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Literature summary for 3.4.21.1 extracted from

  • Cummings, C.; Murata, H.; Koepsel, R.; Russell, A.J.
    Dramatically increased pH and temperature stability of chymotrypsin using dual block polymer-based protein engineering (2014), Biomacromolecules, 15, 763-771.
    View publication on PubMed

Application

Application Comment Organism
synthesis construction of three different molecular weight multimodal temperature-responsive chymotrypsin-poly(sulfobetaine methacrylamide)-block-poly(N-isopropylacrylamide) protein-polymer conjugates that respond structurally to both low and high temperature. In the block copolymer grown from the surface of the enzyme, upper critical solution temperature phase transition is dependent on the chain length of the polymers in the conjugates, whereas lower critical solution temperature phase transition is independent of molecular weight. Each protein conjugate shows temperature dependent changes in substrate affinity and productivity when assayed from 0 to 40°C. The conjugates show higher stability to harsh conditions, including temperature, low pH, and protease degradation. The modified enzyme is active for over 8 h in the presence of a stomach protease at pH 1.0 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P00766
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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Bos taurus
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pancreas
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Bos taurus
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