[Objective] To investigate the optimal enzyme for the hydrolysis of corn gluten meal and the optimal hydrolysis conditions for the enzyme. [Method] Nine kinds of enzymes were used to hydrolyze the corn gluten meal, us...[Objective] To investigate the optimal enzyme for the hydrolysis of corn gluten meal and the optimal hydrolysis conditions for the enzyme. [Method] Nine kinds of enzymes were used to hydrolyze the corn gluten meal, using the formaldehyde titration method for the determination of hydrolysis degree, and orthogonal test was used to determine the optimal hydrolysis conditions for double enzymes hydrol- ysis of corn gluten meal. [Result] The optimal pretreatment condition for corn gluten meal is heating at 121 ~C for 30 min. The double enzyme hydrolysis for the pro- treated corn gluten meal using 2709 alkaline protease and flavourzyme showed that the degree of hydrolysis could reach 32.4% with enzyme addition amount of 4%, hy- drolysis time of 4 h at 45℃ and pH=7.0. [Conclusion] This study laid the foundation for the study on the preparation of bioactive peptides such as oligopeptide with high F value and antihypertensive peptides, further improving the corn intensive process- ing industrial chain.展开更多
The kinetics of casein tryptic hydrolysis to prepare activepeptides was investigated. Taking into account the reaction mechanismincluding single substrate hydrolysis, irreversible enzymeinactivation, and substrate inh...The kinetics of casein tryptic hydrolysis to prepare activepeptides was investigated. Taking into account the reaction mechanismincluding single substrate hydrolysis, irreversible enzymeinactivation, and substrate inhibition, a set of exponentialequations was established to characterize the enzymatic hydrolysiscurves. The verification was carried out by a series of experimentalresults and indicated that the average regressive error was less than5/100. According to the proposed kinetic model, the kinetic constantsand thermodynamic constants of the reaction system were alsocalculated.展开更多
Mackerel （Pneumatophorus japonicus） proteins were hydrolyzed by five proteases： trypsin, papain, neutrase, acid protease, and flavourzyme. The hydrolysate treated by neutrase exhibited the highest antioxidant activ...Mackerel （Pneumatophorus japonicus） proteins were hydrolyzed by five proteases： trypsin, papain, neutrase, acid protease, and flavourzyme. The hydrolysate treated by neutrase exhibited the highest antioxidant activity. Response surface methodology （RSM） was employed to optimize the hydrolysis conditions in an effort to obtain a mackerel protein hydrolysate （MPH） with the highest DPPH radical scavenging activity. The MPH was fractioned using a series of ultrafiltration membranes and five fractions, namely, MPH-I （〉10 kDa）, MPH-II （10-2.5 kDa）, MPH-III （1-2.5 kDa）, MPH-IV （0.4-1 kDa）, and MPH-V （below 0.4 kDa）, were obtained. DPPH radical scavenging activity, reducing power, hydroxyl radical scavenging activity, and the lipid peroxidation inhibition capability of these fractions were evaluated. The fractions in molecular weights 〈2.5 kDa （MPH-III, MPH-IV, and MPH-V）, which occupied 93.4% of the total fractions, showed the strongest antioxidant activity; and the antioxidant activities of the three fractions are similar to each other. Using SP Sephadex C-25 and Sephadex G-25 columns, eight fractions were obtained from the MPH （〈2.5 kDa）. The isolated peptide I （1 664 kDa） displayed the highest DPPH radical scavenging activity. Therefore, MPH is a potential source of antioxidant peptides.展开更多
Focus in nutritional science has turned towards components in, or added to, foods that may possess health beneficial activities beyond the classical nutritional value, namely functional food. Bioactive peptides are ex...Focus in nutritional science has turned towards components in, or added to, foods that may possess health beneficial activities beyond the classical nutritional value, namely functional food. Bioactive peptides are examples of such components. In vitro studies on bioactivities have mainly been executed without concerning subsequent digestion after intake and the aim of this work was hence to investigate how the in vitro antioxidative, antihypertensive and caspase activating activities of peptides are affected by digestion with gastrointestinal （GI） proteases. Five different fish protein hydrolysates were chosen to study the effect of in vitro digestion on bioactivity. The protein concentration decreased in all samples during digestion and the molecular weight distribution of the peptides shifted towards lower values. Thus, in vitro digestion with GI proteases resulted in a further degradation of the peptides obtained by hydrolysis. The antihypertensive effect increased in all samples after digestion with GI proteases whereas the antioxidative capacity decreased. The effect on the caspase activity depended on the proteases used in the preparation of hydrolysates. In conclusion, the caspase activity and antihypertensive activity are maintained during digestion with GI proteases, while the antioxidative capacity seems to be reduced.展开更多
文摘[Objective] To investigate the optimal enzyme for the hydrolysis of corn gluten meal and the optimal hydrolysis conditions for the enzyme. [Method] Nine kinds of enzymes were used to hydrolyze the corn gluten meal, using the formaldehyde titration method for the determination of hydrolysis degree, and orthogonal test was used to determine the optimal hydrolysis conditions for double enzymes hydrol- ysis of corn gluten meal. [Result] The optimal pretreatment condition for corn gluten meal is heating at 121 ~C for 30 min. The double enzyme hydrolysis for the pro- treated corn gluten meal using 2709 alkaline protease and flavourzyme showed that the degree of hydrolysis could reach 32.4% with enzyme addition amount of 4%, hy- drolysis time of 4 h at 45℃ and pH=7.0. [Conclusion] This study laid the foundation for the study on the preparation of bioactive peptides such as oligopeptide with high F value and antihypertensive peptides, further improving the corn intensive process- ing industrial chain.
