{'fraction_non_alphanumeric': 0.032588454376163874, 'fraction_numerical': 0.017690875232774673, 'mean_word_length': 5.935483870967742, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 1, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Comparison of Chitin and Amberlite IRA‐938 for α‐Galactosidase Immobilization

Watermelon α‐galactosidase (EC 3.2.1.22) was immobilized on a natural (chitin) and a synthetic anion‐exchange (Amberlite IRA‐938) support by covalent coupling methods. The procedure entails the activation of supports with 1,1′‐carbonyldiimidazole (CDI), followed by immobilization of the enzyme on to these supports without and with a spacer arm; γ‐aminobutyric acid (GABA). Optimization of activation was performed by changing the CDI concentrations and coupling efficiencies. The comparison of two immobilization techniques for both chitin and Amberlite IRA‐938 was made by comparing different enzyme concentrations against enzyme activity yield. Furthermore, the storage stability of the immobilized enzymes was also investigated and chitin immobilized α‐galactosidase was found to be better. Although the activity yield of immobilized enzymes were the same for both supports, the short storage stability of immobilized enzyme on Amberlite IRA‐938 is currently a drawback to its applications.