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Rheological and spectroscopic characterization of surimi under various comminuting and heating conditions

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dc.contributor.advisor Park, Jae W.
dc.creator Poowakanjana, Samanan
dc.date.accessioned 2012-11-20T18:53:25Z
dc.date.available 2012-11-20T18:53:25Z
dc.date.copyright 2012-11-12
dc.date.issued 2012-11-12
dc.identifier.uri http://hdl.handle.net/1957/35124
dc.description Graduation date: 2013 en_US
dc.description.abstract Optimization of comminuting and heating conditions for surimi gel preparation obtained from three fish species: Alaska pollock (AP) (Theragra chalcogramma), Pacific whiting (PW) (Merluccius productus), and threadfin bream (TB) (Nemipterus spp.) was the focus of this study. Three parameters during comminution were separately evaluated: chopping time, chopping temperature, and salting time. Results from fracture gel analysis suggested a strong relation between the fish's environmental habitat and optimal final chopping temperature. Extending chopping time to 15 min under strictly controlled temperature at 0 °C was preferable for cold water fish AP surimi. Even though high chopping temperature (20 °C) for a shorter time (12 min) surprisingly resulted in strong gel texture similar to that of 0 °C for 15 min, high chopping temperature should not be employed for AP surimi. AP could set as a gel at this temperature within a shorter time in a holding tank which could subsequently cause a problem when extruded on the cooking belt. Temperate water fish Pacific whiting, demonstrated its maximum gel strength when chopped at 15-20 °C. The optimum comminution condition for warm water fish threadfin bream surimi was to chop the surimi until the paste temperature reached between 25-30 °C. Prolongation of chopping once the surimi hit its threshold (optimum) temperature diminished the quality of the resulting protein gel. Cooling system connected to the chopping bowl is strongly recommended as it will allow the comminution process to be extended as long as possible until the surimi paste reaches its target temperature. Raman spectroscopy disclosed the different level of protein unfolding based on secondary structure of α-helix and β-sheet during various comminuting conditions. Unfolding of protein was facilitated by increased chopping temperature to a greater degree than extended chopping time. Extending chopping could denature the light meromyosin structure as it could not form a semi gel-like structure at temperatures between 32-40 °C. Protein solubility of surimi paste in salt solution always decreased with prolonged chopping time. The decrease rate accelerated with increased chopping temperature. The formation of disulfide interchange gradually took place during chopping as observed from Raman spectroscopy. Also the surface hydrophobicity increased with extended chopping time. However, gel strength behaved differently according to the various chopping conditions indicating the lack of its relationship between salt soluble protein, disulfide formation, and surface hydrophobicity to gel strength. During extending chopping time, not only more mechanical force is applied to unfold protein structure, but proteins also have longer time to be extracted more by salt. Addition of salt at a different time during chopping process was therefore conducted using threadfin bream surimi due to its higher thermostability. Extending chopping time without salt followed by salt addition at the last step resulted in lower gel texture compared to the conventional chopping protocol where salt is always added at the early stage of comminution. Mechanical chopping could unfold protein structure; however, proteins, rather than staying solubilized, would precipitate and form a randomized structure under the chopping condition without salt. The heating condition greatly affected the gelation and rheological properties of AP surimi. The highest elastic modulus was obtained with the slowest heating rate at 1 °C/min. Increased heating rate did not only shorten the time for proteins to unfold and form a well-organized network, it also interfered with the protein network through the vibration of water molecules as phase angle increased. This suggested that AP surimi gained more viscous properties and failed to form an elastic gel. Adjusting moisture content along with applying various frequencies did not alter the pattern of G' formation when paste was heated at different heating rates. AP surimi favored the slow heating. en_US
dc.language.iso en_US en_US
dc.subject Surimi en_US
dc.subject Rheology en_US
dc.subject Spectroscopy en_US
dc.subject Comminution en_US
dc.subject.lcsh Surimi en_US
dc.subject.lcsh Fishery processing en_US
dc.subject.lcsh Surimi -- Analysis
dc.title Rheological and spectroscopic characterization of surimi under various comminuting and heating conditions en_US
dc.type Thesis/Dissertation en_US
dc.degree.name Doctor of Philosophy (Ph. D.) in Food Science and Technology en_US
dc.degree.level Doctoral en_US
dc.degree.discipline Agricultural Sciences en_US
dc.degree.grantor Oregon State University en_US
dc.contributor.committeemember Daeschel, Mark
dc.contributor.committeemember Goddik, Lisbeth
dc.contributor.committeemember Penner, Michael H.
dc.contributor.committeemember Ingham, Russell E.
dc.description.peerreview no en_us

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