Effects of Mild Oxidative and Structural Modifications Induced by Argon

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Functional Structure/Activity Relationships

Effects of Mild Oxidative and Structural Modifications Induced by Argon-Plasma on Physicochemical Properties of Actomyosin from King Prawn (Litopenaeus Vannamei) Flora-Glad Chizoba Ekezie, J-H Cheng, and Da-Wen Sun J. Agric. Food Chem., Just Accepted Manuscript • DOI: 10.1021/acs.jafc.8b05178 • Publication Date (Web): 19 Nov 2018 Downloaded from http://pubs.acs.org on November 22, 2018

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Journal of Agricultural and Food Chemistry

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Effects of Mild Oxidative and Structural Modifications Induced by

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Argon-Plasma on Physicochemical Properties of Actomyosin from King

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Prawn (Litopenaeus Vannamei)

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Flora-Glad Chizoba Ekezie a,b,c, Jun-Hu Cheng a,b,c, Da-Wen Sun a,b,c,d

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a School b Academy

of Contemporary Food Engineering, South China University of Technology, Guangzhou Higher Education Mega

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of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China

Center, Guangzhou 510006, China c Engineering

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and Technological Research Centre of Guangdong Province on Intelligent Sensing and Process Control of Cold Chain Foods, Guangzhou Higher Education Mega Centre, Guangzhou 510006, China

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d Food

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Refrigeration and Computerized Food Technology, University College Dublin, National University of Ireland, Agriculture and Food Science Centre, Belfield, Dublin 4, Ireland

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Abstract

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In the present work, the structure and physicochemical properties of natural actomyosin (NAM)

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extracted from king prawn (Litopenaeus vannamei) and subjected to atmospheric pressure plasma jet

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(APPJ) generated in argon gas as a function of treatment time were examined. The results revealed that

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prawn NAM exhibited a correlating decrease in pH from 7.06 ± 0.03 to 6.92 ± 0.02 and slight increase

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(P > 0.05) in solubility 91.89 ± 1.57 to 96.86 ± 1.19 within the first few min of plasma exposure due to

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the formation of soluble aggregates. A rise in turbidity was also noted, confirming the occurrence of

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protein aggregation. These changes were also accompanied by a rise in emulsifying activity from 48.96

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± 1.66 to 67.31 ± 1.39 m2/g (P < 0.05) and nearly 50 % increase in foaming capacity after 5 min APPJ



Corresponding author. Tel: +353-1-7167342, Fax: +353-1-7167493, E-mail: [email protected], Website: www.ucd.ie/refrig; www.ucd.ie/sun

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exposure. The modulation of these properties occurred as a result of conformational changes in NAM

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evident by various complementary structural analyses conducted. Overall, these findings show that mild

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oxidation from argon plasma can be used for modification of protein functionality and emphasizes the

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need for optimal selection of plasma processing conditions.

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Keywords: Plasma species, actomyosin, structure, physicochemical changes, king prawn, muscle

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protein

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1.

Introduction

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Seafood items such as prawns and shrimps are highly consumed worldwide, contributing to

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approximately 16 % of global export value for fishery products. 1-3 They are widely available in the USA

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market with the prawn specie Litopenaeus vannamei also known as king prawn, one of the most popular

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species in the aquaculture industry. This specie of prawn is highly sort after not only for its rich flavor,

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moist flesh and low cholesterol level but also for its high biological value or protein content. An

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interesting subject of investigation in literature is the functionality of muscle proteins and its close

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relationship with protein structure and conformation. Protein-protein interactions such as aggregation,

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association and polymerization, are a result of changes in both secondary and tertiary structures of

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protein molecules, with implications on their physiochemical characteristics. These protein-protein

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interactions are reliant on certain factors such as temperature, pH and ionic strength.4 Natural

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actomyosin (NAM) comprising of myosin and actin is a principal component of muscle proteins. It is

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also an important criterion for judging the suitability of muscle meat processing, owing to its functional

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properties including alteration of spatial advanced structure, protein aggregation, solubility and water-

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holding capacity (WHC) and its influence on the texture of meat products.4 Additionally, an important

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characteristic of NAM complexes is its crucial role in gelation for determining the quality of fish mince 2 ACS Paragon Plus Environment


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and surimi products. To achieve adequate water holding capacity and binding properties, it is important

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to increase the elution level of myosin and actomyosin. Actomyosin is considered more soluble in high

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ionic strength (0.6 M KCl/NaCl solution) but lower salt concentration (0.05) in the intensity of bands of myosin and actin subunits between the

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untreated and different plasma-treated samples was observed in reducing conditions (Fig. 4b), which

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suggested that the plasma gas could not change the NAM molecular weight or cause breakage of the

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polypeptide chain at different time durations used in the current study. Analogously, no noticeable

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changes in actin were seen with increasing plasma exposure time. These results of electrophoretic

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patterns were also confirmed earlier.43 They reported that the number and intensity of various

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polypeptide bands of untreated and DBD-treated peanut protein samples were intact and no additional

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fragments were formed. The inclusion of DTT (dithiothreitol), which is a reducing agent used for

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disruption of S-S bonds, allows NAM proteins to assume a random coil conformation and promote

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better size separation of proteins in SDS-PAGE gels.

