilization of Ovalbumin by an Alkaline Treatment : Examination for the Possible Implications of an Altered Serpin Loop Structure(Food & Nutrition Science)

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Ovalbumin, a member of the serpin superfamily, is transformed via an intermediate state into a noncleaved, thermostabilized form (S-ovalbumin) during either the storage of unfertilized eggs or development of fertilized eggs ; essentially the same thermostabilization also occurs upon in vitro incubation of isolated ovalbumin under alkaline conditions. To investigate the implications of a partial insertion of the α-helical serpin loop into β-sheet A that has been proposed as a conformational mechanism for S-ovalbumin production, we examined the thermostabilization process of ovalbumin with different loop structures. When the thermostabilization processes were compared for the intact, P1-P1'-cleaved and P1-P1'/P8-P7-cleaved forms of egg white ovalbumin, both the rates for the conversion from the native to intermediate and from the intermediate to S-ovalbumin were almost indistinguishable among the three protein forms. Furthermore, the fully loop-inserted form of recombinant ovalbumin mutant R339T that had been thermostabilized by P1-P1' cleavage with Tm values from 72 to 88℃ was further thermostabilized by an alkaline treatment, yielding a final product (loop inserted S-ovalbumin) with a Tm value of 93℃. No significant difference was found between native ovalbumin and S-ovalbumin in respect of the rate of proteolytic cleavage of the loop by elastase and subtilisin. These data strongly suggest that S-ovalbumin is produced by a mechanism other than that of the partial loop insertion model.
社団法人日本農芸化学会の論文
2003-04-23

Thermostabilization of Ovalbumin by an Alkaline Treatment : Examination for the Possible Implications of an Altered Serpin Loop Structure(Food & Nutrition Science)

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