A modified complex coacervation-co-precipitation method was used to prepare bone morphogenetic protein (BMP)-loaded nanospheres. Three natural polymers were used as packing materials to obtain nanoscale delivery devic...A modified complex coacervation-co-precipitation method was used to prepare bone morphogenetic protein (BMP)-loaded nanospheres. Three natural polymers were used as packing materials to obtain nanoscale delivery device for BMP,in the presence of phosphatidylcholine functioning as stabilizer. Positively charged polysaccharide, N,N-diethylaminoethyl dex-tran (DEAE-dextran) tended to form stable, uniform and smaller size particles carrying BMP. Negatively charged bovine serum albumin (BSA) induced precipitation of the produced BMP particles due to its weak interaction with BMP molecules, although it produced nanosized BMP spheres. While collagen, a weakly positively charged protein shaped larger particles due to the strong interaction among themselves. A mechanism of co-precipitation process was also deduced to depict the formation of stable nanospheres.展开更多
采用碱溶酸沉的方法提取南极磷虾分离蛋白(krill protein isolate,KPI),通过喷雾干燥和冷冻干燥的方式制备南极磷虾分离蛋白粉,并对这两种分离蛋白粉的结构及功能特性进行比较分析。结果表明:与冷冻干燥南极磷虾分离蛋白(freeze-dried k...采用碱溶酸沉的方法提取南极磷虾分离蛋白(krill protein isolate,KPI),通过喷雾干燥和冷冻干燥的方式制备南极磷虾分离蛋白粉,并对这两种分离蛋白粉的结构及功能特性进行比较分析。结果表明:与冷冻干燥南极磷虾分离蛋白(freeze-dried krill protein isolate,FKPI)相比,喷雾干燥南极磷虾分离蛋白(spray-dried krill protein isolate,SKPI)明度大,色泽较好;扫描电子显微镜结果显示,SKPI呈现出向内凹陷的不规则球状结构,而FKPI为薄层片状结构,SKPI的堆积密度高于FKPI;圆二色谱进一步表明,与KPI相比,SKPI和FKPI均呈现α-螺旋含量下降、β-转角含量增加的趋势,其中,SKPI的α-螺旋含量下降27.9%,β-转角含量增加12.2%,表明喷雾干燥后蛋白质的二级结构均从有规则的结构向无规则的结构转化;SKPI持水力、持油力、乳化稳定性和起泡性等均高于FKPI,而SKPI的溶解性、乳化性却比FKPI的差。可见,不同的干燥方式会改变南极磷虾分离蛋白的结构特性,并进一步影响其功能特性。展开更多
Seabuckthorn seed meal(SSM) is a waste of oil extraction industry that rich in protein. In order to seek suitable protein extraction method, three different deep eutectic solvents(DESs)(including choline chlorideglyce...Seabuckthorn seed meal(SSM) is a waste of oil extraction industry that rich in protein. In order to seek suitable protein extraction method, three different deep eutectic solvents(DESs)(including choline chlorideglycerol, choline chloride-oxalic acid and choline chloride-urea) were developed for extracting protein from SSM and compared with alkaline. Result indicated that alkaline could effectively extract 56.9% protein from SSM and its protein content was 73.1%, higher than DES at 31.0%-41.4% and 64.3%-67.5%, respectively. However, compared to alkali, DES led to a product with less β-sheet, more β-turn, more essential amino acids, higher total amino acid content, especially choline chloride-urea which extracted protein showing an integrated and similar protein weight distribution compared to SSM. Also, this protein extracted chloride-urea showed a highest digestibility in vitro(by pepsin)(54.2%). These results indicated that choline chloride-urea extraction is better than alkaline extraction for SSM.展开更多
