Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
36689 | Process Biochemistry | 2005 | 4 Pages |
Abstract
Bovine pancreatic α-chymotrypsin was chemically modified with mono-6-amino-6-deoxy-β-cyclodextrin. The modified enzymes contained about 2 mol of oligosaccharide per mol of protein and retained full proteolytic and esterasic activity. The optimum temperature for α-chymotrypsin was increased by 5 °C and its thermostability was enhanced by about 6 °C after modification. The glycosylated enzyme turned markedly more resistant to thermal inactivation at 50 °C and retained 70% of the original activity when pre-incubated at pH 9.0 for 180 min as compared to a complete inactivation seed for the unmodified protease.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Michael Fernández, Alex Fragoso, Roberto Cao, Reynaldo Villalonga,