Abstract
Cross-linked enzyme aggregates (CLEAs) of β-mannanase were prepared by precipitation and subsequent cross-linking. The macromolecular cross-linkers (dialdehyde starch and dextran polyaldehyde) with different molecular weight were developed instead of traditional glutaraldehyde so as to improve the activity of CLEAs toward macromolecular substrates. Scanning electron microscopy revealed that CLEAs prepared using linear dextran polyaldehyde (MW = 2000 kDa) presented a porous structure with low steric hindrance, and thus exhibited excellent activity toward macromolecular substrates, which was 16 times higher than that prepared using glutaraldehyde.
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