TY - JOUR

T1 - Differences in physicochemical properties of high-moisture extrudates prepared from soy and pea protein isolates

AU - Wang, Hong

AU - van den Berg, Frans W.J.

AU - Zhang, Wei

AU - Czaja, Tomasz Pawel

AU - Zhang, Longteng

AU - Jespersen, Birthe Møller

AU - Lametsch, René

N1 - Funding Information: This work was supported by DeePro Technology Co., Ltd. The authors thank Anders Lybecker Christiani (University of Copenhagen) for his training for the extruder. The authors would like to thank Catherine Anne Skrzynski Nielsen (Center for Advanced Bioimaging, University of Copenhagen) and Klaus Qvortrup (Core Facility for Integrated Microscopy, University of Copenhagen) for their assistance in SEM analysis. Additionally, the authors were grateful to Yuhui Ye for the supplementary color evaluation measurements for the raw SPI and PPI powders. Funding Information: This work was supported by DeePro Technology Co. Ltd. The authors thank Anders Lybecker Christiani (University of Copenhagen) for his training for the extruder. The authors would like to thank Catherine Anne Skrzynski Nielsen (Center for Advanced Bioimaging, University of Copenhagen) and Klaus Qvortrup (Core Facility for Integrated Microscopy, University of Copenhagen) for their assistance in SEM analysis. Additionally, the authors were grateful to Yuhui Ye for the supplementary color evaluation measurements for the raw SPI and PPI powders. Publisher Copyright: © 2022 The Authors

PY - 2022

Y1 - 2022

N2 - This study aimed to compare the physicochemical properties of high-moisture extrudates prepared from soy protein isolate (SPI) and pea protein isolate (PPI) at different barrel temperatures (BTs) of 120 °C, 140 °C, and 160 °C. Increasing BT promoted more anisotropic structures and darker extrudates. PPI extrudates produced more fibrous structures than SPI extrudates under the same BT. Textural and rheological properties of SPI extrudates elevated significantly with increasing BT. Compared to SPI extrudates at the same BT, PPI extrudates displayed apparently weaker shear thinning (gel-like) behavior and showed less textural properties of hardness, chewiness, and tensile strength. PPI extrudates showed no significant differences in hardness and chewiness to the cooked chicken breast. Heat-treatment during low-field nuclear magnetic resonance (LF-NMR) measurements promoted the release of intra-space water of the fibrous structure for both SPI and PPI extrudates. Water in PPI extrudates was more prone to migrate compared to SPI extrudates. Hydrogen bonds and hydrophobic interactions played marginally more essential roles than the disulfide bonds to stabilize protein structure for both SPI and PPI extrudates. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that most protein subunits were still present after extrusion, except two bands over 100 kDa in SPI extrudates extracted by phosphates buffer. This study provided valuable information for improving the quality of high-moisture extrudates based on SPI and PPI.

AB - This study aimed to compare the physicochemical properties of high-moisture extrudates prepared from soy protein isolate (SPI) and pea protein isolate (PPI) at different barrel temperatures (BTs) of 120 °C, 140 °C, and 160 °C. Increasing BT promoted more anisotropic structures and darker extrudates. PPI extrudates produced more fibrous structures than SPI extrudates under the same BT. Textural and rheological properties of SPI extrudates elevated significantly with increasing BT. Compared to SPI extrudates at the same BT, PPI extrudates displayed apparently weaker shear thinning (gel-like) behavior and showed less textural properties of hardness, chewiness, and tensile strength. PPI extrudates showed no significant differences in hardness and chewiness to the cooked chicken breast. Heat-treatment during low-field nuclear magnetic resonance (LF-NMR) measurements promoted the release of intra-space water of the fibrous structure for both SPI and PPI extrudates. Water in PPI extrudates was more prone to migrate compared to SPI extrudates. Hydrogen bonds and hydrophobic interactions played marginally more essential roles than the disulfide bonds to stabilize protein structure for both SPI and PPI extrudates. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that most protein subunits were still present after extrusion, except two bands over 100 kDa in SPI extrudates extracted by phosphates buffer. This study provided valuable information for improving the quality of high-moisture extrudates based on SPI and PPI.

KW - Barrel temperature

KW - Fibrous structure

KW - High-moisture extrusion

KW - Pea protein isolate

KW - Soy protein isolate

U2 - 10.1016/j.foodhyd.2022.107540

DO - 10.1016/j.foodhyd.2022.107540

M3 - Journal article

AN - SCOPUS:85124659798

VL - 128

JO - Food Hydrocolloids

JF - Food Hydrocolloids

SN - 0268-005X

M1 - 107540

ER -