Flavor-protein interactions for four plant protein isolates and whey protein isolate with aldehydes

3.0 科研～小助 2025-09-01 6 4 2.79MB 8 页 1知币

侵权投诉

LWT - Food Science and Technology 185 (2023) 115177

Available online 14 August 2023

nc-nd/4.0/).

Flavor-protein interactions for four plant protein isolates and whey protein

isolate with aldehydes

Silvia J.E. Snel

, Mirela Pascu

, Igor Bodn´

, Shane Avison

, Atze Jan van der Goot

Michael Beyrer

Institute of Life Technologies, University of Applied Sciences and Arts Western Switzerland, CH-1950, Sion, Switzerland

Food Process Engineering, Agrotechnology and Food Sciences Group, Wageningen University & Research, Bornse Weilanden 9, 6708 WG, Wageningen, the Netherlands

Firmenich S.A., Rue de la Berg`

ere 7, Meyrin 2, CH-1217, Geneva, Switzerland

ARTICLE INFO

Keywords:

Pea

Soy

Chickpea

Faba bean

Covalent interactions

ABSTRACT

Aldehydes are important avor molecules to consider in plant-based products. Here, the avor retention of a

series of saturated aldehydes and mono-unsaturated aldehydes (2-alkenals) with different chain lengths (C4, C6,

C8, and C10) in dispersions with protein isolates of pea, soy, fava bean, chickpea, and whey (as reference) was

analyzed with APCI-TOF-MS. The headspace concentrations of alkenals were lower than aldehydes, meaning

alkenals were retained more than saturated aldehydes. The retention was modeled by assuming hydrophobic

interactions and covalent interactions. The ratio between the hydrophobic interaction parameter and the co-

valent parameter showed that covalent interactions are mainly important for butanal and butenal (C4). For the

other aldehydes, hydrophobic interactions became increasingly important. Correlations were found between the

chemical interaction parameters and the cysteine and methionine content of the different proteins. The obtained

model parameters for each set of proteins and avors allow the prediction of avor retention when developing a

avored product with high protein content.

1. Introduction

Diet patterns must change to be able to feed the growing world

population in a sustainable matter (Aiking & de Boer, 2018; Broekema

et al., 2020). A route to reach this goal is to replace meat and dairy with

plant-based products. Nevertheless, plant-based products are considered

less appealing by consumers, because of their taste and off-notes (Michel

et al., 2021). Currently, a key success factor for plant products that

should replace meat is a high similarity in texture, avor, and nutritional

value. In case of meat, avors are developed when heating the product

(Ramalingam et al., 2019). The heating of meat generates different

volatile avor compounds such as alkenes, alcohols, aldehydes, ketones,

ethers, esters, carboxylic acids, and sulfur-containing compounds (Kale

et al., 2022). Plant-based products do not undergo a similar avor

development and often have distinct avors of their own, which are

frequently perceived as off-notes (Wang et al., 2022). In order to have a

similar avor prole, avor compounds are added to plant-based

products that both mask plant avor and create meat-like avors.

However, avors can strongly interact with the proteins present in

plant-based products, making them less effective (Guichard, 2002).

Protein-avor retention is mostly hydrophobic, but depending on the

type of avor also irreversible covalent interactions, reversible

hydrogen bonds, ionic bonds, and van der Waals’s forces can lead to

avor retention (Wang & Arnteld, 2014). Aldehydes, for example, can

interact covalently with the amine or thiol groups of the proteins, apart

from hydrophobic interactions (Anantharamkrishnan & Reineccius,

2020b). Aldehydes can react in Schiff base formation, whereas alkenals

are also capable of forming Michael adducts (Anantharamkrishnan

et al., 2020a).

An efcient route to determine avor retention is through comparing

the equilibrium headspace concentration in a avored protein disper-

sion to a control without protein (Gremli, 1974; Wang & Arnteld, 2015;

Zhou & Cadwallader, 2006). However, this approach is time-consuming

and therefore often only a few chemicals are studied, which makes it

challenging to get a full overview of avor retention in protein products.

A more pragmatic method is to model experimental data to predict

avor partitioning. Harrison and Hills developed a mathematical model

to predict avor release for both hydrophilic and hydrophobic

* Corresponding author.

E-mail address: michael.beyrer@hevs.ch (M. Beyrer).

Contents lists available at ScienceDirect

LWT

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

https://doi.org/10.1016/j.lwt.2023.115177

Received 21 April 2023; Received in revised form 5 August 2023; Accepted 8 August 2023

LWT 185 (2023) 115177

compounds from a liquid containing macromolecules (Harrison & Hills,

1997). This model was applied to describe avor retention in whey and

sodium caseinate dispersions (Viry et al., 2018). For esters and alcohols,

good predictions were obtained by only assuming hydrophobic in-

teractions to explain avor retention (Viry et al., 2018). For aldehydes,

stronger retention was observed, which was attributed to the specic

covalent interactions that proteins and aldehydes can undergo (Viry

et al., 2018). Therefore, the model was extended with a covalent inter-

action parameter to describe aldehyde retention (Viry et al., 2018).

