Effect of high pressure processing on heat-induced gelling capacity of blue crab (Callinectes sapidus) meat

Journal Pre-proof Effect of high pressure processing on heat-induced gelling capacity of blue crab (Callinectes sapidus) meat

M.A. Martínez, G. Velazquez, José Alberto Ramírez-de León, A.J. Borderías, H.M. Moreno PII:

S1466-8564(19)30612-5

DOI:

https://doi.org/10.1016/j.ifset.2019.102253

Reference:

INNFOO 102253

To appear in:

Innovative Food Science and Emerging Technologies

Received date:

31 May 2019

Revised date:

18 September 2019

Accepted date:

7 November 2019

Please cite this article as: M.A. Martínez, G. Velazquez, J.A.R.-d. León, et al., Effect of high pressure processing on heat-induced gelling capacity of blue crab (Callinectes sapidus) meat, Innovative Food Science and Emerging Technologies(2019), https://doi.org/10.1016/j.ifset.2019.102253

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Journal Pre-proof Effect of high pressure processing on heat-induced gelling capacity of blue crab (Callinectes sapidus) meat M. A. Martínez 1, G. Velazquez 1, José Alberto Ramírez-de León 2, A.J. Borderías 3

, H.M. Moreno 3,4*.

1

National Polytechnic Institute. CICATA Querétaro Unit. Cerro Blanco 141, Colinas

del Cimatario, 76090. Santiago de Querétaro, México General Direction of Technological Innovation, Autonomous University of

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2

Tamaulipas. Building Center of Excellence, University Center. CP 87040, Ciudad

Institute of Food Science Technology and Nutrition (ICTAN-CSIC), José Antonio

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3

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Victoria, Tamaulipas, México.

4

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Nováis 10, 28040 Madrid, Spain.

Veterinary Faculty. Department Section of Food Technology. Avda. Puerta de

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Hierro, s/n. 28040 Madrid. Spain.

*Corresponding author: Helena M. Moreno

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[email protected]

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Tel. +34 915492300 ext. 231438; Fax: +34 915493687

Abstract There has been increasing use of High pressure processing (HPP) in the fishery industry since this technology facilitates shellfish shucking. Nevertheless, there is limited information about the effect of HPP on protein functional properties of some shellfish. The aim of this study was to evaluate the effect of 100, 300 and 600 MPa/5 min on the gelling capacity of heat-induced (40°C/30 min + 90°C/ 20 min) 1

Journal Pre-proof blue crab (Callinectes sapidus) meat. HPP treatment resulted in crab meat gels with a lighter and reddish colour as compared to the control. HPP at 600 MPa induced the formation of high molecular aggregates from the denaturationaggregation of myosin heavy chain. Pressurization at 100 MPa promoted the shift of α-helix structures to β-sheet and β-turn as compared with the other pressure levels. TPA values were higher in gels made at 100 MPa than at 300 or 600 MPa.

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Low pressure levels, then, increased the heat-induced gelling capacity of crab

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meat, improving the texture through modification of its protein structure.

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Keywords: High pressure processing; blue crab; functional protein; gelling

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Industrial relevance.

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High pressure processing (HPP) technology has been successfully applied to several seafood products, both for processing and storage. However, in the case of

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blue crab meat it is important to study the effect of HPP on protein functional properties such as gelling capacity in order to optimize processing parameters for the preparation of high-quality restructured products. This paper reports the development of a HPP process (100, 300 and 600 MPa/ 5 min 40°C/30 min + 90°C/ 20 min) prior to thermal gelling for the preparation of crab meat gels. The application of 600 MPa produced considerable protein aggregation of gels, whereas with pressures below 300 MPa protein functionality can be modified to produce crab meat gels with adequate brightness, TPA values and a fresh, high2

Journal Pre-proof quality appearance. These results could provide a basis for further pressurization applications in the crab industry to create new seafood product analogues based on this kind of crab meat.

