published_or_final_version / abstract / toc / Zoology / Master / Master of Philosophy

published_or_final_version / Biochemistry / Master / Master of Philosophy

published_or_final_version / Physiology / Doctoral / Doctor of Philosophy

published_or_final_version / abstract / Zoology / Master / Master of Philosophy

published_or_final_version / Medicine / Doctoral / Doctor of Philosophy

A heat stable protease was identified as the cause of textural degradation in cooked arrowtooth flounder (Atheresthes stomias) muscle. Maximum proteolytic activity in the fish muscle was observed between 55°C and 60°C and myosin heavy chain appeared to be the primary substrate for the enzyme. Degradation of this myofibrillar protein at 55°C was extremely rapid and myosin heavy chain was completely hydrolyzed to peptide fragments smaller than actin, while actin itself was unaffected. A single strand 32kD proteolytic enzyme was extracted from the muscle and purified 125-fold. The enzyme was stable to freezing for up to 6 months. Activity of the semi-purified enzyme at 55°C was optimal against casein between pH 6.0 and 7.0. Sulfhydryl reagents p-chloromercuriphenylsulfonic acid, iodoacetate, iodoacetamide and cystatin were effective in inhibiting enzyme activity in casein assays. The serine protease inhibitors phenylmethylsulfonylfluoride and trypsin-chymotrypsin inhibitor appeared to activate enzyme activity against casein. Adenosine triphosphate was also an activator. Arrowtooth flounder was then considered as a raw material for surimi, since the surimi process provides for repeated washing of the minced muscle and a final mixing step during which inhibitory substances can be conveniently added. Arrowtooth muscle was monitored at all stages of surimi production. There was no evidence of myosin degradation on sodium dodecyl sulphate polyacrylamide electrophoretic gels at any time during surimi production or during the preparation of samples for testing. However, when the washed mince was incubated at 55°C, 12% residual proteolytic activity was observed. This level was sufficient to degrade the myosin component of surimi gels prepared from the control surimi to which no inhibitors had been added. The food grade substances tested for proteolytic inhibition were bovine blood plasma powder, egg white powder, whey protein concentrate, carrageenan and crude α₂-macroglobulin. Addition of plasma and/or egg white powders to control surimi resulted in a product that was comparable to pollock in functional properties as measured by gel strength, expressible moisture and fold tests. Electrophoretic comparison of surimi made with 1.0% or 2.0% plasma powder or egg white with surimi produced with 0.1% or 0.2% α₂-macroglobulin suggested that the plasma and egg white contributed gel enhancing effects in addition to protease inhibition. Carrageenan was not effective as either a protease inhibitor or gel enhancer. / Graduation date: 1992

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