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Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes.
International Journal of Food Microbiology ( IF 5.4 ) Pub Date : 2020-08-28 , DOI: 10.1016/j.ijfoodmicro.2020.108851
Saša Vatić 1 , Nemanja Mirković 2 , Jelica R Milošević 3 , Branko Jovčić 4 , Natalija Đ Polović 3
Affiliation  

Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of `foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocytogenes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.



中文翻译:

木瓜蛋白酶和无花果乳胶酶制剂中广泛的底物特异性可改善单核细胞增生李斯特菌的计数。

蛋白水解酶的许多应用包括用于列举食源性致病细菌的发酵肉制品的解离。由于高浓度的酶会影响释放的细菌,因此放弃使用胰蛋白酶来解决这个问题。作为建议的替代品,木瓜蛋白酶和具有较高木瓜蛋白酶样酶含量的无花果胶乳制剂有潜力用于细菌计数。两种源自木瓜和无花果的酶制剂均具有更广泛的底物特异性,包括明胶分解活性,尤其是在丝状蛋白的情况下尤为突出,并且通过用特定抑制剂对二维酶谱进行分析,归因于半胱氨酸蛋白酶丝状蛋白和丝氨酸蛋白酶。对天然胶原蛋白的活性,木瓜蛋白酶较弱,无花果胶乳的广泛应用已通过红外光谱对消化的胶原蛋白进行结构分析得到了证明。对它们在发酵肉产品中解离的潜力的进一步探索表明,木瓜蛋白酶和无花果胶乳酶在存在洗涤剂Tween 20和Triton X-100的情况下都是稳定的,并且可以有效地计数李斯特菌。在操作条件下的明胶分解活性以及至少部分的胶原分解活性和稳定性使得木瓜和无花果乳胶蛋白酶以比以前使用的酶低得多的浓度用于该应用。作为具有不同特性的蛋白水解酶的混合物,无花果胶乳制备物在单核细胞增生李斯特菌释放方面显示出比木瓜蛋白酶更高的效率,即使在存在更强的非离子洗涤剂Triton X-100的情况下也可以保持这种效果。

更新日期:2020-09-08
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