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Mikrobiyal Dipeptidil Peptidaz IV’ün Kinetik Özelliklerinin Belirlenmesi
(Determination of Kinetic Parameters of Microbial Dipeptidyl Peptidase IV )

Author : Özlem ÜSTÜN AYTEKİN  Sevda ARISOY  
Type :
Printing Year : 2018
Number : 2018-1
Page : 28-37


Summary
Dipeptidil peptidaz IV (EC 3.4.14.5; DPPIV) enzimi tüm doku, organ ve sistemlerin düzenlenmesinde rol alan, nörolojik, immünolojik ve gastroenterolojik açıdan araştırılan önemli bir enzimdir. DPPIV enzimi pek çok memeli, bitki, böcek ve mikrobiyal hücrelerde regüle edici enzim olarak eksprese edilmektedir. DPPIV enziminin sindirim enzimi eksikliği, otizm, çölyak ve Asperger sendromu gibi hastalıklarda gıda takviyesi olarak kullanımıyla son yıllarda ticari olarak üretilmesi artmıştır. DPPIV enzim kaynağı olarak hücre-dışı enzim ekspresyonu yapan fungal kaynaklar tercih edilmesine rağmen bakterilerin enzim üretim verimliliği funguslara göre daha fazla olduğundan son yıllardaki ticari enzim üretimlerinde bakteriler tercih edilmektedir. Bu çalışmada, koleksiyon kültüründen satın alınmış bir laktik asit bakterisi, Lactococcus lactis spp. lactis (L. lactis), enzim üreticisi mikroorganizma olarak seçilmiştir. L. lactis, kazein proteinini hidrolizlemek için endo- ve ekzo-peptidazlar eksprese eder. DPPIV enzimi de bunlardan biridir. Hücre-içi DPPIV enzimi, üretiminden sonra saflaştırılmış ve ardından enzim karakterizasyonunu yapmak için kinetik özellikleri incelenmiştir. Sonuçlar, Gly-Pro-pNA substratı için optimum sıcaklığın 40°C ve optimum pH’nın 8,0 olduğunu göstermektedir. Saflaştırılan enzim spesifik substrat olarak Gly-Pro-pNA tercih etmiş ve Hg+2, Zn+2, Ca+2, Fe+2 ve Mg+2 iyonları tarafından sırası ile inhibe edilmiştir. Enzim, Diprotin A tarafından güçlü bir şekilde inhibe edilmiştir. Jelatin inhibisyonu fenilmetilsulfonil florid (PMSF) inhibisyonu ile yakın bulunmuş ve etilendiamin tetra asetik asitin (EDTA) inhibisyona etkisi gözlenmemiştir.

Turkish Keywords
Dipeptidil Peptidaz IV, enzim inhibisyonu, enzim kinetiği, Lactococcus lactis spp. lactis

Abstract
Dipeptidyl peptidase IV (EC 3.4.14.5; DPPIV) is an important enzyme that has role for regulation of tissue and organ systems and been investigated for neurological, immunological and gastroenterological aspects. DPPIV is expressed as regulator enzyme by mammalian, plant, insect and microbial cells. Recently, commercial DPPIV enzyme production has increased via using as dietary supplement for people who suffer from deficiency of digestion enzyme, autism, celiac and Asperger syndrome. Although fungal resources which are expressing extracellular enzyme were preferred to produce DPPIV, production of DPPIV is recently performed by bacteria; because, productivity values are generally higher in bacteria than fungus. In this study, Lactococcus lactis spp. lactis (L. lactis) was used as an enzyme producer microorganism. L. lactis expresses endo– and exo-peptidases which DPPIV is one of them to hydrolyze casein. Intracelluler DPPIV enzyme was purified after the production and some of kinetic properties were investigated for enzyme characterization. Results indicated that the optimum pH and temperature were 8.0 and 40°C with Gly-Pro-pNa as the substrate, respectively. Purified enzyme showed a strong preference for Gly-Pro-pNA as substrate. The enzyme was inhibited by Hg+2, Zn+2, Ca+2, Fe+2 and Mg+2, respectively. It is important and serin protease inhibitor PMSF. The enzyme was strongly inhibited by Diprotin A. Inhibition of the enzyme by jelatin and phenylmethylsulfonyl fluoride (PMSF) were found as similar, and no inhibition was detected with ethylenediaminetatraacetic acid (EDTA).

Keywords
Dipeptidyl Peptidase IV, enzyme inhibition, enzyme kinetic, Lactococcus lactis spp. lactis

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