Oleogels based on peanut protein isolate fibrils: Structural characterization dependent on induction time and suitability in marguerite biscuits

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Food Hydrocolloids 154 (2024) 110106

Available online 16 April 2024

Oleogels based on peanut protein isolate brils: Structural characterization

dependent on induction time and suitability in marguerite biscuits

Kexin Wang , Jie Zhang , Zeyue Fu , Yongxue Luo , Chuanfen Pu , Wenting Tang

, Qingjie Sun

School of Food Science and Engineering, Qingdao Agricultural University, Qingdao, Shandong Province, 266109, China

ARTICLE INFO

Keywords:

Oleogel

Acid-heat

Peanut protein isolate

O/W interface

Fibril

ABSTRACT

In order to develop new plant protein-based lipid substitutes to deal with health problems caused by animal fats

or trans-fatty acids, the emulsion stablized by acid-heat (90 ◦C, pH 2.0) induced aggregation of peanut protein

isolate (PPI) was used as template to fabricate oleogels. Heating time affected the structure, morphology of PPI

and the adsorption characteristics at the O/W interface. The protein with suitable heating time (2–6 h) formed

brils structure, which was benecial to the rapid adsorption of aggregates at the O/W interface. Overheating

(exceeding 8 h) led to the aggregate of protein brils and inhibited the adsorption of proteins at the O/W

interface. Therefore, the heating times of 2 h, 4 h and 6 h were selected to prepare the follow-up emulsion and

oleogels. Among the four heating times, the emulsion prepared by PPI heating for 6 h showed the best storage

stability, ionic strength stability and shear resistance. The resultant oleogels exhibited the least oil loss and the

highest freeze-thaw stability. The margarita biscuits prepared with a substitution rate of 50% oleogels to butter

presented similar sensory property to the margaritas prepared with butter, indicating that the oleogels possessed

favorable shortening properties. The results indicated that PPI brils structure could improve the oleogel for-

maton properties, making it a potential novel additive for the development of new fat substitute products.

1. Introduction

The alternative ingredients that can replace saturated and trans

lipids in foods to reduce their potential health risks and maintain their

original organoleptic attributes have attracted extensive attentions from

food researchers and industry. Oleogel, which a thermally reversible

semisolid lipid mixture with strong viscoelasticity, are composed of

vegetable oil and oleogelators (Aliasl Khiabani, Tabibiazar, Roufegar-

inejad, Hamishehkar, & Alizadeh, 2020; Alvarez-Ramirez,

Vernon-Carter, Carrera-Tarela, Garcia, & Roldan-Cruz, 2020; Okuro,

Martins, Vicente, & Cunha, 2020). It can be designed to mimic the

characteristics typically exhibited by conventional solid fats, but using

liquid vegetable oils with more optimal fatty acid composition. Edible

oleogel is a semisolid material, and liquid oil is trapped in its

three-dimensional network.

Oleogels is considered as a promising candidate to replace animal fat

with vegetable oil, being a research hotspot in the eld of fat substitu-

tion. According to the formation mechanism, the colloidal structures of

oleogel can be achieved through the formation of crystal particle

network, self-assembly network, polymer arrangement and indirect

template (Zhao & Xue, 2021). Among these construction strategies,

emulsion template approach has been believed as an effective method to

form oleogels by entrapping oil phase into biopolymer colloids (Jiang

et al., 2018). The liquid oil has been entrapped into a porous hydrophilic

hydroxypropyl methylcellulose polymer cryogel to obtained a oleogel

with excellent oil sorption ability (Patel et al., 2014). Proteins with high

emulsifying activity can be used as constructor to prepare emulsions and

oleogels. Compared with a single constructor, the synergistic combina-

tion of polysaccharides can stabilize the polymer network and improve

the stability of the oleogels. (Li, Zou, Que, & Zhang, 2022).

