A collagenolytic enzyme fraction was isolated from the hepatopancreas of the lobster (Homarus americanus) and semi-purified by the successive steps of acetone precipitation, ammonium sulfate fractionation, ion exchange chromatography on Mono Q column, followed by gel filtration on a Superdex 75 column or by preparative isoelectric focusing using a Rotofor cell. / Semi-purified collagenase fractions from the lobster hepatopancreas was electrophoresed in polyacrylamide gels both in the presence or absence of SDS, and shown to have molecular weights ranging from 15,000-66,000. The enzymatically active peak 1 fraction from the isoelectric focusing step in the Rotofor cell migrated as a single band in 12% polyacrylamide gel with few light protein bands. / The pH-activity data indicated that the collagenase fraction had two pH optima for the hydrolysis of native collagen, one at pH 4 and the other between pH 7-8. / The temperature-activity data for the hydrolysis of native collagen indicated the lobster enzyme exhibited two temperature optima--a minor one at 25$ sp circ$C and a more pronounced one between 40$ sp circ$C and 50$ sp circ$C.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.60654 |
| Date | January 1992 |
| Creators | Chen, Yizhu |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Food Science and Agricultural Chemistry.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001287514, proquestno: AAIMM74490, Theses scanned by UMI/ProQuest. |
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