Abstract
The thermal and pH stability of "beta-benzyme", an artificial chymotrypsin based on beta-cyclodextrin, has been studied and compared with the stability of real chymotrypsin. Artificial chymotrypsin is vastly superior to real chymotrypsin with regard to both temperature and pH stability. The reasons for this increased stability are discussed.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Schachman H. K., Edelstein S. J. Ultracentrifuge studies with absorption optics. IV. Molecular weight determinations at the microgram level. Biochemistry. 1966 Aug;5(8):2681–2705. doi: 10.1021/bi00872a029. [DOI] [PubMed] [Google Scholar]
- Tsukada H., Blow D. M. Structure of alpha-chymotrypsin refined at 1.68 A resolution. J Mol Biol. 1985 Aug 20;184(4):703–711. doi: 10.1016/0022-2836(85)90314-6. [DOI] [PubMed] [Google Scholar]
- Wu H. L., Lace D. A., Bender M. L. Elimination of cannibalistic denaturation by enzyme immobilization or inhibition. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4118–4119. doi: 10.1073/pnas.78.7.4118. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wu H. L., Wastell A., Bender M. L. Ageing of alpha-chymotrypsin: Cannibalistic and hydroxide ion reactions. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4116–4117. doi: 10.1073/pnas.78.7.4116. [DOI] [PMC free article] [PubMed] [Google Scholar]