Chymotryptic hydrolysis of β-lactoglobulin (β-lg) leads to the release of a wide range of biofunctional peptides.However,the proteolysis of native β-lg is limited due to its compact globular structure,thus ending w...Chymotryptic hydrolysis of β-lactoglobulin (β-lg) leads to the release of a wide range of biofunctional peptides.However,the proteolysis of native β-lg is limited due to its compact globular structure,thus ending with low yields of peptides.Whereas our previous study showed that eco-efficient High Voltage Electric Treatments (HVET),namely Pulsed Electric Fields (PEF) and Electric Arc (ARC),of β-lg substantially improved its enzymatic hydrolysis,no information regarding the nature of released peptides is available up to date.Hence,the time-dependent release of peptides and the dynamics of this release were discussed in the current study.Chromatographic analysis of the final hydrolysates showed that chymotrypsinolysis of HVET samples released 19% more peptides with higher concentration than the native and preheated ones.Furthermore,1-min HVET were found to be more efficient than 10-min ones as they led to the release of bioactive peptides (even without chymotrypsin) with higher eco-efficiency scores.展开更多
基金the Natural Sciences and Engineering Research Council of Canada(NSERC),Discovery grant RGPIN-2017-05970 for funding this project。
文摘Chymotryptic hydrolysis of β-lactoglobulin (β-lg) leads to the release of a wide range of biofunctional peptides.However,the proteolysis of native β-lg is limited due to its compact globular structure,thus ending with low yields of peptides.Whereas our previous study showed that eco-efficient High Voltage Electric Treatments (HVET),namely Pulsed Electric Fields (PEF) and Electric Arc (ARC),of β-lg substantially improved its enzymatic hydrolysis,no information regarding the nature of released peptides is available up to date.Hence,the time-dependent release of peptides and the dynamics of this release were discussed in the current study.Chromatographic analysis of the final hydrolysates showed that chymotrypsinolysis of HVET samples released 19% more peptides with higher concentration than the native and preheated ones.Furthermore,1-min HVET were found to be more efficient than 10-min ones as they led to the release of bioactive peptides (even without chymotrypsin) with higher eco-efficiency scores.