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On the other hand, under non-reducing conditions, the actin bands appear to be slightly affected

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as plasma treatment time progressed (Fig. 4a). This also applies to the myosin portions. These results

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suggested that the main obvious difference between results in Fig. 4a and 4b may be due to the oxidation

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in the sulfhydryl group and the subsequent formation of disulphide bonds. The remnant polymers that

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appeared at the top of the stacking gels may be due to the presence of covalent bonds, such as Tyr-Tyr,

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and active interactions of carbonyl-NH2. In general, the current results on conformational changes of

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actomyosin indicate that high energetic species provided by argon plasma may be able to dissociate

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some polypeptides present in NAM at the primary level. Though the interaction between major proteins


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may be destabilized, losses in band intensities associated with plasma species may be more apparent at

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longer treatment times or for different experimental setups.

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Effects on surface hydrophobicity and total sulfhydryl groups

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The significance of protein hydrophobicity in the structure-function relationship of various food

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proteins as affected by different treatments and/or processes cannot be overemphasized. Normally,

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protein hydrophobicity can be categorized as either aromatic or aliphatic, depending on the input of

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aliphatic and aromatic amino acid residues. In protein studies, aromatic hydrophobicity, measured by

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fluorescence, is a universally accepted biomarker used to ascertain the surface hydrophobicity of

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proteins. Hence, in the current study, the surface hydrophobicity of the king prawn NAM solution was

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determined by using ANS as the fluorescent probe. As shown in Fig. 5a, SoANS of NAM increased

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from 175.79 ± 0.4 to 273.07 ± 3.99 in the first 3 min of treatment. Between 4 and 5 min, SoANS values

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declined to 262.7207 ± 4.73 and 200.25 ± 2.16, respectively. In general, the surface hydrophobicity of

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all the treated samples was significantly higher than the control (P < 0.05). A basic justification for these

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outcomes was that structural and conformational changes in NAM during plasma exposure caused the

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hydrophobic groups to become more exposed and bound with ANS. It may also be posited that

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hydrophilic groups (protein carbonyl groups) in combination with amino acid residues were liberated to

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the surface alongside, which justified the slight increase in solubility in the first 2 min of plasma

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treatment. Perhaps some amounts of hydrophilic aggregates were formed at this point, but thereafter a

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relatively larger number of hydrophobic amino acid residues became exposed, as a result of greater

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inter/intra-molecular hydrophobic interactions, causing decline in solubility.44

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An assortment of intracellular and extracellular oxidants can convert SH groups into disulfide (S-

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S) bonds, formed within a single protein or between two different proteins, as a result of structural



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changes. SH groups are highly reactive functional groups in actomyosin.45 As shown in Fig. 5b, T-SH

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content was observed to decline as plasma treatment time progressed, especially between 2 and 5 min

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although these values were nearly at equilibrium. These observations are consistent with earlier works,

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SH content indicates the unfolding of actomyosin with time and the formation of inter- and/or intra-

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molecular disulfide bonds via SH oxidation or disulfide interchanges. However, it is important to

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mention that the near-equal values obtained in the current study indicates that although free SH contents

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tend to be released upon protein unfolding during plasma treatment, their presence may be also temporal

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as free SH groups are prone to oxidation

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molecular or inter-molecular disulfide bonds. The strong oxidizing agent can transform the thiol groups

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into disulfide bonds. Besides, reactive free radicals such as OH- , H2O

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aqueous medium to yield H2O2. The latter can oxidize liable free-SH groups to form S-S bonds, leading

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to the formation of disulphide (S-S) cross-links or even the production of sulfinic and sulfonic acids.47

where the concentration of SH groups decreased with prolonged treatment time. The decrease in T-

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i.e., they may quickly re-associate to form both intra-

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and H+ alike can react in

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Changes in intrinsic fluorescence

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Tryptophan/tyrosine (Trp/Tyr) fluorescence detection is broadly used to monitor changes in the

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tertiary structure of proteins since nonpolar amino acid residues are very sensitive to the polarity of

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proteins or their micro-environment. Several interactions including hydrophobic, electrostatic, van der

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Waals, and hydrogen bonding are involved during the formation of tertiary structure. However, among

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them, hydrophobic interactions are the key driving forces behind protein folding.48 During protein

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unfolding, hydrophobic residues at the interior of the protein structure are relocated to the protein

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surface, away from the polar environment. As shown in Fig. 6, the maximum emission wavelength of

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NAM shifted by ~3.0 nm (red shift) compared with the control after 5 min of plasma treatment. This


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indicates that the microenvironments of the amino acid residues were first altered, i.e., the exposure of

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buried Trps, and some molecular groups were then oxidized upon exposure to active species, resulting in

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the increase in intrinsic fluorescence intensity. However with continuous exposure to plasma species

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especially at 4 and 5 min of plasma treatment, the liberated Trp/Tyr residues/fluorophores and

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hydrophobic portions may have been oxidized by the active species contained in the plasma, resulting in

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the quenching of fluorescence intensity.

