The mechanistic effect of bromelain and papain on tenderization in jumbo squid (Dosidicus gigas) muscle
Graphical abstract
Introduction
Jumbo squid (Dosidicus gigas) is one of the most important cephalopod species in the world, with 747,010 tons harvested in 2016 (FAO, 2018). In recent years, squid has captured an increasing economic interest in many countries, including China, Japan, Mexico, and Chile, mainly because of the increased land demands due to development and commercialization (Lemus-Mondaca, Zambra, Marín, Pérez-Won, & Tabilo-Munizaga, 2018). Importantly, squid muscle is a good source of nutrition and contains compounds such as protein, unsaturated fatty acids, vitamins A, B, and D, essential amino acids, and other important biomolecules (Torrinha, Gomes, Oliveira, Cruz, Mendes, Delerue-Matos, et al., 2014).
However, the squid muscle has a sticky, tough consistency and is difficult to get to soften, even following storage and heating, which negatively affects consumer acceptance. Squid muscle fibers structurally differ from those of other fish and mammals. They are present in a radial and circular orientation and tightly interposed with connective tissue fibers (Torres-Arreola, Ocaño-Higuera, Ezquerra-Brauer, López-Corona, Rodríguez-Felix, Castro-Longoria, et al., 2017). This particular tissue organization is directly associated with the observed tough muscle texture. Importantly, high content of insoluble myostromin (11%) in squid muscle makes industrial squid products (e.g. shredded squid, read-to-eat squid, dried squid) taste tough and hard, which significantly hinders the edibility of these products by the elderly and infants (Hu et al., 2014). Therefore, it is necessary to find a way to manage and increase values of the squid products.
To improve the textural muscle tissues properties, several approaches, such as exposure to hydrolytic enzymes, ultrasonic waves, electrical stimulation, chemical compounds, high hydrostatic pressure processing, and blade tenderization, have been explored (Bolumar et al., 2013, Vandenberghedescamps et al., 2018, Peña-Gonzalez et al., 2019). These studies have shown that the tenderization processes reduce the degree of sarcomere contraction and affect myofibrillar integrity/degradation and/or connective tissues cleavage to improve muscle tissue tenderness (Morton, Bhat, & Ahmed, 2019). Most of all, the use of exogenous enzymes has been shown to effectively improve muscle tenderness and enhance flavor, as well as increase the nutrient value. Commonly used exogenous proteases, including papain, bromelain, ficin, and actinidin, have been examined in beef (Barekat & Soltanizadeh, 2017), chicken muscle (Wang, Li, Xu, & Zhou, 2013), pork (Sun, Chen, Geng, Luo, Gong, & Jiang, et al., 2017), and lamb tenderization (Han, Morton, Bekhit, & Sedcole, 2009). Among the most promising, bromelain and papain (recognized as Generally Recognized as Safe by United States federal agencies) are plant-derived cysteine proteases and have broad spectrum activity, cleaving a wide variety of bonds, thus degrading myofibrillar and collagenous proteins in muscle. However, one of the major challenges of using these enzymes is countering the effect of overtenderizing, leading to the need for the processor to carefully monitor the process to avoid creating an overly soft texture (Bekhit, Hopkins, Geesink, Bekhit, & Franks, 2014).
While numerous studies investigating the effect of proteases on the textural properties of mammal muscle products have been performed, little is known regarding the actions of bromelain and papain on the squid mantle muscle during the tenderization process. The objective of this study was to explore the effects of bromelain and papain in regard to water holding capacity (WHC), texture, shear force, myofibrillar protein levels, myofibril morphology, and muscle protein degradation during tenderizing in squid mantle.
Section snippets
Samples and chemicals
Frozen giant squid (Dosidicus gigas) were commercially obtained from a local aquatic products market (Donghe Market, Zhoushan, Zhejiang province, China). The samples had an average body length of 20 ± 2 cm and a weight of 400 ± 25 g. The obtained specimen was packaged in ice and transported to the laboratory at Zhejiang Ocean University (Zhoushan, Zhejiang province, China) within 20–30 min. The initial total volatile basic nitrogen (TVBN) was determined to be 4.3–4.8 mg/100 g as previously
Water holding capacity (WHC)
To determine the amount of water retained within the muscle tissue network, which is an important quality indicator, the WHC was calculated. The untreated control squid muscle tissue showed the lowest drip loss, thus the highest WHC (Fig. 1). This indicates that squid muscle tissues have a well-organized structure and stable myofibrillar proteins. In the water-treated samples, the pressing loss increased significantly (P < 0.05) when compared with the control, mainly due to water permeating the
Conclusions
In this study, the effects of bromelain and papain treatments on WHC, texture, myofibrillar stability, microstructural changes, and degradation were examined in the untreated and treated squid mantles. The results demonstrated that both bromelain and papain treatments significantly decrease the WHC, hardness, shear force, myofibrillar protein content, and Ca2+-ATPase activity while increasing the amount of free amino acids and the MFI values, thereby confirming a high proteolytic activity.
CRediT authorship contribution statement
Xu Jun-hui: Methodology, Investigation. Cao Hui-juan: Conceptualization, Writing - original draft. Zhang Bin: Writing - Review & Editing, Funding acquisition. Yao Hui: Data curation.
Declaration of Competing Interest
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Acknowledgments
This study was funded by the National Natural Science Foundation of China (No. 31871871), the Zhejiang Natural Science Foundation of China (Grant No. LY18C200008), and the Key R&D Program of Zhejiang province, China (Grant No. 2019C02075). We thank LetPub (www.letpub.com) for its linguistic assistance during the preparation of this manuscript.
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