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Kiwifruit
Published in Debashis Mandal, Ursula Wermund, Lop Phavaphutanon, Regina Cronje, Temperate Fruits, 2021
The kiwifruit is also known to contain a protein-dissolving enzyme actinidin, belonging to the family, proteases to which papain extracted from papaya belongs. It can be used for tenderization of meat. However, the actinidin reacts with milk protein and results in undesirable products. Hence, the eating of kiwifruit is not advisable with milk or milk products. Rana et al. (2011a) have isolated the protein from kiwifruit which exhibited antifungal activity against Fusarium oxysporum and Rhizoctonia solanii causing several diseases in plants. Numerous edible seeds of kiwifruit containing vitamin E and Ω-3 fatty acids have a potential of a natural blood thinner. A study performed at the University of Oslo in Norway reported that consuming 2–3 kiwifruit daily for 28 days significantly reduced platelet aggregation and blood triglyceride levels, potentially reducing the risk of blood clots.
Efficient three phase partitioning of actinidin from kiwifruit (Actinidia deliciosa) and its characterization
Published in Preparative Biochemistry & Biotechnology, 2023
Bunty Maskey, Dhan Bahadur Karki
The overall profile of TPP-purified actinidin (kiwifruit protease) at 40% ammonium sulfate precipitation, 1.0:0.75 ratio of the CE to tert-butanol, and 6.0 pH is summarized in Table 1. It can be stated that the one-step TPP of kiwifruit crude dialyzed extract at optimum purification parameters resulted highest purification fold and recovery of 3.14 and 142.27%, respectively at the interfacial precipitate. Dhiman et al.[42] purified crude extract of kiwifruit (Actinidia deliciosa) through fractionation using 60% ammonium sulfate saturation and DEAE-anion exchange chromatography, and reported 2.42 purification fold and 22.43% recovery only. Similarly, Lo Piero et al.[43] utilized DEAE-cellulose column chromatography after 50% ammonium sulfate saturation for the purification of actinidin from crude kiwifruit (Actinidia chinensis) extract, and the purity of 2.4 and recovery % of 8.7 were observed. Hence TPP system causes simultaneous enzyme activation, resulting in greater values of both purity and recovery.[44] The reduction of interfering enzymes throughout the pre-dialysis as well as the enzyme activation during ammonium sulfate precipitation might have contributed to increased purification fold, and the synergistic interaction between the concentration of salt and volume of solvent under optimal purification conditions might be the cause of higher activity recovery %.[12] Previous studies on TPP purification of plant proteases by Gul et al.,[29] Gagaoua et al.,[6] Gagaoua et al.,[22] Hafid et al.,[11] Chaiwut et al.,[37] Duman and Kaya,[30] Özer et al.,[36] and Rawdkuen et al.[45] all reported similar results.