Related Experiment Video
Updated: Jan 17, 2026

Surface Functionalization of Metal-Organic Frameworks for Improved Moisture Resistance
Published on: September 5, 2018
Metal-Organic Framework-Encapsulated Transglutaminase Biocatalyst: Enhancing Operational Stability and Freshness
Jiao Yu1, Jie Chen2, Mengqing Liu1
1Anhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases and Key Laboratory of Biomedicine in Gene Diseases and Health of Anhui Higher Education Institutes, College of Life Sciences, Anhui Normal University, Wuhu 241000, Anhui, China.
This study developed an immobilized enzyme, transglutaminase (TG) within a metal-organic framework (HKUST-1), to create enhanced biodegradable food packaging films. The new films show improved stability and effectively reduce fruit and vegetable spoilage.
Area of Science:
- Materials Science
- Biotechnology
- Food Science
Background:
- Enzymatically cross-linked food packaging films using transglutaminase (TG) offer biodegradability and non-toxicity but face enzyme instability and reusability issues.
- Natural enzymes like TG are fragile, limiting their practical application in scalable eco-friendly packaging fabrication.
- Developing robust and reusable enzyme systems is crucial for advancing sustainable food packaging solutions.
Purpose of the Study:
- To immobilize transglutaminase (TG) within HKUST-1 (a copper-based metal-organic framework) using in situ biomineralization with ultrasound assistance.
- To utilize the immobilized enzyme (TG@HKUST-US) for cross-linking zein protein to prepare advanced biodegradable packaging films.
- To evaluate the enhanced stability, reusability, and performance of the TG@HKUST-US immobilized enzyme system in food packaging applications.
Main Methods:
- Immobilization of transglutaminase (TG) within HKUST-1 using in situ biomineralization and ultrasound.
- Cross-linking of zein protein using the immobilized TG@HKUST-US for film preparation.
- Assessment of enzymatic activity, thermal and pH stability, solvent tolerance, water holding capacity, and fruit/vegetable preservation efficacy.
- Evaluation of film toxicity and copper ion leaching levels.
Main Results:
- TG@HKUST-US exhibited 140% higher enzymatic activity than free TG, with improved thermal and pH stability.
- The immobilized enzyme demonstrated enhanced stability in organic solvents and improved pH tolerance.
- Zein films incorporating TG@HKUST-US showed superior water holding capacity, significantly reducing weight loss in apples (41.5%), pears (34.1%), and lettuce (29.5%).
- Films prepared using the reusable TG@HKUST-US system were non-toxic, with copper ion leaching below safety thresholds.
Conclusions:
- The developed TG@HKUST-US system offers a novel and effective strategy for immobilizing enzymes for food packaging applications.
- This approach enhances enzyme stability, reusability, and catalytic efficiency, paving the way for advanced biodegradable films.
- The study establishes a sustainable platform for producing eco-friendly food packaging with improved preservation capabilities.
More Related Videos
10:27Preparation of Highly Porous Coordination Polymer Coatings on Macroporous Polymer Monoliths for Enhanced Enrichment of Phosphopeptides
Published on: July 14, 2015
09:27Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016