1. Introduction

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Recent years have seen an increase in the industrial applications of high pressure

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processing (HPP), and this technology is becoming more economically viable,

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promoting novel applications in the development, processing and storage of seafood products (Torres & Velázquez, 2005). The effect of this non-thermal

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technology on the inactivation of spoilage and pathogenic microorganisms is well

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established; as such, HPP improves safety and prolongs the shelf life of food

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products (Murchie et al., 2005). The application of HPP to food products has minimal effects on nutritional and organoleptic properties (Velazquez, Gandhi &

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Torres, 2002). There are several studies that propose the use of HPP in shellfish

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processing for the promotion of shucking, so as to facilitate extraction of the meat (Cruz-Romero, Kelly, & Kerry, 2007; Martínez, et al., 2017; Murchie et al., 2005). HPP can be used to develop new seafood products thanks to the effect on the functional properties of some ingredients such as proteins (Cao et al., 2012). In the case of myofibrillar proteins, certain pressure levels promote solubilization and unfolding of the protein structure, resulting in physicochemical changes or modifications of gelling properties promoted by water-protein or protein-protein interactions (Wang et al., 2008; Cando et al., 2015). For that reason, the gelling

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Journal Pre-proof capacity of myofibrillar proteins after HPP has been evaluated in several fish species such as blue whiting (Montero et al., 1997), bluefish (Ashie & Simpson, 1996), tilapia (Hwang, Lai, & Hsu, 2007), hake (Cando, et al., 2014), threadfin bream (Ma et al., 2015) and meagre (Ribiero et al., 2018); and it has been concluded that the fish species and the gelling conditions may induce differences in the physicochemical properties of the resulting gels.

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There has been little research into processing conditions for the preparation of

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heat-induced gels with prior application of HPP as a way to reinforce or improve

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mechanical and textural properties of the resulting gels. Cando et al (2014)

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reported that applying HPP (150-500 MPa) to myofibrils before heating improved

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the conformational stability of the protein network. Moreover, Uresti et al. (2004) concluded that pressure treatments between 400 and 600 MPa applied to

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arrowtooth flounder paste followed by heat-induced gelling (90°C) resulted in a better protein structure and greater hardness and gel strength than non-

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pressurized gels. Recently, Truong et al. (2017) studied the effect of HPP on the

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gelling capacity of minced barramundi muscle, reporting that pressure levels of 300-500 MPA (10 min at 4°C) prior to cooking (90°C for 30 min) enhanced the mechanical and functional properties of the gels as compared to heat-induced gels. Therefore, using HPP on seafood proteins before thermal gelling could help improve the technological or functional properties of fish gels. This offers fresh opportunities for the development of new restructured seafood products using HPP.

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Journal Pre-proof In the USA and Mexico blue crab (Callinectes sapidus) is a major fishery activity involving large communities, and it is considered a high-value seafood product (Paolisso, 2007). In the Mediterranean and the Black Sea this species is considered an invasive crustacean (Mancinelli et al., 2017). In both cases, the crab industry offers an opportunity to innovate and to develop new processing techniques as well as new seafood products based on crab meat. The traditional

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process for extraction of the crab meat requires the use of thermal treatment, many

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hours of processing, and in some regions the crab meat is hand-picked. The main

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purpose of the heat treatment (boiling or steaming) is to facilitate the extraction of

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the meat from the shell and so achieve the distinctive flavour compounds of cooked meat and eliminate pathogenic microorganisms (Ward et al., 1990). Heat

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treatment results in low yield extraction (10-15%) of the crab meat. However, HPP

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has been reported to maximize the shucking process of different shellfishes, including oyster (He et al.,2002; Cruz-Romero et al., 2007), bay scallop (Yi et al.,

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2013), shrimp (Yang et al., 2010; Kaur et al., 2016), lobster (Campus, 2010) and

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crabs (Martínez et al., 2017).

The aim of this study was therefore to determine the effect of HPP at 100, 300 and 600 during 5 min on the gelling capacity of heat-induced (40°C/30 min + 90°C/ 20 min) blue crab (Callinectes sapidus) meat for making crab meat gels .

2. Material and methods 2.1. Raw material and sample preparation.

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Journal Pre-proof Live blue crab (Callinectes sapidus) were purchased at a local market (Madrid, Spain) and covered with ice in a plastic container. In the lab, the crabs remained in the plastic container and more ice with water was added to reduce metabolism as described by Martínez et al. (2017). In the lab, the whole crabs were kept in a mixture of water/ice during 30 min before the application of the different treatments. The crab were then put into plastic bags before being subjected to the different

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treatments.

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Ten specimens for each treatment were used. The high-pressure processing

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conditions were selected based on reported parameters for other seafood products

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(Cruz-Romero et al., 2004; Yi et al., 2013) and for blue crab (Martinez et al., 2017).