Peanut protein isolate (PPI) is a natural nutritional resource extrac-

ted from defatted peanut meal, it has outstanding nutritional value, low

cholesterol content and low cost, so its great potential application in

food industry (Sun, Zhang, Zhang, Tian, & Chen, 2020; Yu, Song, Xiao,

Xue, & Xue, 2022; Zang et al., 2020). Peanut protein contains about 10%

albumin and 90% globulin protein, which is composed of arachidin and

arachidin, of which about 63% is arachidin and 33% is conaracin. PPI

has great application potentials in the food industry. However, its

functional properties still need to be improved to meet specic appli-

cation scenarios. For example, unprocessed PPI can not quickly adsorb

* Corresponding author. No. 700, Changcheng Road, Chengyang District, Qingdao, 266109, China.

E-mail address: twty@126.com (W. Tang).

Contents lists available at ScienceDirect

Food Hydrocolloids

journal homepage: www.elsevier.com/locate/foodhyd

https://doi.org/10.1016/j.foodhyd.2024.110106

Received 28 December 2023; Received in revised form 11 April 2024; Accepted 11 April 2024

Food Hydrocolloids 154 (2024) 110106

on the oil-water interface enough to form a stable emulsion (Zhao, Liu,

Zhao, Ren, & Yang, 2011). Under the induction of acid and heat, pro-

teins denature and then self-assembled to form aggregates, such as -

brils, particles and amorphous structure (Akkermans et al., 2008).

Among these self-assembly behaviors, brosis improves the emulsifying

ability of proteins (Serfert et al., 2014). Compared with natural proteins,

protein brils present higher emulsifying activity and higher emulsi-

fying stability (Gao et ai., 2017a). Protein brillation is considered as a

promising strategy to improve the functional properties of natural pro-

teins in food science (Mohammadian & Madadlou, 2018). However,

there are few reports about the brillation of PPI.

Addition of thickener into the formula can facilitate the oleogels

forming porous microstructure and improve the gel network structure

strength and the oil holding capacity. Proteins and polysaccharides can

be used as thickeners to improve the chemical stability of O/W emulsion

by interfacial complexation (Zhang et al., 2020). The interaction be-

tween proteins and polysaccharides through hydrogen bonding and

hydrophobic interactions can improve the oil holding capacity, rheo-

logical properties and structural properties of the oleogels (Mohanan,

Tang, Nickerson, & Ghosh, 2020). Konjac glucomannan (KGM) is a kind

of high molecular weight water-soluble neutral plant polysaccharide

extracted from konjac tuber (Li et al., 2015; Mao, Klinthong, Zeng, &

Chen, 2012). As a hydrophilic colloid, it usually act as a thickener in

food gel (Huang, Takahashi, Kobayashi, Kawase, & Nishinari, 2002). It

has been proved that the mixture combining KGM with soy protein

isolate (SPI) allowed the corresponding mixed gel to become more stable

than single-KGM gel and single-SPI gel (Wang, Yao, Jian, Sun, & Pang,

2010; Yin & Zhang, 2007).

The purpose of this study was to explore the effects of PPI acid-

thermal denaturation product at different heating time on the stability

and physical properties of emulsion and oleogels and the application

feasibility of the obtained oleogels instead of butter in baking. Firstly,

the interfacial and structural properties of thermally denatured PPI with

different heating time were evaluated and compared. Secondly, the

oleogels was prepared by emulsion-template method and characterized

by rheology, microscope, X-ray diffractometer and Fourier transform

infrared spectroscopy, and the freeze-thaw stabilities of the oleogels

were also investigated. In the end, the sensory evaluation and texture

properties of Marguerite biscuits prepared by partially replacing butter

with oleogels were characterized. Overall, this work attempted to

develop the theoretical basis for the plant-based oleogels recipe, and

expand the application of oleogels as fat replacer products.

2. Materials and methods

2.1. Materials

Peanut protein isolate (PPI) was provided by Yuanye Biotechnology

Co., Ltd (Songjiang, Shanghai Province, China); Soybean oil was bought

from the local supermarket. Konjac glucomannan (KGM, food grade)

was supplied by Qiang Sen konjac Technology Co., Ltd (Ehua, Hubei

Province, China). Thioavin T (Th T) was obtained from Ryon Biological

Technology Co., Ltd (Shanghai, China). Nile red was purchased from BBI

Life Sciences Co. (Shanghai, China). Millipore-Q water was used for the

dissolution of powder samples.

