Increased thermostability of Asn182 --> Ala mutant Aspergillus awamori glucoamylase.

@article{Reilly1994IncreasedTO,
  title={Increased thermostability of Asn182 --> Ala mutant Aspergillus awamori glucoamylase.},
  author={Peter J. Reilly and H. M. Chen and Ufuk Bakir and Clark Ford},
  journal={Biotechnology and bioengineering},
  year={1994},
  volume={43 1},
  pages={101-5}
}
Asn182 --> Ala Aspergillus awamori glucoamylase expressed in Saccharomyces cerevisiae had a first-order thermodeactivation coefficient 40% that of wild-type glucoamylase at pH 4.5 between 60 degrees and 65 degrees C, caused by the elimination of an Asn-Gly sequence subject to deamidation and eventual chain breakage. Above 70 degrees C, and at pHs 3.5 and 5.5, thermodeactivation coefficients of wild-type and mutant enzymes were roughly equal, because the fastest deactivation mechanism was no… CONTINUE READING

From This Paper

Topics from this paper.

Similar Papers

Loading similar papers…