首页> 外文期刊>Journal of Agricultural and Food Chemistry >Purification and characterization of an antimicrobial chitinase extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium
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Purification and characterization of an antimicrobial chitinase extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium

机译:虾和蟹壳粉培养基中红曲霉CCRC31499细胞外产生的抗菌几丁质酶的纯化和表征

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摘要

Monascus purpureus CCRC31499 produced an antimicrobial chitinase when it was grown in a medium containing shrimp and crab shell powder (SOSP) of marine wastes. An extracellular antimicrobial chitinase was purified from the culture supernatant to homology. The chitinase had a molecular weight of similar to81000 and a pl of 5.4. The optimal pH, optimum temperature, and pH stability of the chitinase were pH 7, 40 degreesC, and pH 6-8, respectively. The activity of the chitinase was activated by Fe2+ and strongly inhibited by Hg2+. The unique characteristics of the purified chitinase include high molecular weight, nearly neutral optimum pH, protease activity, and antimicrobial activity with bacteria and fungal phytopathogens. This is also the first report of isolation of a chitinase from a Monascus species.
机译:当紫红曲霉CCRC31499在含有海洋废弃物的虾和蟹壳粉(SOSP)的培养基中生长时,会产生抗微生物几丁质酶。从培养物上清液纯化细胞外抗微生物几丁质酶至同源性。几丁质酶的分子量类似于81000,pI为5.4。几丁质酶的最佳pH,最佳温度和pH稳定性分别为7、40℃和6-8。几丁质酶的活性被Fe2 +激活,并被Hg2 +强烈抑制。纯化的几丁质酶的独特特征包括高分子量,接近中性的最佳pH,蛋白酶活性以及对细菌和真菌植物病原菌的抗菌活性。这也是从红曲菌中分离几丁质酶的首次报道。

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