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Changes in secondary structures

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The main components of protein secondary structures include α-helix, β-sheet, β-turn and

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random coil. CD is a routine technique used to ascertain the secondary structure of proteins. Each

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constituent possess their distinctive CD spectra. For instance, α-helical proteins show a positive band at

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193 nm and negative bands at both 208 nm and 222 nm, while β-sheet proteins have positive bands at

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195 nm and a negative band at 218 nm.49 These secondary structures including disordered proteins can

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be affected by a variety of factors including the buffer system employed and processing conditions [78].

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The CD spectra of APPJ-treated NAMs as a function of treatment time (0, 1, 2, 3, 4 and 5 min) are

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presented in Fig. 7, indicating that untreated actomyosin had two negative bands/minima at θ209 and θ222.

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This strongly indicates the existence of mainly supercoiled α-helical structures in actomyosin recovered

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from Litopenaeus vannamei. Alpha-helix is known to be the main pattern or secondary structures in

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myosin rod and is held together by electrostatic interactions and hydrogen bonds. The CD spectra of

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NAMs exposed to argon plasma for up to 3 min were nearly comparable to control, suggesting no

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considerable changes occurred in secondary structures. However, when plasma treatment was applied

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beyond 3 min, noticeable change was observed, indicating that continuous exposure led to significant

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changes in secondary structures. By calculation using CDNN secondary structure software (Fig. 7), after



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exposure to APPJ, the proportion of different secondary structures of NAM was not significant, although

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the α-helix structure was slightly reduced after treatment for 5 min and a slight increase in other

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structures such as β-sheets and turns was noticed (Fig. 7). The current results confirm that the plasma

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density in argon gas produced during short treatment times was not sufficient to induce significant

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changes in NAM secondary structures, in particular myosin rod. However, under longer treatment

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durations, use of other gases such as air, or application of different plasma diameters, different results

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could be obtained.

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In conclusion, most seafood products are mainly composed of proteins, therefore are considered

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to be highly suitable as protein resource materials and can be used as functional ingredients in fish

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sausages and surimi‐based products. Shorter APPJ-treatment duration can positively affect the

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functional performance of NAM in such food systems. Though, it is possible that on prolonged

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exposure, higher protein oxidation and formation of hydrophobic interactions may occur. The

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information derived from this study is significant, as it provides better understanding of the fundamental

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interactions that occur which can aid the design of plasma systems with appropriate conditions that will

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achieve maximum efficiency during seafood processing. A combination of several factors including the

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plasma source, gas type, applied voltage, and substrate state ought to be considered, as this may

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influence the efficacy of CP in a process. Therefore under optimal conditions, CP can serve as a new

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tool for modification of protein properties, leading to subsequent development of new products for the

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food industry.

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Acknowledgements

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The authors are grateful to the National Key R&D Program of China (2017YFD0400404) for its

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support. This research was also supported by the Natural Science Foundation of Guangdong Province

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(2017A030310558), the S&T Project of Guangzhou (201804010469), the China Postdoctoral Science 21 ACS Paragon Plus Environment

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Foundation (2018T110873), the Agricultural Development and Rural Work of Guangdong Province

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(2017LM4173), the S&T Project of Guangdong Province (2017B020207002), the Pearl River S&T

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Nova Program of Guangzhou (201610010104), the International and Hong Kong – Macau - Taiwan

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Collaborative Innovation Platform of Guangdong Province on Intelligent Food Quality Control and

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Process Technology & Equipment (2015KGJHZ001), the Guangdong Provincial R & D Centre for the

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Modern Agricultural Industry on Non-destructive Detection and Intensive Processing of Agricultural

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Products, the Common Technical Innovation Team of Guangdong Province on Preservation and

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Logistics of Agricultural Products (2016LM2154) and the Innovation Centre of Guangdong Province for

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Modern Agricultural Science and Technology on Intelligent Sensing and Precision Control of

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Agricultural Product Qualities. In addition, Flora-Glad Chizoba Ekezie is in receipt of financial support

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from China Scholarship Council for her PhD study.