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HPP consisted of 100, 3000 and 600 MPa/ 10°C/ 5 min (Stansted Fluid Power LTD, FPG 7100, Stansted, UK). Then, samples were placed in refrigerated storage

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(4°C). To obtain cooked crab meat, the whole crab was cooked in boiling water

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(90°C/ 20 min) then kept at 4°C for 12 hours.

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After both treatments, the crab meat was hand-picked and the meat divided into jumbo lump, backfin, special and claw. To make the gels, raw, cooked and pressurized crab meat was homogenized for 1min in different batches (Table 1) with 0.5% NaCl to solubilize proteins. Then 0.5% of microbial transglutaminase (MTGase) and 3% albumin were added and homogenized for 1 min each below 10°C. Homogenized crab meat mixture was stuffed into stainless-steel tubes. Afterwards, the samples were immersed in a water bath at 40°C for 30 min followed by immersion in a water bath at 90°C for 20 min, then cooled in ice water for 30 min. The crab meat gels were removed from 6

Journal Pre-proof the stainless-steel tubes and stored at 4°C until analysed. Samples were coded as shown in Table 1.

2.2. Colour attributes Spectral reflectance of crab meat gels was determined using a HunterLab Mini

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Scan MS/S-4000S (Hunter Associated Laboratory Inc., Reston VA), calibrated

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against black and white tiles. The CIE L, a and b system was used to determine

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the colour parameters values. In addition, hue angle [tan-1 (b/a)], chroma [√(a2 + b2)] and whiteness [L-(3 b)] were calculated from L, a and b results. The

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2.3. SDS-PAGE

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measurements were carried out in six replicates.

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The analysis of SDS-polyacrylamide gel electrophoresis (SDS-PAGE) (Laemmli,

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1970) was carried out using a Mini-Protean® TGX Stain FreeTM Gels with 7.5% acrylamide. A sample of crab meat gel (0.1 g) was dissolved in 2 mL SDS-UM solution (2% SDS, 8 M Urea, 5% 2-mercaptoethanol, 20 mM Tris HCl (pH 7.5)). The sample was dissolved by constant shaking overnight at room temperature. Protein separation conditions were 15 mA/gel and 250 V. The Precision Plus Protein All Blue Standards (Bio-Rad Laboratories, Inc., Richmond, CA, USA) was used for molecular reference weight. Staining was done with Coomassie Brilliant Blue R-250. The gels were evaluated on a Gel Doc XR Scanner (Bio-Rad Laboratories, Inc., Richmond, CA, USA). 7

Journal Pre-proof

2.4. Fourier transform infrared spectroscopy (FTIR) FTIR spectra of crab meat gel samples were recorded as described by Cando et al (2014) using an infrared spectrometer (Spectrum 400. Perkin-Elmer Inc., Waltham, MA, USA) equipped with an ATR prism crystal accessory. One-milligram (wet

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basis) of each gel was used to perform the analysis, at room temperature. FTIR

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spectra were obtained from 4000 to 650 cm−1 with 16 scans at 4cm−1 resolution. Background interference was eliminated using the Spectrum software version 6.3.2

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(Perkin Elmer Inc.). Also, Fourier self-deconvolution (FSD) in the amide I region

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(1700–1600 cm−1) was applied to increase the resolution spectra. All experiments

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were performed in triplicate. The changes in secondary protein structures were calculated assuming that any protein can be considered as a linear sum of a few

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fundamental secondary structure elements and the percentage of each element is

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only related to the spectral intensity (Kong & Yu, 2007).

2.5. Texture profile analysis Crab meat gel samples were subjected to texture profile analysis (TPA) as described by Bourne, Moyer & Hand (1966). Gels were compressed to 50% of initial height (50 N load cell connected to the crosshead on a TA-XT plus Texture analyzer -Texture technologies corp., Scarsdale, NY, USA) at a compression rate of 50 mm min-1 and a 50-mm-diameter aluminium probe (P/50). TPA parameters calculated for each treatment were hardness (peak force during the first 8

Journal Pre-proof compression cycle -N-), cohesiveness (area under second compression cycle / area under first compression cycle-dimensionless-) and springiness (distance sample recovers after the first compression -mm-). The measurements were carried out in quadruplicate.

