National Engineering Laboratory on Wheat and Corn Further Processing

Changchun, China

National Engineering Laboratory on Wheat and Corn Further Processing

Changchun, China

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Wu D.,Jilin Agricultural University | Wu D.,National Engineering Laboratory on Wheat and Corn Further Processing | Min W.H.,Jilin Agricultural University | Min W.H.,National Engineering Laboratory on Wheat and Corn Further Processing | And 11 more authors.
Advanced Materials Research | Year: 2014

The functional properties of protein isolate and major protein fractions prepared from Changbai Mountain pine nuts were investigated. Albumin, globulin, glutelin, and protein isolates were obtained after the Osborne method and alkaline dissolution and acid precipitation, and protein contents of the fractions are 48.02%, 81.93%, 83.02%, and 89.69%, respectively. For the sulfhydryl contents, albumin is the highest, and glutelin is the lowest. In a disulphide bond, the protein isolate content is the highest with a value of 28.74 μmol/g, and the glutelin content is the lowest with the value of 13.46 μmol/g. For the four kinds of proteins, the essential amino acids in percentage of total amino acids are 31.13%, 34.22%, 30.30%, and 34.54%, respectively. The pH dependent protein solubility profile reveals that the minimum solubility is at pH 5.0, which corresponds to the isoelectric point. Protein isolate has the minimum water absorption capacity with a value of 0.59 ml/g. On the other hand, albumin has the minimum oil absorption capacity with a value of 2.11 ml/g. The emulsifying activity and stability and the foaming activity and stability increased with increasing concentration of four kinds of proteins. SDS-PAGE results showed that these four kinds of proteins have different molecules. © (2014) Trans Tech Publications, Switzerland.


Jiang W.,Jilin Agricultural University | Jiang W.,National Engineering Laboratory on Wheat and Corn Further Processing | Wu D.,Jilin Agricultural University | Wu D.,National Engineering Laboratory on Wheat and Corn Further Processing | And 8 more authors.
Journal of the Chinese Cereals and Oils Association | Year: 2014

The functional properties of Perilla protein isolate (PPI), Perilla albumin protein (PAP), Perilla globulin protein (PGP), Perilla glutelin protein (PLP) from defatted Perilla seed meal used as raw materials were studied. The results showed that protein contents of PPI, PAP, PGP and PLP were 86.1%, 60.1%, 82.9% and 74.7%, respectively. The amino acids contents of Perilla proteins met the Adult Standard recommended by FAO/WTO. PGP showed the highest exposed sulfhydryl content (27.3 μmol/g); PLP showed the highest S-S content (20.38 μmol/g); SDS-PAGE indicated that PPI lane contained all the rest three proteins' band, and the mainly subunit were about 10.5, 20.1, 32.7 and 40.6 ku. The solubility curve was similar to U letter. PPI, PAP, PLP showed the lowest solubility with pH 4.0 except PGP of pH5.0, the four proteins showed the highest solubility with pH 12.0. All the four proteins expressed the lowest foam capacity when pH near the isoelectric point, and foam stability showed the similar change trend with foam capacity except PAP. There were not apparent effect of pH range on emulsion capacity and emulsion stability. PAP showed the maximum water absorption (3.81 mL/g) and oil absorption (3.93 mL/g).


Ren D.,Jilin Agricultural University | Ren D.,National Engineering Laboratory on Wheat and Corn Further Processing | Wang M.,Jilin Agricultural University | Wang M.,National Engineering Laboratory on Wheat and Corn Further Processing | And 10 more authors.
Journal of the Science of Food and Agriculture | Year: 2016