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Satoh, Y.; Nakaya, M.; Ochiai, Y.; Watabe, S. Characterization of fast skeletal myosin from white croaker in comparison with that from walleye pollack. Fisheries Sci. 2006, 72,646-655.



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637

List of Figures

638

Fig. 1. Experimental set up of the plasma jet system, (b) typical optical emission spectra of Ar/O2

639 640 641

measured close to the nozzle outlet (at 5 mm). Fig. 2. Comparison of (a) pH and (b) turbidity at 350 nm of untreated (at 0 min) and plasma treated NAM solutions at different time intervals.

642

Fig. 3. Effects of APPJ treatment durations on (a) solubility and foaming properties, and (b)

643

emulsifying characteristics of NAM proteins. Values are the mean of n = 3 ± the standard

644

deviation. a–d Different letters indicate significant differences (P < 0.05).

645

Fig. 4. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profiles of NAM

646

proteins from Litopenaeus vannamei subjected to APPJ treatment. (a) without DTT and (B)

647

with DTT. Lane 1: marker; lanes 2–6: samples treated for 0, 1, 2, 3, 4 and 5 min,

648

respectively. MHC = myosin heavy chain

649

Fig. 5. Effects of APPJ treatment durations on (a) surface hydrophobicity and (b) total sulfhydryls

650

characteristics of NAM proteins. Values are the mean of n = 3 ± the standard deviation.

651

Different letters indicate significant differences (p < 0.05).

652 653 654 655

Fig. 6. Changes in fluorescence spectra of NAM extracted from muscle of prawn.

a–d

a–d

Different

letters indicate significant differences (p < 0.05). Fig. 7. Changes in secondary structure of NAM subjected to APPJ treatment as measured by far-UV CD-spectroscopy.


Page 31 of 37


Ar O (777.1 nm)

Intensity (counts)

2800

O (842.3 nm)

2400 2000 1600 1200 800 400 0 200

400

600

800

1000

1200

Wavelength (nm)

Figure 1. (a) Experimental set up of the plasma jet system, (b) typical optical emission spectra of Ar/O2 measured close to the nozzle outlet (at 5 mm).



Page 32 of 37

(a)

(b) 0.5

Turbidity A350 nm

7.1

pH

7.0

6.9

0.4

0.3

6.8 0.2 6.7 0

1

2

3

4

5

Treatment time (min)

0

1

2

3

4

5


Figure 2. Comparison of (a) pH and (b) turbidity at 350 nm of untreated (at 0 min) and plasma treated NAM solutions at different time intervals.


Page 33 of 37


Solubility (%) Foaming capacity (%)

Physicochemical property (%)

100

a

a

a

a

a

b

b

60

b

c c

40

a

70

b a

80

EAI (m2/g) ESI (min)

(b)

Emuslifying propeties

(a)

60 50 40 30

a

20 20 0

c

0 1

2

3


4

5

b

d

10

0

b

bc

c

a

a

0

1 2 3 Treatment time (min)

d

4

d

5

Figure 3. Effects of APPJ treatment durations on (a) solubility and foaming properties, and (b) emulsifying characteristics of NAM proteins. Values are the mean of n = 3 ± the standard deviation. a–d Different letters indicate significant differences (P < 0.05).



Page 34 of 37

Figure 4. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profiles of NAM proteins from Litopenaeus vannamei subjected to APPJ treatment. (a) without DTT and (B) with DTT. Lane 1: marker; lanes 2–6: samples treated for 0, 1, 2, 3, 4 and 5 min, respectively. MHC = myosin heavy chain


Page 35 of 37


(a)

300 b

So-ANS

250

a

b

c d

200

e

150 100 50 0

0

1

2

3

4

5


(b)

Total SH content (mol/g protein)

17 a

a

16 b

bc bc

c

15

14

0

1

2 3 Treatment time (min)

4

5

Figure 5. Effects of APPJ treatment durations on (a) surface hydrophobicity and (b) total sulfhydryls characteristics of NAM proteins. Values are the mean of n = 3 ± the standard deviation. a–d Different letters indicate significant differences (p < 0.05).



max value (nm), intensity

Control 1 min 2 min 3 min 4 min 5 min

Intensity

800

600

a

333.00a 333.00a 333.00b 333.00 b 335.66b 335.67

Page 36 of 37

bc

737.30 bc 742.30 c 760.01 a 805.23 b 722.47a 693.70

400

200

0 300

325

350

375

400

Wavelength (nm)

Figure 6. Changes in fluorescence spectra of NAM extracted from muscle of prawn.

a–d Different

letters indicate significant differences (p < 0.05).


Page 37 of 37


Figure 7. Changes in secondary structure of NAM subjected to APPJ treatment as measured by farUV CD-spectroscopy.


Effects of Mild Oxidative and Structural Modifications Induced by Argon

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