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2.6. Statistical analysis

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Data were analysed using STATISTICA 7.0 software (StatSoft Inc). A one-way

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analysis of variance was applied. Differences among mean values were evaluated

3. Results and discussion

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by the Turkey test using a 95% confidence interval.

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3.1. Colour parameters of blue crab meat gels

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The changes in colour parameters of crab meat gels are summarized in table 2. L*

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values of all samples ranged from 66.30 to 76.96; for a* and b* the values ranged from -1.49 to 2.90 and from 8.16 to 13.21 respectively. Whiteness varied from 65.19 to 75.51. The application of HPP before heat treatment (T3, T4, and T5) in gel the preparation resulted in a statistically significant decrease (P≤ 0.05) in L* values compared with raw crab meat (T1). L* values were lowest in gel samples from cooked crab meat (T2). In the literature, high levels of lightness in a restructured product have been associated with protein aggregation through the increase of

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Journal Pre-proof cross-links promoting a compact structure and a greater area of light reflectance (Uresti, et al., 2004). In T2 gels, the samples were subjected to a two-step heating process, so the gel structure seemed not to be able to form a very compact structure capable of reflecting the light. There was a significant increase (P≤ 0.05) of a* and b* values in all the HPP samples compared to the T1 gels. These results could be related to

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carotenoprotein (a blue-green pigment) and hemocyanin (a blue blood protein)

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which are contained in blue crabs among other crustaceans (Verhaeghe et al.,

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2018). Due to the post-HPP heat treatment, the carotenoprotein in the crab meat

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may denature, releasing astaxanthin in free form (Cheecharoen et al., 2011). As a

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result, a* values increased in gels T3, T4 and T5. In gels T1 and T2, the effect of heat could be explained by a partial dissociation of the protein-carotenoid, causing

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the formation of a green colour and thus reducing a* values.

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All crab meat gels presented high positive b* values, although in gels subjected to

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HPP, b* was significantly higher (P≤ 0.05). This may be associated with the presence of hemocyanin, which remained oxygenated (Verhaeghe et al., 2018), and due to the high pressure could have induced the dissociation products of hemocyanin, primarily dimers that bind oxygen (Bonafe, Araujo & Silva, 1944).

3.2. SDS-PAGE profile of crab meat gels Protein patterns of crab meat gels made from the extracted meat of raw, heattreated and HPP blue crab were very similar (Fig. 1) reflecting the characteristic 10

Journal Pre-proof myofibrillar protein profile (Benjakul & Sutthipan, 2009). All the samples exhibited bands at ~200 kDa corresponding to myosin heavy chain, 116-98 kDa corresponding to paramyosin and glycogen phosphorylase and below 47 kDa, bands related to actin and tropomyosin, as well as small proteins or degraded proteins of small molecular weight (Lin & Park, 1996). All samples also showed a clear band at the top of the resolving gel. This band has

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been related to protein aggregation during thermal gelation, forming high molecular

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weight aggregates which do not enter the electrophoresis gel (Liu, Xiong &

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Butterfield, 2000). Accordingly, higher protein aggregates were observed in T1 and

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T2 gels made with raw crab meat or with cooked crab meat, suggesting that HPP

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could have stabilized T3, T4 and T5 gels by establishing covalent and noncovalent interactions (Uresti et al., 2004; Martínez et al., 2017) different from those

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formed in the gels made from raw and cooked crab meat (T1 and T2). Thus, a different protein matrix was formed in either group of gels. This Means that the

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denaturing solution used to stabilize the protein matrix was not able to solubilize

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the intensely aggregated crab meat proteins as a result of the heating and HPP (Liu, Xiong & Butterfield, 2000).

3.3. Secondary structures of crab meat gels A quantitative estimation was made from the Fourier deconvoluted spectra of the amide l band (1700-1600 cm-1) to determine the contribution of secondary structures in crab meat gels. The amide I band is the most commonly used for

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Journal Pre-proof infrared spectroscopic analysis of secondary structures of proteins since it is the most sensitive band to changes in the myofibrillar proteins (Krimm & Bandekar, 1986; Kong & Yu, 2007). In the present study, twelve bands were located and identified on the Amide I region as reported by Cando et al. (2014) and Martínez et al. (2017). The α-helix structures were assigned the 1652 cm-1 band, β-sheet fractions bands numbers 1696,1675,1642, 1638, 1633, 1627 and 1624 cm-1; β-turn

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the 1687 and 1667 cm-1 bands; random structures were identified at bands 1656

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and 1648 cm-1.

