Study On Separation And Properties Of Camphor Tree Seed Kernel Protein

South of the Yellow River can produce several tons of seed camphor(camphor tree seed kernel).Camphor tree seed kernel oil is rich in carbon chain(over 50%)and vegetable protein(over 18%).Camphor tree seed kernel oil as a novel vegetable oils,studied of the extraction n composition and the physiological were more.But camphor tree seed kernel protein as a novel plant protein resource,still no research report about their separation,composition,structure and characteristics.It has great potential for development.This paper analyzes the determination of the composition of camphor tree seed kernel,Using Osborne grade extraction of proteins analysis method for determining the protein composition of camphor tree seed kernel.Optimizing the extraction process of the separated camphor tree seed kernel protein,and studied the physicochemical and functions properties of camphor tree seed kernel protein isolate.The main research conclusions are as follows:The content of crude protein in camphor tree seed kernel was 18.15%,moisture content was 3.97%,the ash content was 1.96%,fat content was 58.02%,carbohydrate content was 17.90%.It can be seen from the composition analysis,the' content of protein of camphor tree seed kernel was second only to oil.The content of albumin,globulin,gliadin and gluten are respectively of 25.64%,23.51%,2.32%and 23.51%.The protein extraction rate was as index,Through the single factor experiment and orthogonal experiment to optimize the extraction process of four proteins,The results show that:?The optimum extraction process of albumin:Solid-liquid ratio was 1:12,extraction time was 2.5h,temperature was 45?,under the condition,the albumin extraction rate was 52.78%,the purity was 91.10%.?The optimum extraction process of globulin:Solid-liquid ratio was 1:12,extraction time was 3.0h,temperature was 40?,concentration of NaCI was 2%,under the condition,the globulin extraction rate was 25.14%,the purity was90.69%.?The optimum extraction process of gliadin:Solid-liquid ratio was 1:10,extraction time was 3.0h,temperature was 45?,concentration of ethanol was 80%,under the condition,the gliadin extraction rate was 4.49%,the purity was89.21%.? The optimum extraction process of gluten:Solid-liquid ratio was 1:8,extraction time was 2.5h,temperature was 40?,lye concentration was 0.015mol/L,under the condition,the gluten extraction rate was 33.14%,the purity was91.29%.The isoelectric point of albumin,globulin,gliadin and glutenin respectively were pH3.1,pH3.5,pH3.3,pH4.5;The essential amino acid content of albumin is quite high and gliadin is less;Albumin and glutenin were rule,the surface of globulin and gliadin surface were shine;Albumin,globulin,gliadin and glutenin denaturation temperature were 45.35 ?,46.15 ?,43.53 ? and 52.56 ?,respectively,the denaturation temperature of glutenin was highest;Albumin and globulin secondary structure is similar,Beta-folding accounts for a higher percentage,gliadin random coil structure,gluten is alpha helix structure;The relative molecular mass of the four kinds of protein isolated is larger,the molecular weight of albumin are mainly distributed in 15KDa,22KDa,35KDa,40KDa and 130KDa,the molecular weight of globulin are mainly distributed in 10?15KDa?23KDa?35?40KDa and 94KDa,gliadin only has two bands,distributed in 16KDa and 24KDa,the molecular weight of glutenin are mainly distributed in 23?25KDa?29KDa?40KDa and 57KDa.?With the gradual increase of pH,the solubility of four kinds of protein isolate first decreases after increasing trend,the solubility near the isoelectric point was worst,best solubility of albumin,the solubility of gliadin was worst;Gradually increased with the temperature of the solubility of protein isolates showed a trend of decrease after the first increase.?Gradually increased with the pH of the WHC of protein isolates showed a trend of increase after the first decrease.When reach maximum pH 9,the WHC of albumin,globulin,gliadin and glutenin were maximum,were 4.1 g/g?2.0g/g?2.1g/g and1.7g/g;With the increase of temperature first increases and then decreases;With the increase of incubation time,the WHC of albumin,gliadin and glutenin showed a trend of increasing,the WHC of globulin showed increasing trend after decreases.?With the gradual increase of temperature,the OAC of four kinds of isolated proteins showed a trend of decreasing,the OAC of globulin is best,at room temperature 25 ? is 4.2 g/g.With the increase of incubation time,the OAC is increasing gradually.?EAI and ESI of four kinds of protein isolate trend along with the change of pH are similar with the solubility trend along with the change of pH,also increase trend have been reduced,the EAI and ESI near isoelectric point is the worst,EAI and ESI of albumin was best,gliadin was worst;With the increase of the protein concentration,the EAI and ESI of four kinds of protein isolate increase gradually,with the increase of the temperature showed a trend of decrease after the first increase.?With the increase of pH,the FC of four kinds of protein isolate first decreases after increasing trend,the FC near the isoelectric point was worst,the change trend of FSC just the opposite,showed a trend of decrease after the first increase.The FC and FSC of albumin was best,gliadin was worst.With the increase of the protein concentration,the FC and FSC of four kinds of protein showed a trend of increase gradually.The FC of the four proteins with the increase of temperature showed a trend of decrease after the first increase,the FSC of albumin,gliadin and glutenin increased with the increasing of temperature first after the trend of decrease,the FSC of globulin increasing trend with the increasing of temperature.