Effect of pulsed electric field on calpain activity and proteolysis of venison

Bhat, Zuhaib F.; Morton, James D.; Mason, Susan L.; Mungure, Tanyaradzwa E.; Jayawardena, S. Reshan

doi:10.1016/j.ifset.2018.11.006

Cited by 33 publications

(9 citation statements)

References 37 publications

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“…For sensory analysis, treatment was considered as the main effect and panelists as random variable. The effect of storage time and treatments were analyzed using Duncan's multiple range tests at 0.05 level of significance (Bhat et al 2018).…”

Section: Discussionmentioning

confidence: 99%

Rubia cordifoliabased novel edible film for improved lipid oxidative and microbial stability of meat products

Sharma

Kumar

et al. 2021

J. Food Process. Preserv.

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Rubia cordifolia, commonly known as Indian Madder, is a highly valuable and well-known medicinal plant that belongs to the coffee family, Rubiaceae (Chandrashekar et al., 2018). The root extract of R. cordifolia has a potent antioxidant, antimicrobial, antiviral and free radical scavenging activity owing to a range of bioactive metabolites (Chandrashekar et al., 2018;Martelli & Giacomini, 2018).Recently, R. cordifolia mediated nanoparticles were developed by Ahn et al. (2019) who observed antioxidant and free radical scavenging properties of the developed silver nanoparticles. However, no study has explored the potential of R. cordifolia as an active ingredient for edible and biodegradable films for food applications. Being a rich source of polyphenols, flavonoids, and free radical scavengers (Chandrashekar et al., 2018;Martelli & Giacomini, 2018), its use as a bioactive ingredient in food packaging is highly justifiable.

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Section: Discussionmentioning

confidence: 99%

Rubia cordifoliabased novel edible film for improved lipid oxidative and microbial stability of meat products

Sharma

Kumar

et al. 2021

J. Food Process. Preserv.

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“…Additionally, proteins extracted from intact shrimp showed the lowest density compared to other samples, suggesting that the muscle proteins in intact shrimp might be severely dissociated during chilled storage. The density of the 90 and 110 kDa bands reduced noticeably in the muscle at the initial stage of storage, which was considered to be a sign of proteolysis in the MHCs (Bhat et al., 2019; Ramirez‐Suarez et al., 2008). Additionally, the intact shrimp samples also showed a considerable decrease in the intensity of the protein bands compared to the beheaded shrimp samples.…”

Section: Resultsmentioning

confidence: 99%

Investigation of the activity of cathepsin B in red shrimp (Solenocera crassicornis) and its relation to the quality of muscle proteins during chilled and frozen storage

Zhou

et al. 2022

Journal of Food Science

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Cathepsin B is a cysteine protease that has important effects on the quality of muscle products. In this study, the changes of cathepsin B activity and its relation to muscle proteins were investigated in intact and beheaded shrimp during chilled and frozen storage. The obtained results indicated that the water holding capacity (WHC), shear force, hardness, and myofibrillar protein (MP) content all significantly decreased in both the intact and beheaded shrimp samples with increasing storage period (p < 0.05). Specifically, beheading shrimp exhibited much more stable characteristics than intact shrimp samples during both chilled and frozen storage. The enzyme activity results suggested that cold temperature and storage induced the release of cathepsin B from the lysosomes to the mitochondria, sarcoplasm, and myofibrils in the muscle tissues. Furthermore, SDS‐PAGE and transmission electron microscopy (TEM) analysis revealed that beheading the shrimp greatly inhibited the dissociation of shrimp muscle proteins during storage. The current findings suggest that cathepsin B located in the head of shrimp was likely transferred to the muscle through the first abdominal segment during storage, accelerating the dissociation of the muscle proteins. Therefore, beheading the shrimp was conducive to prolonging the shelf‐life of stored shrimp products.

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“…Bukhari, et al., 2008; Pathak, Bhat, et al., 2008). Food processing fulfils some industrial and marketing needs such as improving storage quality or shelf‐life (Ahmed et al., 2014; Bhat, Kumar, P. Kumar, et al., 2015, 2013; Bukhari et al., 2014‐11; Jamwal et al., 2015; Kaur et al., 2015; Kumar, Bhat, et al., 2012; Kumar, Kumar, et al., 2012; Singh, Kumar, Bhat, Kumar, & Kumar, 2015; Zargar et al., 2017, 2016), production of functional food products (Bhat, Kumar, & H.F. Bhat, 2015, Bhat, Kumar, & H. Bhat, 2015; Bhat & Pathak, 2009; Bhat & Pathak, 2012; Bhat, Pathak, Bukhari, & Ahmed, 2010; Bhat, Pathak, Bukhari, & Ahmed, Bhat, 2010; Bhat, Morton, S. Mason, A. E. B. Bekhit, & Bhat, 2019, 2011; Kumar et al., 2015, 2016; Kumar, Bhat, et al., 2013; Kumar, Kumar, et al., 2013; Kumar et al., 2011, 2014; Pathak et al., 2009; Bhat, Morton, Zhang, et al, 2020; Singh, Kumar, Bhat, & Kumar, 2015) and inducing special effects using novel technologies such as pulsed electric field (PEF; Bhat et al., 2018b; Bhat, Morton, Mason, Mungure, et al., 2018; Bhat et al., 2019a, 2019b; Singh et al., 2012). Before being ready in a final consumable form, food proteins therefore undergo several manufacturing processes, both thermal and nonthermal.…”

Section: Food Processing and Its Impact On Functionality Structure An...mentioning

confidence: 99%

Effect of processing technologies on the digestibility of egg proteins

Morton

Bekhit

Kumar

et al. 2021

Comp Rev Food Sci Food Safe

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Egg and egg products are a rich source of highly bioavailable animal proteins.Several processing technologies can affect the structural and functional properties of these proteins differently and can influence their fate inside the gastrointestinal tract. The present review examines some of the processing technologies for improving egg protein digestibility and discusses how different processing conditions affect the digestibility of egg proteins under gastrointestinal digestion environments. To provide up-to-date information, most of the studies included in this review have been published in the last 5 years on different aspects of egg protein digestibility. Digestibility of egg proteins can be improved by employing some processing technologies that are able to improve the susceptibility of egg proteins to gastrointestinal proteases. Processing technologies, such as pulsed electric field, high-pressure, and ultrasound, can induce conformational and microstructural changes that lead to unfolding of the polypeptides and expose active sites for further interactions. These changes can enhance the accessibility of digestive proteases to cleavage sites. Some of these technologies may inactivate some egg proteins that are enzyme inhibitors, such as trypsin inhibitors. The underlying mechanisms of how different technologies mediate the egg protein digestibility have been discussed in detail. The proteolysis patterns and digestibility of the processed egg proteins are not always predictable and depends on the processing conditions. Empirical input is required to tailor the optimization of processing conditions for favorable effects on protein digestibility.

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Effect of pulsed electric field on calpain activity and proteolysis of venison

Cited by 33 publications

References 37 publications

Rubia cordifoliabased novel edible film for improved lipid oxidative and microbial stability of meat products

Rubia cordifoliabased novel edible film for improved lipid oxidative and microbial stability of meat products

Investigation of the activity of cathepsin B in red shrimp (Solenocera crassicornis) and its relation to the quality of muscle proteins during chilled and frozen storage

Effect of processing technologies on the digestibility of egg proteins

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