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The secondary protein structures of all crab meat gel samples are shown in Table

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3. Although some significant differences were noted in the secondary structures

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when comparing the samples, all gels were heated before analysis, so the effect of the heat treatment is the most evident. Thermal gelation led to a shift from α-helix

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to β-sheet, presumably due to the unfolding of protein structures that were denatured-aggregated at high temperature (90°C) (Cando et al., 2016). Moreover,

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HPP induced protein conformational changes through destabilization of hydrogen

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bonds; this would be reflected in a loss of α-helix structures and the appearance of reactive groups that promote inter-molecular bonding, leading to protein denaturation, aggregation or gelation (Zhou et al.,2014; Zhang et al., 2017). Martínez et al. (2017) reported the use of HPP on native myofibrillar protein of blue crab and concluded that with high pressure the α-helix structures diminished and there was an increase in β-sheet and β-turn structures. However, these shifts of structure percentages are not as evident in these samples as in those reported by

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Journal Pre-proof Martínez et al. (2017) because of the heat treatment-HPP overlap effect (Cando et al., 2014).

3.4. Texture Profile Analysis of blue crab meat gels The TPA parameter data are presented in Fig 2. Hardness of blue crab gels

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ranged from 9.66 to 27.07 N (Fig. 2-A), springiness from 0.71 to 0.83 mm (Fig. 2-B)

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and cohesiveness from 0.37 to 0.79 (Fig. 2-C).

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Hardness (27.63 N) was higher in gels treated with 100 MPa (T3) than in other

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treatments (P≤ 0.05). There was a statistical decrease in hardness of samples cooked (T2) and treated with 300 (T4) and 600 (T5) MPa as compared to untreated

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samples (T1); the decline in hardness was 52.17, 13.72 and 51.77 % respectively.

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Crab meat gels pressurized at between 100 and 300 MPa had the highest springiness values. After the first compression, these gels almost recovered their

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initial height, which is typical of viscoelastic materials. Springiness did not differ

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significantly (P≤ 0.05) in gels from T2 and T5 samples, meaning that HPP did not affect this parameter. Cohesiveness exhibited the same trend as springiness. Cohesiveness of gels treated with low pressure levels (T3 and T4) was greater (P≤ 0.05) than that of gels treated with 600 MPa (T5). These results suggest that applying high pressure to the whole blue crab resulted in the formation of a protein network that is different from a protein network formed with non-pressurized or heat-treated gels, as noted above in section 3.2. The changes in the protein structure of blue crab meat at pressures lower than 300 MPa could favour the

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Journal Pre-proof formation of a well-structured network during subsequent full denaturation by cooking, promoting the formation of covalent and non-covalent bonds (Uresti, 2004; Hwang, Lai & Hsu, 2007). These changes are associated with the high proportion of β-sheet structures (Table 3) detected in the gel samples from treatment T1 and T2 and the higher hardness values of these crab meat gels. The development of β-sheet structures has a bearing on textural properties, in that

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these structures are closely associated with an ordered protein network.

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Thus, TPA parameters increased in treatment T3 samples. Additionally, the

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application of 600 MPa had a similar effect on the TPA parameters of the crab gels

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to that of the heat treatment of whole blue crab. Both treatments could have

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induced initial, partial depolymerization, unfolding, denaturation and aggregation of blue crab proteins, resulting in inhibition of a well-defined protein network-structure

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after cooking. This could be due to the poor mechanical properties of crab gels

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(such as lower hardness, springiness and cohesiveness)

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Research into the use of HPP on whole crabs and the subsequent development of crab meat gels is still limited. However, other studies have been reported comparing the application of HPP prior to heat treatment in aquatic foods. Ashie & Lanier (1999) reported that the application of high pressure (250 MPa) followed by heating (90°C) in Alaska pollock surimi led to stronger gels than those formed only with cooking. Montero et al. (1997) found that applying low pressure (<300 MPa) followed by heating produced harder sardine gels than those treated only at high pressure. Recently, Truong et al. (2017) reported the application of 300 to 500

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Journal Pre-proof MPa on minced barramundi muscle after cooking, resulting in better mechanical and functional properties of barramundi gels than achieved with heat-induced gels.

