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Summary

A detailed study has been made of the kinetics of inactivation of invertase at 25°C. in acid media. The results indicate the existence of two processes, one of them being very fast and coming up at comparatively high pH values and the other coming up at lower pH.

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References

  1. Doss and SaraswatProc. Ind. Acad. Sci., 1952,36, 343.

    Google Scholar 

  2. SaraswatIbid.,.

    Google Scholar 

  3. Euler and LaurinZ. Physiol. Chem., 1919,108, 64.

    Google Scholar 

  4. Gorter and DieuProc. Kon. Ned. Akad. V. Wetens K., 1947,50, 329.

    Google Scholar 

  5. Kraut and WenzelZ. Physiol. Chem., 1925,142, 71.

    Google Scholar 

  6. Zerban and BrowneSugar Analysis, 3rd Edition, p. 646.

  7. Ibid., Zerban and BrowneSugar Analysis, 3rd Edition, p. 836.

  8. Ibid., Zerban and BrowneSugar Analysis, 3rd Edition, p. 1235, Table 19 A.

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Doss, K.S.G., Saraswat, H.C. Kinetics of inactivation of invertase. Proc. Indian Acad. Sci. 37, 63–67 (1953). https://doi.org/10.1007/BF03052859

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  • DOI: https://doi.org/10.1007/BF03052859

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