KaydedilenlerDerginizi ekleyin

Dergiler / Turkish Journal of Biology / 2012 / Cilt: 36 - Sayı: 6

Dipeptidyl peptidase IV production by solid state fermentation using alternative fungal sources

Gaye ÖNGEN
Sayıt SARGIN
Özlem ÜSTÜN
Ceren KUTLU
Mesut YÜCEL
Sayfa
665–671
Yayın Tarihi
2012-06-01
DOI
—
🏛️Bu makalenin bibliyografik verileri ve tam metin bağlantısı DergiPark üzerinden sağlanmıştır.
DergiPark Kaydı ↗
✨

Yapay Zeka Hızlı Bakış & Çıkarımlar

AI Insight
⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

The response for these results was also shown to be in very close agreement with the experimental data.

📌 3 Maddede Bu Makale

🎯
Amaç & Hipotez:The present work was carried out for the production of dipeptidyl peptidase IV (DPP IV; EC 3.4.14.5) using Aspergillus, Penicillium, and Rhizopus strains under solid state fermentation conditions.
📊
Temel Bulgular & Veri:The optimal parameters of DPP IV activity for the independent variables, namely the amount of corn flour (% w/w), initial moisture content (% w/w), and cultivation time (days), were evaluated to be 2.44%, 60.85%, and 4.69 days, respectively, using Aspergillus awamori T116.
💡
Sonuç & Katkı:The response for these results was also shown to be in very close agreement with the experimental data.
🔬Tür:Modelleme & Sayısal Simülasyon
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Key words: Dipeptidyl peptidase IV · Aspergillus · Penicillium

Özet

The present work was carried out for the production of dipeptidyl peptidase IV (DPP IV; EC 3.4.14.5) using Aspergillus, Penicillium, and Rhizopus strains under solid state fermentation conditions. Response surface methodology was applied for the optimization of the selected operational variables (corn flour, initial moisture content, and cultivation time) for DPP IV activity as the response. The optimal parameters of DPP IV activity for the independent variables, namely the amount of corn flour (% w/w), initial moisture content (% w/w), and cultivation time (days), were evaluated to be 2.44%, 60.85%, and 4.69 days, respectively, using Aspergillus awamori T116. The response for these results was also shown to be in very close agreement with the experimental data.

Abstract

The present work was carried out for the production of dipeptidyl peptidase IV (DPP IV; EC 3.4.14.5) using Aspergillus, Penicillium, and Rhizopus strains under solid state fermentation conditions. Response surface methodology was applied for the optimization of the selected operational variables (corn flour, initial moisture content, and cultivation time) for DPP IV activity as the response. The optimal parameters of DPP IV activity for the independent variables, namely the amount of corn flour (% w/w), initial moisture content (% w/w), and cultivation time (days), were evaluated to be 2.44%, 60.85%, and 4.69 days, respectively, using Aspergillus awamori T116. The response for these results was also shown to be in very close agreement with the experimental data.

🔖

Bu Makaleye Atıf Yap

ÖNGEN, G., SARGIN, S., ÜSTÜN, Ö., KUTLU, C., YÜCEL, M. (2012). Dipeptidyl peptidase IV production by solid state fermentation using alternative fungal sources. Turkish Journal of Biology, Cilt: 36 - Sayı: 6, 665–671. https://ajindex.com/articles/182585

📄 Tam Metin PDF Okuyucu

📄

PDF görüntüleyici hazırlanıyor...

Kaynakça (14)

  1. Aleksandra EN, Ivana Z, Matić MD et al. Serum DPP IV activity and CD26 expression on lymphocytes in patients with benign or malignant breast tumors. Immunobiology 216: 942- 946, 2011.
  2. Wasilewska J, Sienkiewicz-Szłapka E, Kuźbida E et al. The exogenous opioid peptides and DPP IV serum activity in infants with apnoea expressed as apparent life threatening events (ALTE). Neuropeptides 45: 189-195, 2011.
  3. Andrade CF, Bigni R, Pombo-de-Oliveira MS et al. CD26/DPP IV cell membrane expression and DPP IV activity in plasma of patients with acute leukemia. J Enzyme Inhib Med Chem 24: 708-714, 2009.
  4. Bergmann A, Bohuon C. Decrease of serum dipeptidyl peptidase activity in severe sepsis patients: relationship to procalcitonin. Clin Chim Acta 321: 23-126, 2002.
  5. Lambeir AM, Proost P, Scharpé SD et al. A kinetic study of glucagon-like peptide-1 and glucagon-like peptide-2 truncation by dipeptidyl peptidase IV, in vitro. Biochem Pharmacol 64: 1753-1756, 2002.
  6. Keane NM, Price P, Lee S et al. An evaluation of serum soluble CD30 levels and serum CD26 (DPP IV) enzyme activity as markers of type 2 and type 1 cytokines in HIV patients receiving highly active antiretroviral therapy. Clin Exp Immunol 126: 111-116, 2001.
  7. Iwaki-Egawa S, Watanabe Y, Kikuya Y et al. DPP IV from human serum: purification, characterization, and N-terminal amino acid sequence. J Biochem 124: 428-433, 1998.
  8. Urade M, Uematsu T, Mima T et al. Serum dipeptidyl peptidase (DPP) IV activity in hamster buccal pouch carcinogenesis with 9,10-dimethyl-1,2-benzanthracene. J Oral Pathol Med 21: 109- 112, 1992.
  9. Püschel G, Mentlein R, Heymann E. Isolation and characterisation of dipeptidyl peptidase IV from human placenta. Eur J Biochem 126: 359-365, 1982.
  10. Cunningham DF, O’Connor B. Proline specific peptidases. Biochim Bophys Acta 1343: 160-186, 1997. Mentlein R. Dipeptidyl peptidase IV (CD26) - role in the inactivation of regulatory peptides. Regul Pept 85: 2-4, 1999.
  11. Baum O, Reuter W, Bermpohl F. Structure function relationship of DPP IV: insight into its dimerisation and gelatinase activity. Adv Exp Med Biol 524: 19-27, 2004.
  12. Iwan M, Jarmolowska B, Bielkowicz K et al. Transport of µ-opioid receptor agonists and antagonist peptides across Caco-2 monolayer. Peptides 29: 1042-1047, 2008.
  13. Hunter LC, O’Hare A, Herron WJ et al. Opioid peptides and dipeptidyl peptidase in autism. Dev Med Child Neurol 45: 121- 128, 2003.
  14. Cade R, Privette R, Fregly M et al. Autism and schizophrenia: intestinal disorders. Nutr Neurosci 3: 53-