BACKGROUND: Hazelnut dregs are by-products of hazelnut oil expression, which have not been fully exploited. This research aims to assess the immunomodulatory function of hazelnut hydrolysed peptides (HHPs). RESULTS: HHPs with a hydrolysis degree of 38.08% were divided into three fractions by ultra-filtration: the high molecular weight peptide (>10 kDa), medium molecular weight peptide (3 kDa to 10 kDa), and low molecular weight peptide (<3 kDa). Mice were fed daily with HHPs of different molecular weights at doses of 200, 400, and 800 mg kg−1 body weight. On the 10th, 20th and 30th day of feeding, representative immune indexes were measured. Results showed that HHPs can regulate the immune system of mice, which is affected by the molecular weight of HHP and the feeding time. Generally, short-term feeding (10 d to 20 d) with HHPs of different molecular weights can improve most immune indexes (organ index, spleen lymphocyte proliferation, macrophage activity, secretory immunoglobulin A content, and number of CD4+ and CD8+ T cells), whereas during long-term feeding (30 d), low molecular weight HHP can better sustain immune regulation. CONCLUSION: HHPs exhibit potential immunomodulatory properties, which has promising implications for the development of new functional foods. © 2015 Society of Chemical Industry. © 2015 Society of Chemical Industry


Wang X.-F.,Jilin Agricultural University | Wang X.-F.,National Engineering Laboratory on Wheat and Corn Further Processing | Min W.-H.,Jilin Agricultural University | Min W.-H.,National Engineering Laboratory on Wheat and Corn Further Processing | And 10 more authors.
Modern Food Science and Technology | Year: 2015

Globulin is a major protein component of walnuts (Juglans mandshurica Maxim) from the Changbai mountain. The walnut is rich in proteins; therefore, it must be further developed and processed for appropriate utilization of the protein resources. Walnut globulin was extracted by optimized Osborne method, and purified by ion-exchange chromatography. Walnut globulin was subjected to a preliminary structural analysis; subsequently, its functional properties were comprehensively compared (and analyzed) against those of soy protein isolates (SPI), in order to provide a theoretical basis for its application in food processing. The prepared globulin contained 80.71% protein content. Anion-exchange chromatography showed four peaks; the relative molecular weights corresponding to these peaks were concentrated in the ranges 14.3~27.0 ku, 18.0~21.0 ku, 30.0~37.0 ku, and 44.3~59.0 ku, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The essential amino acid content of the prepared globulin conformed to the Adult Standard Recommendation of the FAO/WTO. The differential scanning calorimetry (DSC) spectrogram of the prepared globulin revealed two endothermic peaks, indicating denaturation temperatures of 98.08℃ and 155.33℃, corresponding to enthalpy values of 13.06 J/g and 764.80 J/g, respectively. The Fourier transform-infrared (FT-IR) spectrum revealed that the prepared globulin mainly consisted of alpha helical secondary structures. The functional properties of the prepared globulin, excluding foamability and water absorption (which were significantly lower than those of SPI), were observed to be comparable to those of SPI. ©, 2015, South China University of Technology. All right reserved.


Zhang L.,Jilin Agricultural University | Zhang L.,National Engineering Laboratory on Wheat and Corn Further Processing | Liu C.,Jilin Agricultural University | Liu C.,National Engineering Laboratory on Wheat and Corn Further Processing | And 6 more authors.
Journal of Chinese Institute of Food Science and Technology | Year: 2015

[Objective] To improve the enzyme activityof amylosucrase (AS) by site-directed mutagenesisand provide experiment basis for large-scale preparation and application of AS by the study of enzymology properties characterization. [Methods] The gene of AS from Neisseria polysaccharea were cloned and heterologously expressed in E. coli BL21 by using the genetic engineering techniques and F191M was obtained by site-directed mutagenesis. The enzymology properties of AS from F191M and wild type were detected after the inducible expression and purification. [Results] F191M was built successfully, and its specific activity was 202 U/mg, increasing by 1.44 times compared with wild type. By comparing the enzymology properties of F191M and wild type, the optimal pH of F191M was 8.0 higher than the wild type 7.0.The optimal temperature was the same as the wild type(35℃). The half-life of F191M and the wild type were 19 h and 20 h at 35℃, respectively. F191M had better resistance on metalions and organic solvents than wild type. The Kinetics study showed that the Vmax of F191M increased by 1.45 times. [Conclusions] The mutant strain F191M was expressed in E. coliBL21 effectively, and the activity of AS increased by 1.44 times compared with wild type. © 2015, Chinese Institute of Food Science and Technology. All right reserved.

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