The muscle of shellfish, in particular shrimp, is characterized by high amounts of free amino acids especially glycine as well as proline, serine and alanine which all contribute to the overall pleasant and desirable flavour perceived. The two major proteolytic enzymes, chymotrypsin and trypsin, were used at different ratios (E/S, 0.0-0.3%), temperatures (25$ sp circ$C-45$ sp circ$C) and time of hydrolysis (1-3h) for frozen and fresh shrimp. These conditions were optimized in order to generate a product with desirable sensory and chemical characteristics. The thermal stability of chymotrypsin and trypsin were investigated, to determine the suitability of heat to stop the hydrolysis reactions at desired conditions. The results for the frozen shrimp showed that chymotrypsin was found to be inactivated after incubation for 1 min at 80$ sp circ$C while trypsin was found to be relatively heat stable. The commercial soybean trypsin inhibitor was used to inactivate trypsin. The use of both enzymes accelerate the rate of hydrolysis to some extent. Higher free amino acids yield for glycine, serine, and proline were obtained for chymotrypsin-treated hydrolysates. (Abstract shortened by UMI.)
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.61080 |
| Date | January 1992 |
| Creators | Nayeri, Gita |
| 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: 001283002, proquestno: AAIMM74678, Theses scanned by UMI/ProQuest. |
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