Targeted inactivation of soybean proteinase inhibitors using zinc

•Model system to study disulfide bond reduction successfully monitored by MECC.•Metallic zinc proved to be an effective reductant for proteinase inhibitors (PI).•Activity of KTI was reduced by 72% and BBI by 85% using zinc.•Reduction potential of zinc comparable to that of DTT for TI activity.•Reduc...

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Bibliographic Details
Published in:Food chemistry 2021-07, Vol.349, p.129049-129049, Article 129049
Main Authors: Rehder, Alina, Sørensen, Jens Christian, Markedal, Keld Ejdrup, Sørensen, Hilmer, Sørensen, Susanne, Petersen, Iben Lykke
Format: Article
Language:English
Subjects:
BBI
Bowman-Birk inhibitor
Disulfides - chemistry
DTT
Enzyme Activation - drug effects
Glutathione
KTI
Kunitz family
MECC
Serine proteinase inhibitor
Trypsin inhibitor
Trypsin Inhibitor, Bowman-Birk Soybean - chemistry
Trypsin Inhibitor, Bowman-Birk Soybean - metabolism
Trypsin Inhibitor, Kunitz Soybean - chemistry
Trypsin Inhibitor, Kunitz Soybean - metabolism
Zinc
Zinc - pharmacology
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Summary:•Model system to study disulfide bond reduction successfully monitored by MECC.•Metallic zinc proved to be an effective reductant for proteinase inhibitors (PI).•Activity of KTI was reduced by 72% and BBI by 85% using zinc.•Reduction potential of zinc comparable to that of DTT for TI activity.•Reduction in proteinase inhibitor activity coincides with disulfide bond reduction. In this study the potential targeted use of zinc to inactivate proteinase inhibitors (PI) has been investigated as an alternative to the widely applied heat treatment used industrially for inactivation of PI. Zinc was utilized for the reduction of disulfide bonds leading to the structural changes in proteins, thus affecting the decreased affinity between PI and proteinases. The protein disulfide bond reduction mechanism was studied using a newly developed micellar electrokinetic capillary chromatography (MECC) with the glutathione redox reaction with dithiothreitol (DTT) as model system. This model proved efficient in monitoring the reduction of disulfide bonds in the Kunitz trypsin inhibitor (KTI) and Bowman-Birk inhibitor (BBI). The use of zinc as a reductant resulted in a significant reduction of trypsin inhibitor activity (TIA) of 72% for KTI and 85% for BBI, highlighting zinc as a promising potential agent to reduce the activity of PI as an alternative to heat treatment.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2021.129049