4. Conclusions The use of HPP on blue crab for hand-picking of the meat followed by heat-

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induced gelling of the pressurized meat resulted in high-quality gels. With HPP

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crab meat gels were redder (high a* value) and glossier. Pressures above 300

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MPa and heating caused considerable protein aggregation with a high proportion of β-sheet structures and low proportions of α-helix and β-turn. Thus, HPP modified

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protein secondary structures, and 100 MPa was enough to improve the mechanical

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properties of the gels.

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These gels could provide a base for new seafood analogues. However, studies on protein digestibility are required to properly understand the effect of HPP on crab

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meat and crab meat gels.

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Journal Pre-proof Captions Figure 1. SDS-PAGE profile of crab meat gels. Lane 1) Molecular weight; 2) T1; 3) T2; 4) T3; 5) T4; 6) T5. See Table 1 for samples code.

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Figure 2. Effect of HPP treatment on the physico-chemical properties of blue crab gels (Hardness (A), Springiness (B), Cohesiveness (C). All values are mean ± standard deviation of six replicates (n=6). a,b,c . Different letters indicate significant differences (p < 0.05) between the different treatments. See Table 1 for samples code.

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Journal Pre-proof Tables Table 1. Samples code according to HPP treatment on the blue crab and gel processing conditions made from the crab meat Heat-induced treatment

T1

Untreated

40°C / 30 min + 90°C/ 20 min

T2

Cooked crab (90°C / 20 min)

40°C / 30 min + 90°C/ 20 min

T3

100 MPa / 5 min / 10°C

40°C / 30 min + 90°C/ 20 min

T4

300 MPa / 5 min / 10°C

40°C / 30 min + 90°C/ 20 min

T5

600 MPa / 5 min / 10°C

40°C / 30 min + 90°C/ 20 min

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Blue crab treatment

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Samples

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Table 2. HPP treatment effect on color properties of heat-induced crab meat gels Samples L* a* b* Whitness a c c T1 76.96 ± 0.73 -1.49 ± 0.25 8.16 ± 0.50 75.51 ± 0.66 a T2 66.30 ± 0.92 b -0.48 ± 0.14 b 8.67 ± 0.78 c 65.19 ± 0.84 c T3 75.22 ± 0.84 c 2.90 ± 0.15 d 12.71 ± 0.29 b 72.00 ± 0.74 d T4 72.84 ± 0.56 d 2.67 ± 0.11 d 13.21 ± 0.54 b 69.67 ± 0.60 a T5 73.76 ± 1.37 cd 1.11 ± 0.24 a 11.13 ± 0.81 a 71.46 ± 1.26 d

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Data are presented as mean values (n=6) ± standard deviation. a,b,c Different letters indicate significant (p < 0.05) differences between treatments for the elaboration of blue crab meat gels. See Table 1 for samples code.

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Table 3 HPP effects on the secondary structures of proteins determined by Fourier transform infrared (FTIR) spectroscopy self-deconvolution of heat-induce crab meat gels α-helix (%)

β-sheet (%)

β-turn (%)

Random (%)

T1

21.65 ± 0.22

a

44.64 ± 0.74

ab

23.62 ± 0.87

a

10.09 ± 1.54

b

T2

23.82 ± 2.27

b

42.73 ± 1.23

c

22.65 ± 1.34

a

10.79 ± 0.98

ab

T3

21.24 ± 0.96

a

45.25 ± 1.19

b

21.40 ± 2.81

ac

12.11 ± 0.84

ab

T4

22.68 ± 0.16

ab

44.65 ± 1.49

ab

18.61 ± 0.61

b

14.06 ± 0.81

a

T5

24.04 ± 1.09

b

41.93 ± 0.96

c

19.56 ± 0.36

bc

14.47 ± 0.23

a

Data are presented as mean values (n=3) ± standard deviation. a,b,c Different letters indicate significant (p < 0.05) differences between treatments for the elaboration of blue crab meat gels. See Table 1 for samples code. 23

Journal Pre-proof

Highlights High pressure processing modified protein gelling capacity in crab meat

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Application of 600 MPa increased protein aggregation of crab meat gels

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Crab meat gels were improved by pressure levels below 300 MPa

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Figure 1

Figure 2