Recently, this model was applied to predict avor retention in four plant

proteins and whey dispersions with esters, and ketones, assuming hy-

drophobic interactions only (Snel et al., 2023). Apart from esters and

ketones, aldehydes are an important chemical class to consider for the

avoring of plant-based products such as meat analogues. Therefore,

probing the interactions between plant proteins and aldehydes is

essential and could give great insights into the applicability of the model

when covalent interactions are involved. Furthermore, it would high-

light the relative contribution of hydrophobic and covalent interactions

for aldehyde retention.

This study describes the retention of aldehydes by plant proteins and

applies a avor partitioning model to analyze the results. The proteins

studied are pea protein isolate (PPI), soy protein isolate (SPI), chickpea

protein isolate (CPPI), and fava bean protein isolate (FBPI). Besides,

whey protein isolate (WPI) will be included as a control. The investi-

gated avors include a series (C4, C6, C8, C10) of saturated aldehydes

and 2-mono-unsaturated aldehydes (alkenals), from now on addressed

as aldehydes and alkenals. Furthermore, the obtained partitioning pa-

rameters will be correlated with amino acid composition.

2. Theory: avor partitioning models

Harrison and Hills (1997) developed a rst-order mathematical

model to predict avor release from an aqueous solution containing

polymers at equilibrium conditions. In the case of proteins, avors can

interact with the proteins through either hydrophobic interactions or

specic covalent interactions. The avor-partitioning model will be

shortly summarized here. The partition coefcient (Kf

wg)at equilibrium

between avor concentration in the water phase (ce

fw)and gas phase (ce

fg)

is dened as:

wg =ce

(1)

When protein is added to the water phase, part of the avors could

interact with the protein. When we consider that the avor-protein

interaction is a reversible, rst-order reaction, the global interaction

constant (Kf

p)between protein P and avor F is dened as:

p=ce

pce

(2)

in which ce

fp and ce

p are the concentrations of protein-retained avor in

the dispersion at equilibrium, and protein. Since in the experimental set-

up, protein concentration exceeds the avor concentration largely, c

simplied as the total concentration of protein in the dispersion that

thus remains constant during the experiment. Now, the effective parti-

tion coefcient Keff

wg between avor in the gas phase and the water-

protein phase becomes:

Keff

wg =ce

(3)

in which ce

ft is the total avor in the water system. The mass balance

reads:

cft =cfp +cfw (4)

In which c

equals c

when no protein is present in the water phase.

Using the mass balance and eq. (1) and eq. (2), we can describe Keff

wg as:

Keff

wg =Kf

1+Kf

pce

(5)

When avor retention is dominated by hydrophobic interactions, we

could approach the interaction constant with:

p=apPf

ow (6)

in which a

and Pf

ow are the hydrophobic interaction parameter and the

octanol-water partition coefcient. For aldehydes, the covalent inter-

action has to be taken into account, leading to (Viry et al., 2018):

p=apPf

ow +KAld (7)

in which K

Ald

is the covalent interaction parameter between aldehydes

and proteins. For alkenals, this parameter becomes K

alk

. Aldehydes can

interact with proteins through a condensation reaction (Schiff base

adduct), and alkenals can have an additional conjugate addition

(Michael adduct, Fig. 1) (Anantharamkrishnan et al., 2020a). The total

contribution of both reactions is captured in the parameters K

ald

or K

alk

3. Methods and materials

3.1. Materials

Soy protein isolate (SPI, Supro® 500E A) was obtained from Solae

(St. Louis, United States). Pea protein isolate (PPI, Nutralys® F85M) was

obtained from Roquette Fr`

eres S.A. (Lestrem, France). Fava bean protein

isolate (FBPI, FFBP-90-C-EU) and chickpea protein isolate (CPPI, FCPP-

70) were both obtained from AGT Foods (Regina, Canada). Whey pro-

tein isolate (WPI, BiPRO) was obtained from Davisco Foods Interna-

tional (Minnesota, USA). Amino acid content was measured in a

Fig. 1. Schematical representation of the chemical reactions possible between

the amine group of amino acids and butanal (A), and trans-2-butenal (B), and

the thiol group of cysteine with trans-2-butenal (C) (Anantharamkrishnan &

Reineccius, 2020b). Butanal and trans-2-butenal are chosen in this example to

represent aldehydes and alkenals respectively. SB =schiff base, MA =

michael adduct.

S.J.E. Snel et al.

文档加载中……请稍候！
如果长时间未打开，您也可以点击刷新试试。

下载文档到电脑，查找使用更方便

1 知币 4人已下载

立即下载

Flavor-protein interactions for four plant protein isolates and whey protein isolate with aldehydes.pdf

共8页,预览3页

还剩页未读，继续阅读

Flavor-protein interactions for four plant protein isolates and whey protein isolate with aldehydes

相关推荐

开通VIP享超值会员特权

作者详情

相关内容

推荐作者

热门标签

举报选择: