Targeted inactivation of soybean proteinase inhibitors using zinc

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Targeted inactivation of soybean proteinase inhibitors using zinc. / Rehder, Alina; Sørensen, Jens Christian; Markedal, Keld Ejdrup; Sørensen, Hilmer; Sørensen, Susanne; Petersen, Iben Lykke.

In: Food Chemistry, Vol. 349, 129049, 2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rehder, A, Sørensen, JC, Markedal, KE, Sørensen, H, Sørensen, S & Petersen, IL 2021, 'Targeted inactivation of soybean proteinase inhibitors using zinc', Food Chemistry, vol. 349, 129049. https://doi.org/10.1016/j.foodchem.2021.129049

APA

Rehder, A., Sørensen, J. C., Markedal, K. E., Sørensen, H., Sørensen, S., & Petersen, I. L. (2021). Targeted inactivation of soybean proteinase inhibitors using zinc. Food Chemistry, 349, [129049]. https://doi.org/10.1016/j.foodchem.2021.129049

Vancouver

Rehder A, Sørensen JC, Markedal KE, Sørensen H, Sørensen S, Petersen IL. Targeted inactivation of soybean proteinase inhibitors using zinc. Food Chemistry. 2021;349. 129049. https://doi.org/10.1016/j.foodchem.2021.129049

Author

Rehder, Alina ; Sørensen, Jens Christian ; Markedal, Keld Ejdrup ; Sørensen, Hilmer ; Sørensen, Susanne ; Petersen, Iben Lykke. / Targeted inactivation of soybean proteinase inhibitors using zinc. In: Food Chemistry. 2021 ; Vol. 349.

Bibtex

@article{8d4ebe1763b14b94b193bfcbfb30c901,
title = "Targeted inactivation of soybean proteinase inhibitors using zinc",
abstract = "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.",
keywords = "BBI, Bowman-Birk inhibitor, DTT, Glutathione, KTI, Kunitz family, MECC, Serine proteinase inhibitor, Trypsin inhibitor, Zinc",
author = "Alina Rehder and S{\o}rensen, {Jens Christian} and Markedal, {Keld Ejdrup} and Hilmer S{\o}rensen and Susanne S{\o}rensen and Petersen, {Iben Lykke}",
year = "2021",
doi = "10.1016/j.foodchem.2021.129049",
language = "English",
volume = "349",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Targeted inactivation of soybean proteinase inhibitors using zinc

AU - Rehder, Alina

AU - Sørensen, Jens Christian

AU - Markedal, Keld Ejdrup

AU - Sørensen, Hilmer

AU - Sørensen, Susanne

AU - Petersen, Iben Lykke

PY - 2021

Y1 - 2021

N2 - 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.

AB - 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.

KW - BBI

KW - Bowman-Birk inhibitor

KW - DTT

KW - Glutathione

KW - KTI

KW - Kunitz family

KW - MECC

KW - Serine proteinase inhibitor

KW - Trypsin inhibitor

KW - Zinc

U2 - 10.1016/j.foodchem.2021.129049

DO - 10.1016/j.foodchem.2021.129049

M3 - Journal article

C2 - 33581435

AN - SCOPUS:85100658113

VL - 349

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

M1 - 129049

ER -

ID: 257975359