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Proteolytic enzymes like trypsin prevent yeast invertase reactivation. However, purified reactivated invertase regains its original activity, unaffected by these enzymes once active.

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Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Yeast invertase is crucial for sucrose hydrolysis.
  • Understanding enzyme inactivation and reactivation is vital for biochemical applications.

Purpose of the Study:

  • To investigate factors affecting acid-inactivated yeast invertase reactivation.
  • To determine the effect of proteolytic enzymes and foreign proteins on invertase activity.

Main Methods:

  • Acid inactivation of yeast invertase.
  • Assessing reactivation in the presence of various proteins (proteolytic and non-enzymatic).
  • Enzyme activity assays at pH 3.0.

Main Results:

  • Proteolytic enzymes (trypsin, pepsin, chymotrypsin) inhibited invertase reactivation.
  • Non-enzymatic proteins showed variable effects on reactivation.
  • Native invertase resisted digestion by trypsin and chymotrypsin.
  • Reactivated invertase exhibited original activity, including acceleration by foreign proteins at pH 3.0.
  • Proteolytic enzymes did not affect already reactivated invertase but blocked further reactivation.

Conclusions:

  • Proteolytic enzymes interfere with the reactivation process of acid-inactivated yeast invertase.
  • The structural integrity of native invertase confers resistance to certain proteases.
  • Reactivated invertase recovers its characteristic functional properties.