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.
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