Improvement in emulsifying properties of soy protein isolate by conjugation with maltodextrin using high-temperature, short-time dry-heating Maillard reaction

2013 ◽  
Vol 49 (2) ◽  
pp. 460-467 ◽  
Author(s):  
Jinbo Zhang ◽  
Nana Wu ◽  
Ting Lan ◽  
Xiaoquan Yang
Keyword(s):  
High Temperature ◽  
Maillard Reaction ◽  
Soy Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
High Temperature Short Time ◽  
Dry Heating ◽  
Short Time

scholarly journals Exploring the Use of a Modified High-Temperature, Short-Time Continuous Heat Exchanger with Extended Holding Time (HTST-EHT) for Thermal Inactivation of Trypsin Following Selective Enzymatic Hydrolysis of the β-Lactoglobulin Fraction in Whey Protein Isolate

Foods ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 367 ◽  
Author(s):  
Laura Sáez ◽  
Eoin Murphy ◽  
Richard J. FitzGerald ◽  
Phil Kelly
Keyword(s):  
High Temperature ◽  
Heat Exchanger ◽  
Whey Protein ◽  
Protein Isolate ◽  
Holding Time ◽  
High Temperature Short Time ◽  
Incubation Periods ◽  
Short Time ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

Tryptic hydrolysis of whey protein isolate under specific incubation conditions including a relatively high enzyme:substrate (E:S) ratio of 1:10 is known to preferentially hydrolyse β-lactoglobulin (β-LG), while retaining the other major whey protein fraction, i.e., α-lactalbumin (α-LA) mainly intact. An objective of the present work was to explore the effects of reducing E:S (1:10, 1:30, 1:50, 1:100) on the selective hydrolysis of β-LG by trypsin at pH 8.5 and 25 °C in a 5% (w/v) WPI solution during incubation periods ranging from 1 to 7 h. In addition, the use of a pilot-scale continuous high-temperature, short-time (HTST) heat exchanger with an extended holding time (EHT) of 5 min as a means of inactivating trypsin to terminate hydrolysis was compared with laboratory-based acidification to <pH 3 by the addition of HCl, and batch sample heating in a water bath at 85 °C. An E:S of 1:10 resulted in 100% and 30% of β-LG and α-LA hydrolysis, respectively, after 3 h, while an E:S reduction to 1:30 and 1:50 led >90% β-LG hydrolysis after respective incubation periods of 4 and 6 h, with <5% hydrolysis of α-LA in the case of 1:50. Continuous HTST-EHT treatment was shown to be an effective inactivation process allowing for the maintenance of substrate selectivity. However, HTST-EHT heating resulted in protein aggregation, which negatively impacts the downstream recovery of intact α-LA. An optimum E:S was determined to be 1:50, with an incubation time ranging from 3 h to 7 h leading to 90% β-LG hydrolysis and minimal degradation of α-LA. Alternative batch heating by means of a water bath to inactivate trypsin caused considerable digestion of α-LA, while acidification to <pH 3.0 restricted subsequent functional applications of the protein.

scholarly journals Fabricating a Pickering Stabilizer from Okara Dietary Fibre Particulates by Conjugating with Soy Protein Isolate via Maillard Reaction

Foods ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 143 ◽  
Author(s):  
Tolulope Joshua Ashaolu ◽  
Guohua Zhao
Keyword(s):  
Maillard Reaction ◽  
Soy Protein ◽  
Dietary Fibre ◽  
Activity Index ◽  
Soy Protein Isolate ◽  
Stability Index ◽  
Amino Acid Profile ◽  
Protein Isolate ◽  
Interfacial Behaviour ◽  
Droplet Sizes

Okara is underutilized despite its numerous values explorable in food products. In this study, okara dietary fibre (ODF) was micronized and decorated with soy protein isolate (SPI) through a Maillard reaction by dry heating at 60 °C. The resulting ODF-SPI conjugates were thermally stable, hydrophilic rather than hydrophobic, and exhibited excellent Pickering emulsion stabilization potentials as indicated in their interfacial behaviour, microstructure, droplet sizes, emulsifying activity index (EAI) and emulsion stability index (ESI). In addition, the conjugates’ structure–function relationships, amino acid profile, and emulsifying potentials are indicative of being employed in the formulation of emulsion-based foods or non-edible products.

Effect of High Temperature and Humidity in Storage on Emulsibility of Soy Protein Isolate

2014 ◽  
Vol 1004-1005 ◽  
pp. 823-826
Author(s):  
Bing Yu Sun ◽  
Yan Guo Shi ◽  
Lin Lin Liu
Keyword(s):  
High Temperature ◽  
Soy Protein ◽  
Food Industry ◽  
Soy Protein Isolate ◽  
White Paper ◽  
Protein Isolate ◽  
Packaging Material ◽  
Barrier Property ◽  
Sds Page ◽  
Temperature Time

The SPI was applied in food industry widely, but its functionalities may change during storage. The effect of store temperature, time, RH and package material on emulsibility and the component of SPI were studied, when SPI was packaged in 100% N2 and Al, 80%N2:20%CO2 and Al, 60%N2:40% CO2 and Al, vacuum and Al, white paper/plastic/HDPE, and PE and then stored for 5 months in the conditions of RH 80% and 30°C. It was observed by SDS-PAGE that the subunit of SPI disaggregated and molecules aggregated. Comparing the functionalities of SPI with different packaging material, it was shown that the sequence of the barrier property of material to T and RH was Al packaging>factory packaging>PE packaging. Analyzed by relatedness, it was shown that the 7S/11S of SPI with PE packaging storage was not significant with emulsibility. The content of -SH with PE was significantly positive with emulsibility (EAI 0.975**/ESI 0.985**), but the -S-S- of SPI in PE was significantly negative (EAI -0.975**/ESI -0.967**) correlation with emulsibility.

Fabrication and emulsifying properties of non-covalent complexes between soy protein isolate fibrils and soy soluble polysaccharides

2021 ◽  
Author(s):  
Hekai Zhao ◽  
Shengnan Wang ◽  
Guilan Zhao ◽  
Yangyang Li ◽  
Xiulin Liu ◽  
...  
Keyword(s):  
Ir Spectroscopy ◽  
Zeta Potential ◽  
Soy Protein ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Emulsifying Properties ◽  
Oil In Water ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Non-covalent complexes (SPIF/SSPS) between soy protein isolate fibrils (SPIF) and soy soluble polysaccharides (SSPS) were fabricated and used to stabilize oil-in-water (O/W) emulsions. FT-IR spectroscopy and zeta potential results demonstrated...

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