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Core-cross-linked polyion complex (PIC) micelles effectively stabilized entrapped trypsin, maintaining its activity and enhancing thermal stability. This novel formulation improves enzyme function and storage, offering potential for biotechnological applications.

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Area of Science:

  • Biotechnology
  • Polymer Science
  • Enzyme Engineering

Background:

  • Enzyme stability and controlled release are critical for biotechnological applications.
  • Polyion complex (PIC) micelles offer a versatile platform for encapsulating biomolecules.
  • Improving enzyme thermal tolerance and maintaining activity under storage are significant challenges.

Purpose of the Study:

  • To develop core-cross-linked PIC micelles for entrapping and stabilizing trypsin.
  • To investigate the impact of micelle encapsulation on trypsin's enzymatic activity, storage stability, and thermal tolerance.

Main Methods:

  • Preparation of core-cross-linked PIC micelles by mixing trypsin with poly(ethylene glycol)-block-poly(alpha,beta-aspartic acid) and subsequent glutaraldehyde cross-linking.
  • Assessment of trypsin storage stability at ambient temperature over one week.
  • Evaluation of enzymatic activity and thermal tolerability of encapsulated trypsin compared to native trypsin.

Main Results:

  • Successfully prepared core-cross-linked PIC micelles encapsulating trypsin.
  • Trypsin within the micelles exhibited high storage stability, retaining initial activity after one week.
  • Encapsulated trypsin demonstrated improved thermal tolerability and an increased maximum reaction rate compared to native trypsin.

Conclusions:

  • Core-cross-linked PIC micelles provide a robust system for stabilizing trypsin.
  • Encapsulation modulates trypsin's enzymatic functions, enhancing its stability and thermal performance.
  • This approach holds promise for developing more stable and functional enzyme formulations.