Ice Recrystallization Inhibition Activity of Soy Protein Hydrolysates

Madison Fomich, Vermont P. Día, Uvinduni I. Premadasa, Benjamin Doughty, Hari B. Krishnan, Tong Wang

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Identifying and developing ice recrystallization inhibitors from sustainable food proteins such as soy protein isolate (SPI) can lead to practical applications in both pharmaceutical and food industries. The objective of this study was to investigate the ice recrystallization inhibition (IRI) activity of SPI hydrolysates, and this was achieved by using an IRI activity-guided fractionation approach and relating IRI activity to interfacial molecular activity measured by vibrational sum frequency generation (VSFG). In addition, the impact of molecular weight (MW) and enzyme specificity was analyzed using three different proteases (Alcalase, trypsin, and pancreatin) and varying hydrolysis times. Using preparative chromatography, hydrolysates from each enzyme treatment were fractionated into five different MW fractions (F1-F5), which were then characterized by high-performance liquid chromatography (HPLC). All SPI hydrolysates had IRI activity, resulting in a 57-29% ice crystal diameter reduction when compared to native SPI. The F1 fraction (of 4-14 kDa) was most effective among all tested hydrolysates, while the lower MW peptide fractions lacked activity. One sample (SPI-ALC 20-F1) had a 52% reduction of ice crystal size at a lower concentration of 2% compared to the typical 4% used. SFG showed a difference in H-bonding and hydrophobic interactions of the molecules on the water/air interface, which may be linked to IRI activity. This study demonstrates for the first time the ability of SPI hydrolysates to inhibit ice crystal growth and the potential application of SFG to study molecular interaction at the interface that may help illustrate the mechanism of action.

Original languageEnglish
Pages (from-to)11587-11598
Number of pages12
JournalJournal of Agricultural and Food Chemistry
Volume71
Issue number30
DOIs
StatePublished - Aug 2 2023

Funding

This manuscript has been co-authored by UT-Battelle, LLC, under contract DE-AC05-00OR22725 with the US Department of Energy (DOE). The US government retains and the publisher, by accepting the article for publication, acknowledges that the US government retains a nonexclusive, paid-up, irrevocable, worldwide license to publish or reproduce the published form of this manuscript or allow others to do so, for US government purposes. DOE will provide public access to these results of federally sponsored research in accordance with the DOE Public Access Plan ( http://energy.gov/downloads/doe-public-access-plan ). Acknowledgments This work is supported by an NSF grant [Award Number: 2103558] and Hatch/Multi-state project [Accession Number: 1023982].

FundersFunder number
National Science Foundation1023982, 2103558
U.S. Department of Energy

    Keywords

    • antifreeze peptides
    • enzymatic hydrolysis
    • ice recrystallization inhibition
    • soy protein

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