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LWT - Food Science and Technology
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Efects of dielectric barrier discharge cold plasma treatment on the structure
and binding capacity of aroma compounds of myofbrillar proteins from dry-
cured bacon
Ji Luo
a
, Mustapha Muhammad Nasiru
a
, Wenjing Yan
a
, Hong Zhuang
b
, Guanghong Zhou
a
,
Jianhao Zhang
a,∗
a
National Center of Meat Quality and Safety Control, Synergetic Innovation Center of Food Safety and Nutrition, College of Food Science and Technology, Nanjing
Agricultural University, Nanjing, Jiangsu, 210095, PR China
b
Quality and Safety Assessment Research Unit, 950 College Station Road, Athens, GA, 30605, United States
ARTICLE INFO
Keywords:
Cold plasma
Myofbrillar protein
FTIR spectroscopy
Secondary structure
Binding ability
ABSTRACT
The aim of this work was to investigate the infuence of dielectric barrier discharge cold plasma (DBD-CP) on the
structure and aroma compounds binding capacity of myofbrillar proteins (MPs) extracted from Chinese dry-
cured bacon. MPs were treated with DBD-CP at 0, 50, 60 and 70 kV for 150s to monitor the binding ability with
aroma compounds such as 3-methyl-butanal, 2-methyl-butanal, nonanal, heptanal and octanal, microstructure,
primary and secondary structure changes of MPs using GC-MS, SDS-PAGE, scanning electron microscope (SEM)
and FTIR spectroscopy. FTIR spectroscopy revealed a decrease in the α-helices structure while an increasing
portion of β-sheets and random coils for all treatments, the relative contents of β-turns had no signifcant dif-
ference between treatments. The favor compounds binding capacity of MPs enhanced from 50 kV to 70 kV
treatment, probably due to the diferent modifcations in protein structure and surface, also the oxidation sys-
tems generated by DBD-CP treatment increased hydrophobicity and unfolding of MPs. The result also showed
that hydrophobic amino acids increased from 50 kV to 70 kV treatment which could be related to the im-
provement of binding ability. This study demonstrated that DBD-CP could be exploited to modify the func-
tionality of MPs and improve the favor of meat products.
1. Introduction
The favor characteristics can strongly afect the quality of meat
products, such as the kinds, content and odor threshold of volatiles, also
the interaction between them and protein (Lv et al., 2017; Pérez-Juan,
Flores, & Toldrá, 2008). In order to better comprehend the interaction
between proteins and aroma compounds from dry-cured meat products
and promote the favor properties of meat products, we need to concern
about the species and amount favor component, the functional prop-
erties of protein, the quantity and quality of protein, the ionic strength
of the medium and temperature (Gianelli, Flores, & Toldrá, 2003).
Meat MPs have hardly any favor of their own, however, they have
binding ability with volatiles. The binding between proteins and aroma
compounds includes reversible and irreversible ways (Pérez-Juan et al.,
2008). In addition, the major constituent of MPs has great impact on the
binding ability of meat products (Asghar, Samejima, & Yasui, 1985).
It has been demonstrated that the binding capability of MPs with
favor compounds is related with the structures change of amino acid
side chain, especially hydrophobic bonding, intermolecular force, ionic
bonding, hydrogen bonding, and disulfde bond (Wang & Arntfeld,
2017). The change of protein conformation is a major factor in ab-
sorbing and release of volatiles. Zhou, Zhao, Su, and Sun (2014) studied
the infuences of oxidative modifed on the binding capacity of MPs
with aroma compounds. Pérez-Juan, Flores, and Toldrá (2006) com-
pared the diference characteristic favor compounds binding capability
between raw pork protein and dry-cured ham protein. Martinez-
Arellano, Flores, and Toldra (2016) also reported the binding ability of
peptides extracted from dry-cured ham at diferent ripening process to
the aroma compounds. Zhou, Zhao, Cui, and Sun (2015) demonstrated
that oxidative modifed could alter physicochemical and functional
properties of MPs which was mainly caused by the signifcant variation
of secondary and tertiary conformation of them.
Cold plasma (CP), as a partially or completely ionized gas, is con-
sidered as the fourth state of matter which consists of positive and
https://doi.org/10.1016/j.lwt.2019.108606
Received 22 May 2019; Received in revised form 18 July 2019; Accepted 7 September 2019
∗
Corresponding author.
E-mail address: nau_zjh@njau.edu.cn (J. Zhang).
LWT - Food Science and Technology 117 (2020) 108606
Available online 11 September 2019
0023-6438/ © 2019 Elsevier Ltd. All rights reserved.
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