Bernal M A, Calderón A A, Pedreño M A, Ferrer M A, Merino de Cáceres F, Ros Barceló A
Department of Plant Biology, Faculty of Sciences, University of La Coruña, Spain.
Z Lebensm Unters Forsch. 1994 Sep;199(3):240-2. doi: 10.1007/BF01193453.
Pepper fruits contain a peroxidase isoenzyme of basic pI, the peroxidase isoenzyme B6, located in vacuoles and the principal component of peroxidase polymorphism in the whole fruit. This isoenzyme was purified by preparative isoelectric focusing in glycerol-stabilized 3.0-10.0 pH gradients and characterized for its ability to oxidize capsaicin (8-methyl-N-vanillyl-6-nonenamide). Spectrophotometric studies illustrated that the capsaicin oxidation by pepper peroxidase isoenzyme B6 was H2O2-dependent and was totally abolished by antibodies raised against horseradish peroxidase. From these studies, it can be concluded that capsaicin is oxidized by pepper peroxidase isoenzyme B6, thus confirming a role for this peroxidase isoenzyme in capsaicin turnover and degradation.
辣椒果实含有一种碱性pH值的过氧化物酶同工酶，即过氧化物酶同工酶B6，它位于液泡中，是整个果实过氧化物酶多态性的主要成分。这种同工酶通过在甘油稳定的3.0 - 10.0 pH梯度中进行制备性等电聚焦进行纯化，并对其氧化辣椒素（8 - 甲基 - N - 香草基 - 6 - 壬烯酰胺）的能力进行了表征。分光光度研究表明，辣椒过氧化物酶同工酶B6对辣椒素的氧化依赖于H2O2，并且被针对辣根过氧化物酶产生的抗体完全消除。从这些研究可以得出结论，辣椒素被辣椒过氧化物酶同工酶B6氧化，从而证实了这种过氧化物酶同工酶在辣椒素周转和降解中的作用。
