Heat induced gelation of pulse protein networks

Burcu Guldiken; Jarvis Stobbs; Michael Nickerson

doi:10.1016/j.foodchem.2021.129158

Heat induced gelation of pulse protein networks

Food Chem. 2021 Jul 15:350:129158. doi: 10.1016/j.foodchem.2021.129158. Epub 2021 Jan 27.

Authors

Burcu Guldiken¹, Jarvis Stobbs², Michael Nickerson³

Affiliations

¹ Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, SK S7N 5A8, Canada.
² Canadian Light Source Inc., 44 Innovation Boulevard, Saskatoon, SK S7N 2V3, Canada.
³ Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, SK S7N 5A8, Canada. Electronic address: Michael.Nickerson@usask.ca.

PMID: 33610848
DOI: 10.1016/j.foodchem.2021.129158

Abstract

This study examines the effect of salts (0.5 M NaCl or 0.25 M CaCl₂) and protein concentration (7.5-15%) on the gel-forming abilities of lentil (LPC), yellow pea (YPC), and faba bean (FPC) protein concentrates formed at pH 7.0. The surface hydrophobicity of YPC (84.8 arbitrary units, a.u.) was found to be lower than LPC (147.2 a.u.) and FPC (135.0 a.u.). In contrast, the surface charge for LPC, YPC, and FPC was -37.8, -28.4, and -29.3 mV, respectively. The Lg/Vn ratio of YPCs was determined as 0.65 followed by LPC (0.57) and FPC (0.41). The presence of salts reduced the least gelling concentration. LPC and FPC also appeared to have a more ordered structure than YPC as evident by CLSM. The network appeared more ordered as the protein concentration increased or in the presence of NaCl or CaCl₂ according to CLSM and synchrotron based micro computed tomography (µCT).

Keywords: Heat-induced gelation; Lg/Vn; Pulse proteins; Rheology; SDS-page; Synchrotron X-ray microcomputed tomography.

MeSH terms

Gels
Hot Temperature*
Hydrogen-Ion Concentration
Plant Proteins / chemistry*
Sodium Chloride / chemistry

Substances

Gels
Plant Proteins
Sodium Chloride