Proteolysis is one of the most important biochemical reactions during cheese ripening.Studies on the secondary structure of proteins during ripening would be helpful for characterizing protein changes for assessing ch...Proteolysis is one of the most important biochemical reactions during cheese ripening.Studies on the secondary structure of proteins during ripening would be helpful for characterizing protein changes for assessing cheese quality.Fourier transform infrared spectroscopy(FTIR),with self-deconvolution,second derivative analysis and band curve-fitting,was used to characterize the secondary structure of proteins in Cheddar cheese during ripening.The spectra of the amide I region showed great similarity,while the relative contents of the secondary structures underwent a series of changes.As ripening progressed,the α-helix content decreased and the β-sheet content increased.This structural shift was attributed to the strengthening of hydrogen bonds that resulted from hydrolysis of caseins.In summary,FTIR could provide the basis for rapid characterization of cheese that is undergoing ripening.展开更多
The paper was to find the bacteria to degrade aflatoxin B 1 (AFB 1) and realize the application of biological degradation on AFB 1. Using cumarin as the carbon source and energy on the first screening, then the ten ...The paper was to find the bacteria to degrade aflatoxin B 1 (AFB 1) and realize the application of biological degradation on AFB 1. Using cumarin as the carbon source and energy on the first screening, then the ten strains which were first screened out were taken to degrade AFB 1 100 pg kg^-1. Strain NMO-3 was screened out of ten strains, the degradation ratio of AFB 1 reached 85.7%, which was more prominent than the others (P 〈 0.01). With the analysis of colony morphology, physiological and biochemistry experiments, and 16S rDNA gene sequence, the strain NMO-3 was finally identified as Stenotrophomonas sp. Using cumarin as the carbon source and energy could screen out the AFB 1 degradation strains. Acute toxicity tests show that the viable number of NMO-3 lower than 3.12 × 10^10 cfu mL-1 is safety. The crude enzyme was obtained by 65% ammonium sulfate fractionation, and it could degrade AFB1. It is the first report for the strain's detoxi- AFB1.展开更多
Fourier transform infrared spectroscopy(FTIR) and circular dichroism(CD) were used to investigate the conformational changes of heated whey protein(WP) and the corresponding changes in the hydrolysates immunoreactivit...Fourier transform infrared spectroscopy(FTIR) and circular dichroism(CD) were used to investigate the conformational changes of heated whey protein(WP) and the corresponding changes in the hydrolysates immunoreactivity were determined by competitive enzyme-linked immunosorbent assay(ELISA).Results showed that the contents of α-helix and β-sheet of WP did not decrease much under mild heating conditions and the antigenicity was relatively high;when the heating intensity increased(70 ℃ for 25 min or 75 ℃ for 20 min),the content of α-helix and β-sheet decreased to the minimum,so was the antigenicity;However,when the WP was heated at even higher temperature and for a longer time,the β-sheet associated with protein aggregation begun to increase and the antigenicity increased correspondingly.It was concluded that the conformations of heated WP and the antigenicity of its hydrolysates are related and the optimum structure for decreasing the hydrolysates antigeniity is the least content of α-helix and β-sheet.Establishing the relationship between the WP secondary structure and WP hydrolysates antigenicity is significant to supply the reference for antigenicity reduction by enzymolysis.展开更多
基金financially supported by Beijing Municipal Commission of Education Co-Constructed Programand Chinese Universities Scientific Fund(2009-4-25)
文摘Proteolysis is one of the most important biochemical reactions during cheese ripening.Studies on the secondary structure of proteins during ripening would be helpful for characterizing protein changes for assessing cheese quality.Fourier transform infrared spectroscopy(FTIR),with self-deconvolution,second derivative analysis and band curve-fitting,was used to characterize the secondary structure of proteins in Cheddar cheese during ripening.The spectra of the amide I region showed great similarity,while the relative contents of the secondary structures underwent a series of changes.As ripening progressed,the α-helix content decreased and the β-sheet content increased.This structural shift was attributed to the strengthening of hydrogen bonds that resulted from hydrolysis of caseins.In summary,FTIR could provide the basis for rapid characterization of cheese that is undergoing ripening.
基金the Ministry of Science and Technology of China (2005DKA21204-11)the Na-tional Natural Science Foundation of China (30571353)the National High Technology Research and Devel-opment Program of China (863 Program,2006AA10Z442)
文摘The paper was to find the bacteria to degrade aflatoxin B 1 (AFB 1) and realize the application of biological degradation on AFB 1. Using cumarin as the carbon source and energy on the first screening, then the ten strains which were first screened out were taken to degrade AFB 1 100 pg kg^-1. Strain NMO-3 was screened out of ten strains, the degradation ratio of AFB 1 reached 85.7%, which was more prominent than the others (P 〈 0.01). With the analysis of colony morphology, physiological and biochemistry experiments, and 16S rDNA gene sequence, the strain NMO-3 was finally identified as Stenotrophomonas sp. Using cumarin as the carbon source and energy could screen out the AFB 1 degradation strains. Acute toxicity tests show that the viable number of NMO-3 lower than 3.12 × 10^10 cfu mL-1 is safety. The crude enzyme was obtained by 65% ammonium sulfate fractionation, and it could degrade AFB1. It is the first report for the strain's detoxi- AFB1.
基金National Science and Technology Support Program(2009BADB9B06)Beijing Science and Technology Program(D10110504601002)
文摘Fourier transform infrared spectroscopy(FTIR) and circular dichroism(CD) were used to investigate the conformational changes of heated whey protein(WP) and the corresponding changes in the hydrolysates immunoreactivity were determined by competitive enzyme-linked immunosorbent assay(ELISA).Results showed that the contents of α-helix and β-sheet of WP did not decrease much under mild heating conditions and the antigenicity was relatively high;when the heating intensity increased(70 ℃ for 25 min or 75 ℃ for 20 min),the content of α-helix and β-sheet decreased to the minimum,so was the antigenicity;However,when the WP was heated at even higher temperature and for a longer time,the β-sheet associated with protein aggregation begun to increase and the antigenicity increased correspondingly.It was concluded that the conformations of heated WP and the antigenicity of its hydrolysates are related and the optimum structure for decreasing the hydrolysates antigeniity is the least content of α-helix and β-sheet.Establishing the relationship between the WP secondary structure and WP hydrolysates antigenicity is significant to supply the reference for antigenicity reduction by enzymolysis.