Heat inactivation kinetics of trypsin inhibitors during high temperature-short time processing of soymilk

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Standard

Heat inactivation kinetics of trypsin inhibitors during high temperature-short time processing of soymilk. / Rouhana, Amal; Adler-Nissen, Jens; Cogan, Uri; Frøkiær, Hanne.

I: Journal of Food Science, Bind 61, Nr. 2, 1996, s. 265-269.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Rouhana, A, Adler-Nissen, J, Cogan, U & Frøkiær, H 1996, 'Heat inactivation kinetics of trypsin inhibitors during high temperature-short time processing of soymilk', Journal of Food Science, bind 61, nr. 2, s. 265-269. https://doi.org/10.1111/j.1365-2621.1996.tb14173.x

APA

Rouhana, A., Adler-Nissen, J., Cogan, U., & Frøkiær, H. (1996). Heat inactivation kinetics of trypsin inhibitors during high temperature-short time processing of soymilk. Journal of Food Science, 61(2), 265-269. https://doi.org/10.1111/j.1365-2621.1996.tb14173.x

Vancouver

Rouhana A, Adler-Nissen J, Cogan U, Frøkiær H. Heat inactivation kinetics of trypsin inhibitors during high temperature-short time processing of soymilk. Journal of Food Science. 1996;61(2):265-269. https://doi.org/10.1111/j.1365-2621.1996.tb14173.x

Author

Rouhana, Amal ; Adler-Nissen, Jens ; Cogan, Uri ; Frøkiær, Hanne. / Heat inactivation kinetics of trypsin inhibitors during high temperature-short time processing of soymilk. I: Journal of Food Science. 1996 ; Bind 61, Nr. 2. s. 265-269.

Bibtex

@article{7cf809cdf4f04f42a811cd43f03391d6,
title = "Heat inactivation kinetics of trypsin inhibitors during high temperature-short time processing of soymilk",
abstract = "Heat treatment of soymilk was studied in the conventional batch boiling process and under High Temperature-Short Time (HTST) conditions. Reduction in total trypsin inhibitor was assayed enzymatically, and individual inhibitors, the Kunitz and the Bowman-Birk inhibitor, were assayed by ELISA technique. Standard first-order reaction kinetics and thermodynamics were applicable for inactivation, and results indicated that the mechanism was not protein unfolding, because entropy changes were zero or negative. The two inhibitors were inactivated at the same rate around 137°C. Therefore, a simple first-order kinetic model which gave a good, slightly conservative estimate of residual anti-trypsin activity under HTST conditions could be established.",
keywords = "High temperature-short time (HTST), Soymilk, Trypsin inhibitors",
author = "Amal Rouhana and Jens Adler-Nissen and Uri Cogan and Hanne Fr{\o}ki{\ae}r",
year = "1996",
doi = "10.1111/j.1365-2621.1996.tb14173.x",
language = "English",
volume = "61",
pages = "265--269",
journal = "Journal of Food Science",
issn = "0022-1147",
publisher = "Wiley-Blackwell",
number = "2",

}

RIS

TY - JOUR

T1 - Heat inactivation kinetics of trypsin inhibitors during high temperature-short time processing of soymilk

AU - Rouhana, Amal

AU - Adler-Nissen, Jens

AU - Cogan, Uri

AU - Frøkiær, Hanne

PY - 1996

Y1 - 1996

N2 - Heat treatment of soymilk was studied in the conventional batch boiling process and under High Temperature-Short Time (HTST) conditions. Reduction in total trypsin inhibitor was assayed enzymatically, and individual inhibitors, the Kunitz and the Bowman-Birk inhibitor, were assayed by ELISA technique. Standard first-order reaction kinetics and thermodynamics were applicable for inactivation, and results indicated that the mechanism was not protein unfolding, because entropy changes were zero or negative. The two inhibitors were inactivated at the same rate around 137°C. Therefore, a simple first-order kinetic model which gave a good, slightly conservative estimate of residual anti-trypsin activity under HTST conditions could be established.

AB - Heat treatment of soymilk was studied in the conventional batch boiling process and under High Temperature-Short Time (HTST) conditions. Reduction in total trypsin inhibitor was assayed enzymatically, and individual inhibitors, the Kunitz and the Bowman-Birk inhibitor, were assayed by ELISA technique. Standard first-order reaction kinetics and thermodynamics were applicable for inactivation, and results indicated that the mechanism was not protein unfolding, because entropy changes were zero or negative. The two inhibitors were inactivated at the same rate around 137°C. Therefore, a simple first-order kinetic model which gave a good, slightly conservative estimate of residual anti-trypsin activity under HTST conditions could be established.

KW - High temperature-short time (HTST)

KW - Soymilk

KW - Trypsin inhibitors

UR - http://www.scopus.com/inward/record.url?scp=0000478363&partnerID=8YFLogxK

U2 - 10.1111/j.1365-2621.1996.tb14173.x

DO - 10.1111/j.1365-2621.1996.tb14173.x

M3 - Journal article

AN - SCOPUS:0000478363

VL - 61

SP - 265

EP - 269

JO - Journal of Food Science

JF - Journal of Food Science

SN - 0022-1147

IS - 2

ER -

ID: 331794886