Effect of dissolved CO2 on bovine serum albumin (BSA) solubilization in the reverse micelles of sodium bis (2-ethylhexyl) sulfosuccinate (AOT) in 2,2,4-trimethylpentane (iso-octane) has been studied at 308.2 K. It was...Effect of dissolved CO2 on bovine serum albumin (BSA) solubilization in the reverse micelles of sodium bis (2-ethylhexyl) sulfosuccinate (AOT) in 2,2,4-trimethylpentane (iso-octane) has been studied at 308.2 K. It was found that BSA can be precipitated completely by CO2 while the AOT and water remain in the iso-octane continuous phase. This opens up a possibility for recovery of pure protein solids directly from reverse micellar solutions.展开更多
Tryptophan is one of the nine essential amino acids in humans that can only be obtained through diets and supplements.It is a precursor to many biological processes,such as serotonin,melatonin,kynurenin,and niacin(nic...Tryptophan is one of the nine essential amino acids in humans that can only be obtained through diets and supplements.It is a precursor to many biological processes,such as serotonin,melatonin,kynurenin,and niacin(nicotinamide)vitamin synthesis.The content of tryptophan in foods,such as soybean is an important indicator of nutritional value.Therefore,accurate quantification of tryptophan in soybean is crucial to soybean nutritional improvement.Quantification of soybean protein-bound amino acids first involves acid hydrolysis of total protein to liberate amino acids.However,tryptophan quantification following acid hydrolysis is difficult or impossible due to its reactions with soybean carbohydrates.Therefore,removal of carbohydrates from soy proteins prior to acid hydrolysis is necessary.In this study,we compared four common protein precipitation methods(i.e.,methanol,acetonitrile,acetone,and trichloroacetic acid(TCA)protein precipitation methods)to determine the best method to separate soy proteins from carbohydrates,and concluded that acetone provided the highest recovery of soy proteins.Tryptophan content in the precipitated proteins was determined after acid hydrolysis of the proteins using liquid chromatography-tandem mass spectrometry multiple reaction monitoring(LC-MS/MS-MRM).No significant difference in the tryptophan content was found among proteins precipitated with methanol,acetonitrile,and TCA,suggesting that these precipitated proteins have similar compositions.A slightly lower,but statistically significant tryptophan content was found in the acetonitrile-precipitated proteins,suggesting that these proteins contain slightly higher glycosylated proteins.展开更多
基金Project supported by the Basic Research Program (863) of China
(No. G1999054305) and the National Natural Science Foundation
of China (No. 50173024)
文摘A modified complex coacervation-co-precipitation method was used to prepare bone morphogenetic protein (BMP)-loaded nanospheres. Three natural polymers were used as packing materials to obtain nanoscale delivery device for BMP,in the presence of phosphatidylcholine functioning as stabilizer. Positively charged polysaccharide, N,N-diethylaminoethyl dex-tran (DEAE-dextran) tended to form stable, uniform and smaller size particles carrying BMP. Negatively charged bovine serum albumin (BSA) induced precipitation of the produced BMP particles due to its weak interaction with BMP molecules, although it produced nanosized BMP spheres. While collagen, a weakly positively charged protein shaped larger particles due to the strong interaction among themselves. A mechanism of co-precipitation process was also deduced to depict the formation of stable nanospheres.
