| Literature DB >> 17696317 |
Akifumi Kawamura1, Atsushi Harada, Kenji Kono, Kazunori Kataoka.
Abstract
Core-cross-linked polyion complex (PIC) micelles entrapping trypsin in the core were prepared by mixing trypsin and poly(ethylene glycol)-block-poly(alpha,beta-aspartic acid) in aqueous medium, followed by the introduction of glutaraldehyde cross-linkages. Trypsin incorporated into the core-cross-linked micelles showed high storage stabilities, and the initial enzymatic activity of trypsin was maintained even after standing for one week at ambient temperature. Further, stable compartmentalization of trypsin into the core-cross-linked micelles led to a unique modulation in the enzymatic functions including an improved thermal tolerability with an increased maximum reaction rate compared to native trypsin.Entities:
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Year: 2007 PMID: 17696317 DOI: 10.1021/bc070029t
Source DB: PubMed Journal: Bioconjug Chem ISSN: 1043-1802 Impact factor: 4.774