Krystalia Sarigiannidou, Davide Odelli, F. Jessen, M. Mohammadifar, Fatemeh Ajalloueian, Mar Vall-llosera, A. D. de Carvalho, Federico Casanova
{"title":"Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength","authors":"Krystalia Sarigiannidou, Davide Odelli, F. Jessen, M. Mohammadifar, Fatemeh Ajalloueian, Mar Vall-llosera, A. D. de Carvalho, Federico Casanova","doi":"10.3390/colloids6040076","DOIUrl":null,"url":null,"abstract":"The effect of a tryptic hydrolysis as well as the effect of ionic strength (0–0.4 M NaCl) was investigated on the oil/water interfacial properties of soluble pea protein hydrolysate (SPPH) at neutral pH and room temperature (20 ± 0.01 °C). SEC-MALS and SDS-Page analysis showed that tryptic hydrolysis created a lower molecular weight polypeptide mixture, whereas FTIR analysis and DSC thermograms demonstrated a more disordered and flexible structure. The bulk properties of SPPH were studied in terms of hydrodynamic diameter and turbidity, where higher particle size (+ ~13 nm) and turbidity were observed at 0.4 M NaCl. Regarding the interfacial properties, the surface activity of SPPH improved by increasing ionic strength, with maximum interfacial pressure (14.28 mN/m) at 0.4 M NaCl. Nevertheless, the addition of NaCl negatively affected the elasticity and strength of the interfacial film, where the sample without salt exhibited the highest dilatational and shear storage modulus in all the frequencies considered.","PeriodicalId":10433,"journal":{"name":"Colloids and Interfaces","volume":null,"pages":null},"PeriodicalIF":2.5000,"publicationDate":"2022-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Colloids and Interfaces","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3390/colloids6040076","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 2
Abstract
The effect of a tryptic hydrolysis as well as the effect of ionic strength (0–0.4 M NaCl) was investigated on the oil/water interfacial properties of soluble pea protein hydrolysate (SPPH) at neutral pH and room temperature (20 ± 0.01 °C). SEC-MALS and SDS-Page analysis showed that tryptic hydrolysis created a lower molecular weight polypeptide mixture, whereas FTIR analysis and DSC thermograms demonstrated a more disordered and flexible structure. The bulk properties of SPPH were studied in terms of hydrodynamic diameter and turbidity, where higher particle size (+ ~13 nm) and turbidity were observed at 0.4 M NaCl. Regarding the interfacial properties, the surface activity of SPPH improved by increasing ionic strength, with maximum interfacial pressure (14.28 mN/m) at 0.4 M NaCl. Nevertheless, the addition of NaCl negatively affected the elasticity and strength of the interfacial film, where the sample without salt exhibited the highest dilatational and shear storage modulus in all the frequencies considered.
在中性pH和室温(20±0.01°C)下,研究了胰蛋白酶水解以及离子强度(0–0.4 M NaCl)对可溶性豌豆蛋白水解产物(SPPH)油/水界面性质的影响。SEC-MALS和SDS-Page分析表明,胰蛋白酶水解产生了较低分子量的多肽混合物,而FTIR分析和DSC热谱图显示了更无序和更灵活的结构。从流体动力学直径和浊度的角度研究了SPPH的本体性质,其中在0.4M NaCl下观察到更高的颗粒尺寸(+13nm)和浊度。关于界面性质,SPPH的表面活性通过增加离子强度而提高,在0.4M NaCl下具有最大界面压力(14.28mN/m)。然而,NaCl的添加对界面膜的弹性和强度产生了负面影响,其中不含盐的样品在所有考虑的频率下都表现出最高的膨胀和剪切储能模量。