The Value of Bifunctional Catalase-Phenol Oxidase and Other Catalases in Food Industry (Turkish with English Abstract)

Abstract

Catalases, responsible for hydrogen peroxide degradation into water and oxygen and belonging to a group of antioxidant metalloenzymes, are known as promoting cellular life. They are widely used in food either alone in milk pasteurization and cheese production or its combination with glucose oxidase in the production of dietetic beverages and maltose excluding glucose and invert sugar that does not contain fructose. The need for economic and highly stable catalase production has recently become inevitable due to an increase in the use of hydrogen peroxide in the industry. Despite catalases have been functionally and structurally studied for many years, some unknown characteristics of these enzymes are still coming up. For example, the thermophilic fungus Scytalidium thermophilum constituvely produces a catalase in a growth- associated manner, and this catalase possesses an additional phenol oxidase activity in the absence of hydrogen peroxide. With this discovery, it was also shown that catalases, found in various organisms including humans, exhibit oxidase activity at varying degrees. Although research on catalases has been going on for more than a century, the peroxide independent secondary oxidase activity of these enzymes is a new discovery in the literature. Studies of changing three dimensional structure of enzyme with protein engineering to increase the effectiveness of oxidase activity in catalase have already been started. In this manner, the chance of catalase production with low cost and high yield, which can remove both hydrogen peroxide and oxygen at one step, has encouraged the in-depth investigation of these enzymes.

Keywords

• Food, hydrogen peroxide, catalase, oxidase, Scytalidium thermophilum

Çift Aktiviteli Katalaz-Fenol Oksidazının ve Diğer Katalazların Gıda Sanayisindeki Önemi

Abstract

Katalazlar, hidrojen peroksiti su ve oksijene dönüştüren, antioksidan metalloenzimler grubuna dahil, hücre ömrünün uzamasına önemli katkıları olduğu bilinen enzimlerdir. Gıdalarda, gerek tek başlarına süt pastörizasyonunda ve peynir yapımında, gerekse glukoz oksidaz ile beraber glukoz içermeyen diyetetik içecekler, fruktoz içermeyen invert şeker ve glukoz içermeyen maltoz üretiminde kullanılmaktadırlar. Son yıllarda hidrojen peroksitin endüstride kullanımının artması, ekonomik ve oldukça kararlı katalaz enziminin üretilmeye çalışılmasını gerekli kılmıştır. Katalaz enziminin fonksiyonel ve yapısal karakterizasyonu uzun yıllardır çalışılmış olmasına rağmen halen enzimin bilinmeyen karakteristik özellikleri ortaya çıkmaktadır. Örneğin, termofilik bir mantar olan Scytalidium thermophilum’un büyümeye bağlı olarak sürekli (konstitütif) bir şekilde ürettiği katalaz, hidrojen peroksit yokluğunda fenol oksidaz aktivitesi de göstermektedir. Bu özelliğin keşfi ile birlikte, insan da dâhil çok farklı organizmaların katalazlarında değişen oranlarda oksidaz aktivitesi olduğu belirlenmiştir. Katalazlar üzerine yaklaşık yüz yıldır çalışıldığı halde, bu enzimlerin peroksitten bağımsız ikincil oksidaz aktivitesi literatürde yeni bir bulgudur. Katalazın oksidaz aktivitesinin etkinliğini arttırmak için üç boyutlu yapısının protein mühendisliği ile değiştirilmesi çalışmalarına başlanmıştır. Bu şekilde, tek aşamada hem hidrojen peroksiti hem de oksijeni ortamdan uzaklaştırabilecek maliyeti düşük ve yüksek verimli katalazların üretilmesi olasılığı, bu enzimlerin araştırılmasında yepyeni ufuklar açmıştır.

Keywords

• Gıda, hidrojen peroksit, katalaz, oksidaz, Scytalidium thermophilum

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