文摘采用碱溶酸沉的方法提取南极磷虾分离蛋白(krill protein isolate,KPI),通过喷雾干燥和冷冻干燥的方式制备南极磷虾分离蛋白粉,并对这两种分离蛋白粉的结构及功能特性进行比较分析。结果表明:与冷冻干燥南极磷虾分离蛋白(freeze-dried krill protein isolate,FKPI)相比,喷雾干燥南极磷虾分离蛋白(spray-dried krill protein isolate,SKPI)明度大,色泽较好;扫描电子显微镜结果显示,SKPI呈现出向内凹陷的不规则球状结构,而FKPI为薄层片状结构,SKPI的堆积密度高于FKPI;圆二色谱进一步表明,与KPI相比,SKPI和FKPI均呈现α-螺旋含量下降、β-转角含量增加的趋势,其中,SKPI的α-螺旋含量下降27.9%,β-转角含量增加12.2%,表明喷雾干燥后蛋白质的二级结构均从有规则的结构向无规则的结构转化;SKPI持水力、持油力、乳化稳定性和起泡性等均高于FKPI,而SKPI的溶解性、乳化性却比FKPI的差。可见,不同的干燥方式会改变南极磷虾分离蛋白的结构特性,并进一步影响其功能特性。
基金the financial support from the National Natural Science Foundation of China (No. 31201416)Science and Technology Research Program of Guangdong Province (No. 2017A01010502)。
文摘Seabuckthorn seed meal(SSM) is a waste of oil extraction industry that rich in protein. In order to seek suitable protein extraction method, three different deep eutectic solvents(DESs)(including choline chlorideglycerol, choline chloride-oxalic acid and choline chloride-urea) were developed for extracting protein from SSM and compared with alkaline. Result indicated that alkaline could effectively extract 56.9% protein from SSM and its protein content was 73.1%, higher than DES at 31.0%-41.4% and 64.3%-67.5%, respectively. However, compared to alkali, DES led to a product with less β-sheet, more β-turn, more essential amino acids, higher total amino acid content, especially choline chloride-urea which extracted protein showing an integrated and similar protein weight distribution compared to SSM. Also, this protein extracted chloride-urea showed a highest digestibility in vitro(by pepsin)(54.2%). These results indicated that choline chloride-urea extraction is better than alkaline extraction for SSM.
文摘Effect of dissolved CO2 on bovine serum albumin (BSA) solubilization in the reverse micelles of sodium bis (2-ethylhexyl) sulfosuccinate (AOT) in 2,2,4-trimethylpentane (iso-octane) has been studied at 308.2 K. It was found that BSA can be precipitated completely by CO2 while the AOT and water remain in the iso-octane continuous phase. This opens up a possibility for recovery of pure protein solids directly from reverse micellar solutions.
基金the National Science Foundation(NSF Molecular and Cellular Biosciences Award 1024976National Science Foundation IOS and Japanese Science and Technology Agency joint Metabolomics for Low Carbon Society Awards 1139489 and 1639618+1 种基金National Science Foundation IOS Awards 1340058 and 1743594)Ritesh Kumar was supported by a grant from the United Soybean Board(USB,award#1920-152-0120-B)to Minviluz G.Stacey,Lloyd W.Sumner and Zhentian Lei.
文摘Tryptophan is one of the nine essential amino acids in humans that can only be obtained through diets and supplements.It is a precursor to many biological processes,such as serotonin,melatonin,kynurenin,and niacin(nicotinamide)vitamin synthesis.The content of tryptophan in foods,such as soybean is an important indicator of nutritional value.Therefore,accurate quantification of tryptophan in soybean is crucial to soybean nutritional improvement.Quantification of soybean protein-bound amino acids first involves acid hydrolysis of total protein to liberate amino acids.However,tryptophan quantification following acid hydrolysis is difficult or impossible due to its reactions with soybean carbohydrates.Therefore,removal of carbohydrates from soy proteins prior to acid hydrolysis is necessary.In this study,we compared four common protein precipitation methods(i.e.,methanol,acetonitrile,acetone,and trichloroacetic acid(TCA)protein precipitation methods)to determine the best method to separate soy proteins from carbohydrates,and concluded that acetone provided the highest recovery of soy proteins.Tryptophan content in the precipitated proteins was determined after acid hydrolysis of the proteins using liquid chromatography-tandem mass spectrometry multiple reaction monitoring(LC-MS/MS-MRM).No significant difference in the tryptophan content was found among proteins precipitated with methanol,acetonitrile,and TCA,suggesting that these precipitated proteins have similar compositions.A slightly lower,but statistically significant tryptophan content was found in the acetonitrile-precipitated proteins,suggesting that these proteins contain slightly higher glycosylated proteins.