2.2. Preparation of thermal-denatured PPI

The thermal-denatured PPI was prepared according to Liu’s method

with some modication. The PPI suspension (0.08 g/mL, w/v) was

prepared by dispersing the PPI powder in distilled water, the mixture

was stirred at 600 rpm for 4 h and then left overnight at 4 ◦C for full

hydration of the proteins. The pH of the PPI solution after the storage

was adjusted to 2.0 using 1 M HCl. The PPI suspension was heated at

90 ◦C for 2 h, 4 h, 6 h, 8 h, 10 h, and then immediately cooled in an ice

bath to room temperature. The proteins heated for 0h, 2 h, 4 h, 6 h, 8 h

and 10 h were designated as PPI, HPPI

, HPPI

, and

HPPI

10.

2.3. Characterization of PPI and thermal-denatured PPI

2.3.1. Transmission electron microscopy (TEM)

According to the method of Feng et al. (2019), the morphological

characteristics of PPI and thermally denatured PPI were evaluated by

TEM (HT-7700, Hitachi Company, Japan). The samples were diluted 40

times with Milli-Q water. A drop of the sample was transferred to a

copper mesh on the carbon lm, placed for 15 min, and then it was dyed

with 2% uranyl acetate for 8 min. Finally, the treated samples were

observed by transmission electron microscope.

2.3.2. Particle size distribution and zeta potential of PPI and thermal-

denatured PPI

The zeta potential and average particle size of the samples were

measured using dynamic light scattering (DLS) (Nano-ZS90, Malvern,

UK) at 25 ◦C. The sample was diluted to 0.05 mg/mL with millipore-Q

water before each measurement to meet the determination re-

quirements. Next, about 1 mL of the sample was injected into the quartz

cuvette, then the zeta potential and particle size distribution were tested

respectively. All measurements were conducted at 25 ◦C for three times.

The refractive index of the dispersed phase was set to 1.33.

2.3.3. ThT uorescence spectroscopy

The ThT spectroscopic assay was used to monitor the thermal-

denatured PPI over time. The powder of ThT was dissolved in the

phosphate buffer (10 mM, pH 7.0) to prepare the ThT stock solution.

Then the stock solution of ThT was ltered by a 0.22

M lter. The

collected ThT stock solution was diluted 50 times with phosphate buffer

(10 mM, pH 7.0) to obtain the working solution, and then 50

L of the

sample was mixed with 4 mL of the ThT working solution. The con-

centration of ThT working solution was 0.16 mg/mL, and the proteins

concentration detected by THT were 0.8 mg/mL. The ThT uorescence

intensity of the sample was determined with the excitation wavelength

of 440 nm and the emission wavelength of 490 nm using a uorescence

spectrophotometer (F-7000, Hitachi Co., Japan).

According to the results of ThT uorescence, the bril conversion

rate of acid-thermal denaturated PPI was calculated with the following

formula (Suzanne, Leonard, Paul, & Erik, 2007).

Cfibril =K[(IThT −I0)/I0]

Where, C

bril

is the percentage of protein converted into bril, wt%; K is

a linear constant (0.35); I

ThT

and I

are the ThT uorescence intensity of

the sample and the uorescence background value of the working so-

lution, respectively.

2.3.4. Interfacial tension measurement

The interfacial tension of the PPI and the thermal-denatured PPI was

measured using a Drop Shape Analyzer-DSA100 (Krüss GmbH,

Hamburg, Germany) equipped with a hanging drop device for recording

the change of the interfacial tension (

) at the soybean oil–PPI and

thermal-denatured PPI interface with the adsorption time (t). A small

amount of surface active ingredients are present in commercial soybean

oil. Oil purication was thus conducted to prevent interference with the

surface tension results. Purication was performed using a method

described by Gaonkar with modications (Gaonkar, 1989). One percent

(w/v) of silicon-magnesium adsorbent was added to soybean oil, and the

sample was stirred for 2 h at 2000 rpm and then centrifuged at 11,000

rpm for 30 min. This operation was repeated three times. A stainless

steel needle connected to the syringe (outer diameter 1.832 mm) was

inserted into a glass container lled with the puried soybean oil. PPI

and thermal-denatured PPI suspensions diluted with millipore-Q water

to 1000 times were placed in a syringe with a drop on the tip of the

K. Wang et al.

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