Study On The Technology To Prevent Protein Oxidation Caused The Deterioration Of Coregonus Peled Muscle

Coregonus peled were characteristic advantage industry of fish culture in cold water in xinjiang,due to its fresh meat and extremely susceptible by protein oxidation,leading to the deterioration of muscle protein during production,processing,transportation and storage,which greatly reduce the quality of the coregonus peled and bring the directly economic losses.Therefore,its very important to explore and research key technology about how to prevent protein oxidation caused the deterioration of coregonus peled muscle protein.This subject with coregonus peled as the research object,using the in vitro protein oxidation system to simulate protein oxidation,researching prevent the coregonus peled protein oxidation under in different ways of rinsing,adding different antifreeze material,different freezing and different packaging,so as to obtain some technological conditions and process parameters to prevent protein oxidation caused the deterioration of coregonus peled protein,providing theoretical basis for the development of cold water fish industry in xinjiang.1.In the several different rinsing conditions,myofibril protein was extracted from coregonus peled,the results show that 0.3% of PG and 0.5% Nacl was the best rinse solution and the effect of PG to prevent protein oxidation is superior to sodium chloride and ascorbic acid sodium.The carbonyl content and surface hydrophobicity of myofibril protein was positively correlated with the extension of storage time,total sulphur content and free ammonia was negatively correlated.2.Using the response surface experiments to study rinsing process of coregonus peled for prevent the deterioration of muscle protein,and the best technological conditions as follows: 0.21% PG solution,rinse time was 6 min,rinse times for 2 times and the inhibition rate of protein oxidation was 30.12%.3.The results showed that sample were frozen after 1 ~ 5 weeks,adding sodium lactate group,SPI + TiO2(nm)distribution of liquid and commercial antifreeze(sucrose + sorbitol)group of myofibril protein carbonyl content were 6.884 nmol/mg,6.909 nmol/mg and 7.109 nmol/mg,while the control group was 7.505 nmol/mg;Total sulphur content fell respectively by 20.49%,23.75% and 20.49%,and the control group decreased by 32.17%;Free ammonia respectively by 31.40%,33.33% and 31.40%,and the control group decreased by 40.26%;Surface hydrophobicity respectively increased 44.71%,45.20% and 46.36%,while the control group increased by 47.01%.In addition,adding sodium lactate group,SPI + TiO2(nm)distribution of liquid and commercial antifreeze(sucrose + sorbitol)group of myofibril protein nitrogen solubility index,emulsification and emulsion stability and foamability declined with the increase of freezing storage time,but decreased significantly less than the control group.In addition,adding sodium lactate and SPI + TiO2(nm)distribution of liquid group to a certainly extent than commercial antifreeze had better ability to prevent protein oxidation,and SPI + TiO2(nm)was superior to the effect of sodium lactate.4.Freezing(liquid nitrogen rapidly cooling,ordinary freezed)and packaging(heat sealing packaging,vacuum packaging)in two different ways to studied the myofibril protein physicochemical and functional properties.Results showed that with the temperature by-18℃,the content of carbonyl and hydrophobic of liquid nitrogen rapidly cooling significantly below ordinary freezed,and the content of the total sulphur,free ammonia and nitrogen solubility index,emulsification and emulsion stability and foamability significantly better than-18℃ordinary freezing during frozen storage;At the same times-24℃liquid nitrogen rapidly cooling had better than-24℃ordinary freezed effect on prevent coregonus peled myofibril protein oxidation,using liquid nitrogen rapidly cooling could effectively prevent the oxidation of the protein to caused coregonus peled muscle protein deterioration,the lower of temperature,the more beneficial to prevent the deterioration of coregonus peled muscle.The coregonus peled protein content of carbonyl by the initial value of 6.206 nmol/mg rising 8.973 nmol/mg,hydrophobic from 50.56μg rising to 95.82μg,total sulfhydryl decreased by 81.38%,free ammonia down to 46.67% under heat sealing packing,and nitrogen solubility index fall by 43.28%,emulsification fall by 22.37%,emulsion stability fall by 50.00%,foamability fall by 33.33% after storaged by 4 weeks;Vacuum packaging(0.085,0.090,0.095 MPa three vacuum)Carbonyl content by 6.204,6.001,5.364 nmol/mg respectively rising to 8.543,8.262,8.181 nmol/mg,hydrophobic by 41.65,33.17,24.21 μ g rising to 89.98,89.98,73.32 μ g,total sulfhydryl group respectively fall to 77.09%,74.42% and 76.42%,free ammonia had respectively fallen by 40.57%,37.56% and 25.59%,and nitrogen solubility index fall by 42.03%,37.50% and 27.85%,the emulsification had fallen by 20.51%,12.50% and 14.63%,emulsion stability had respectively fallen by 48.33%,40.00% and 35.38%,foamability fall by 40.00%,44.44% and 45.00% after 4 weeks storaged;Using vacuum packing could avoid the coregonus peled muscle deterioration caused by protein oxidation,improving the quality of fish;The experiment processing selected three different vacuum packaging,the results found that the higher of vacuum,the better effect to prevent coregonus peled muscle protein oxidation,but pay attention to the process of packing in the extraction time.