基金Supported by National Natural Science Foundation of China (No. 20276052) and Tianjin Science & Technology Commission (No. 023105411).
文摘The kinetics of casein tryptic hydrolysis to prepare activepeptides was investigated. Taking into account the reaction mechanismincluding single substrate hydrolysis, irreversible enzymeinactivation, and substrate inhibition, a set of exponentialequations was established to characterize the enzymatic hydrolysiscurves. The verification was carried out by a series of experimentalresults and indicated that the average regressive error was less than5/100. According to the proposed kinetic model, the kinetic constantsand thermodynamic constants of the reaction system were alsocalculated.
基金Supported by the Commonweal Item of State Oceanic Administration of the People's Republic of China(Nos.201305016-2,201405038-2)
文摘Mackerel （Pneumatophorus japonicus） proteins were hydrolyzed by five proteases： trypsin, papain, neutrase, acid protease, and flavourzyme. The hydrolysate treated by neutrase exhibited the highest antioxidant activity. Response surface methodology （RSM） was employed to optimize the hydrolysis conditions in an effort to obtain a mackerel protein hydrolysate （MPH） with the highest DPPH radical scavenging activity. The MPH was fractioned using a series of ultrafiltration membranes and five fractions, namely, MPH-I （〉10 kDa）, MPH-II （10-2.5 kDa）, MPH-III （1-2.5 kDa）, MPH-IV （0.4-1 kDa）, and MPH-V （below 0.4 kDa）, were obtained. DPPH radical scavenging activity, reducing power, hydroxyl radical scavenging activity, and the lipid peroxidation inhibition capability of these fractions were evaluated. The fractions in molecular weights 〈2.5 kDa （MPH-III, MPH-IV, and MPH-V）, which occupied 93.4% of the total fractions, showed the strongest antioxidant activity; and the antioxidant activities of the three fractions are similar to each other. Using SP Sephadex C-25 and Sephadex G-25 columns, eight fractions were obtained from the MPH （〈2.5 kDa）. The isolated peptide I （1 664 kDa） displayed the highest DPPH radical scavenging activity. Therefore, MPH is a potential source of antioxidant peptides.
文摘Focus in nutritional science has turned towards components in, or added to, foods that may possess health beneficial activities beyond the classical nutritional value, namely functional food. Bioactive peptides are examples of such components. In vitro studies on bioactivities have mainly been executed without concerning subsequent digestion after intake and the aim of this work was hence to investigate how the in vitro antioxidative, antihypertensive and caspase activating activities of peptides are affected by digestion with gastrointestinal （GI） proteases. Five different fish protein hydrolysates were chosen to study the effect of in vitro digestion on bioactivity. The protein concentration decreased in all samples during digestion and the molecular weight distribution of the peptides shifted towards lower values. Thus, in vitro digestion with GI proteases resulted in a further degradation of the peptides obtained by hydrolysis. The antihypertensive effect increased in all samples after digestion with GI proteases whereas the antioxidative capacity decreased. The effect on the caspase activity depended on the proteases used in the preparation of hydrolysates. In conclusion, the caspase activity and antihypertensive activity are maintained during digestion with GI proteases, while the antioxidative capacity seems to be reduced.
