Fish sauce : the alternative solution for Pacific whiting and its by-products Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/8g84mq02m

Descriptions

Attribute NameValues
Creator
Abstract or Summary
  • Pacific whiting and its by-products were good raw materials for high quality fish sauce production. Heat stable and salt activated enzymes were responsible for autolytic activity in Pacific whiting and by-products. According to temperature profiles of raw materials at various salt concentrations, two fermentation temperatures, 35°C and 50°C, were selected and compared at 25% salt under static atmospheric condition. Higher yields and faster production rate were obtained from samples incubated at 50°C. Therefore, the apparent optimum condition for fish sauce fermentation using Pacific whiting and its by-products was at 50°C with 25% salt under static atmospheric condition. All physicochemical characteristics, except color and browning color, reached the level of commercial fish sauce within 20 days. Nitrogen contents in all samples reached the level of commercial fish sauce (16.3 g-N/mL) within 112 days. Predominant microorganisms found during fermentation were Staphylococcus, Bacillus and Micrococcus. Alpha-amino acid content appeared to be identified as a good parameter to estimate total nitrogen content during fermentation (adjusted R²=0.84). Soluble solid was a good index for protein degradation in fermentation (adjusted R²=0.71). Proteolytic activity in Pacific whiting and its by-products were investigated using hemoglobin as substrate. Specific substrates and specific inhibitors were also used to classify the types of enzymes responsible for protein degradation in fish sauce fermentation. Serine proteases, cathepsin L-like enzymes and metalloproteases were active at 50°C in whole fish. However, trypsin-like enzymes, and cathepsin L-like enzymes were responsible for protein degradation in by-products at 50°C. At 35°, whole fish was degraded by serine proteases, cathepsin B-like enzymes, trypsin-like enzymes, and metalloproteases. Cysteine proteases were mainly responsible for the degradation of proteins in by-products, and serine proteases and trypsin-like enzymes had a minor role in hydrolyzing of by-products during fermentation.
Resource Type
Date Available
Date Copyright
Date Issued
Degree Level
Degree Name
Degree Field
Degree Grantor
Commencement Year
Advisor
Academic Affiliation
Non-Academic Affiliation
Subject
Rights Statement
Peer Reviewed
Language
Digitization Specifications
  • File scanned at 300 ppi (Monochrome) using Scamax Scan+ V.1.0.32.10766 on a Scanmax 412CD by InoTec in PDF format. LuraDocument PDF Compressor V.5.8.71.50 used for pdf compression and textual OCR.
Replaces
Additional Information
  • description.provenance : Made available in DSpace on 2012-01-09T16:41:17Z (GMT). No. of bitstreams: 1 LOPETCHARATKANNAPON1999.pdf: 1306928 bytes, checksum: fc29a63d58e0939e3ee50ba7b4e47c89 (MD5) Previous issue date: 1999-06-04
  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2011-12-20T16:59:32Z (GMT) No. of bitstreams: 1 LOPETCHARATKANNAPON1999.pdf: 1306928 bytes, checksum: fc29a63d58e0939e3ee50ba7b4e47c89 (MD5)
  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2012-01-09T16:41:17Z (GMT) No. of bitstreams: 1 LOPETCHARATKANNAPON1999.pdf: 1306928 bytes, checksum: fc29a63d58e0939e3ee50ba7b4e47c89 (MD5)
  • description.provenance : Submitted by Erin Clark (ecscannerosu@gmail.com) on 2011-12-20T16:22:20Z No. of bitstreams: 1 LOPETCHARATKANNAPON1999.pdf: 1306928 bytes, checksum: fc29a63d58e0939e3ee50ba7b4e47c89 (MD5)

Relationships

Parents:

This work has no parents.

Last modified

Downloadable Content

Download PDF

Items