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Cold adaptation, ca2+ dependency and autolytic stability are related features in a highly active col...

Cold adaptation, ca2+ dependency and autolytic stability are related features in a highly active col...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1430420667

Cold adaptation, ca2+ dependency and autolytic stability are related features in a highly active cold-adapted trypsin resistant to autoproteolysis engineered for biotechnological applications

About this item

Full title

Cold adaptation, ca2+ dependency and autolytic stability are related features in a highly active cold-adapted trypsin resistant to autoproteolysis engineered for biotechnological applications

Publisher

United States: Public Library of Science

Journal title

PloS one, 2013-08, Vol.8 (8), p.e72355-e72355

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Pig trypsin is routinely used as a biotechnological tool, due to its high specificity and ability to be stored as an inactive stable zymogen. However, it is not an optimum enzyme for conditions found in wound debriding for medical uses and trypsinization processes for protein analysis and animal cell culturing, where low Ca(2+) dependency, high act...

Alternative Titles

Full title

Cold adaptation, ca2+ dependency and autolytic stability are related features in a highly active cold-adapted trypsin resistant to autoproteolysis engineered for biotechnological applications

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1430420667

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1430420667

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0072355

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