Isolation and characterization of a protease from the Actinidia arguta fruit for improving meat tenderness

Wang, Juan; Liu, Haoming; Wang, Haili; Cui, Mingxun; Jin, Qing; Jin, Tie; Fu-shun, Cui; Cui, Taihua; Cheng-yun, Liang; Kim, Bumsik; Li, Guanhao

doi:10.1007/s10068-016-0171-y

Cited by 7 publications

(2 citation statements)

References 24 publications

(18 reference statements)

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“…Papain, bromelain (Kim & Taub 1991;Xu et al 2020), ficin (Maqsood et al 2018), actinidin (Ha et al 2012;Wang, Liu, et al 2016), and zingibain (Cruz et al 2020;Tsai et al 2012) are common plant-derived exogenous enzymes, and papain is one of the most widely studied plant proteases. Generally, its sulfhydryl endopeptidase activity can cleave most peptide bonds and disintegrate proteins under different pH conditions (Abdel-Naeem & Mohamed 2016;Maqsood et al 2018).…”

Section: Enzymatic Techniquesmentioning

confidence: 99%

Techniques for postmortem tenderisation in meat processing: effectiveness, application and possible mechanisms

Shi

Shahidi

Wang

et al. 2021

Food Prod Process and Nutr

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Developing efficient and promising tenderising techniques for postmortem meat is a heavily researched topic among meat scientists as consumers are willing to pay more for guaranteed tender meat. However, emerging tenderising techniques are not broadly used in the meat industry and, to some degree, are controversial due to lack of theoretical support. Thus, understanding the mechanisms involved in postmortem tenderisation is essential. This article first provides an overview of the relationship of ageing tenderisation and calpain system, as well as proteomics applied to identify protein biomarkers characterizing tenderness. In general, the ageing tenderisation is mediated by multiple biochemical activities, and it can exhibit better palatability and commercial benefit by combining other interventions. The calpain system plays a key role in ageing tenderisation functions by rupturing myofibrils and regulating proteolysis, glycolysis, apoptosis and metabolic modification. Additionally, tenderising techniques from different aspects including exogenous enzymes, chemistry, physics and the combined methods are discussed in depth. Particularly, innovation of home cooking could be recommended to prepare relatively tender meat due to its convenience and ease of operation by consumers. Furthermore, the combined interventions provide better performance in controlled tenderness. Finally, future trends in developing new tenderising techniques, and applied consideration in the meat processing industry are proposed in order to improve meat quality with higher economical value. Graphical abstract

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Section: Enzymatic Techniquesmentioning

confidence: 99%

Techniques for postmortem tenderisation in meat processing: effectiveness, application and possible mechanisms

Shi

Shahidi

Wang

et al. 2021

Food Prod Process and Nutr

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show abstract

“…The cDNA structure and amino acid sequence derived from cDNA structures of cysteine protease from A. arguta have been reported [17], and the crystallographical structure of the enzyme has also been determined [18]. However, little is known about the biochemical and physiological properties of cysteine protease in the fruit juice of A. arguta [19].…”

Section: Introductionmentioning

confidence: 99%

Purification and Biochemical Characterization of Cysteine Protease from Baby Kiwi (Actinidia arguta)

Miyazaki-Katamura¹,

Yoneta-Wada²,

Kozuka³

et al. 2019

TOBIOCJ

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Background: It has recently been reported that the fruit, stems and leaves of Actinidia arguta have various potential health effects including an antioxidant effect, anticancer effect, anti-allergic effect and α-glucosidase inhibitory effect. However, little is known about the biochemical properties of cysteine protease in the fruit juice of A. arguta. Methods: Ion exchange chromatography to purify the cysteine protease from the fruit juice of A. arguta, and some synthetic substrates to determinate the enzyme activity were used. Results: Cysteine protease was purified to homogeneity from A. arguta fruit juice by ion exchange chromatography. The molecular weight of the purified enzyme was calculated to be approximately 25,500 by SDS-PAGE in the presence of β-ME. The enzyme rapidly hydrolyzed the substrate Z-Leu-Arg-MCA and moderately hydrolyzed other substrates including Boc-Val-Leu-Lys-MCA, Z-Val-Val-Arg-MCA and Z-Phe-Arg-MCA. Kinetic parameters for these four substrates were determined. The Km, Vmax, Kcat and Kcat/Km values for Z-Leu-Arg-MCA, the most preferentially cleaved by the enzyme, were 100 μM, 63.8 μmoles/mg/min, 27.26 sec-1 and 0.2726 sec-1μM-1, respectively. Furthermore, the activity of the enzyme was strongly inhibited by inhibitors including antipain, leupeptin, E-64, E-64c, kinin-free-LMW kininogen and cystatin C. Those biochemical data indicated that the enzyme was a cysteine protease. The amino acid sequence of the first 21 residues of cysteine protease purified from Actinidia arguta was Val1-Leu-Pro-Asp-Tyr5-Val-Asp-Trp-Arg-Ser10-Ala-Gly-Ala-Val-Val15-Asp-Ile-Lys-Ser-Qln20-Gly. This sequence showed high homology to the sequences of actinidin from Acinidia deliciosa (95.0%) and actinidin from Actinidia eriantha (90%). These three cysteine proteases were thought to be common allied species. Conclusion: The biochemical properties of the enzyme purified from A. arguta fruit juice were determined. These basic data are expected to contribute to the maintenance and improvement of human health as well as to the promotion of protein digestion and absorption through its proteolytic functions.

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Plant Proteases in Food Processing

Shah

Mir

2018

Reference Series in Phytochemistry

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Isolation and characterization of a protease from the Actinidia arguta fruit for improving meat tenderness

Cited by 7 publications

References 24 publications

Techniques for postmortem tenderisation in meat processing: effectiveness, application and possible mechanisms

Techniques for postmortem tenderisation in meat processing: effectiveness, application and possible mechanisms

Purification and Biochemical Characterization of Cysteine Protease from Baby Kiwi (Actinidia arguta)

Plant Proteases in Food Processing

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