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Dergiler / Hacettepe Journal of Biology and Chemistry / 2026 / Volume: 35 Issue: 2

Effect of Some Medium Components on Lactase Production from T. Viride ATCC 32098

Işıl Seyis(Hacettepe University; Department of Biology, Ankara, Turkey)
Nilüfer Aksöz(Hacettepe University; Department of Biology, Ankara, Turkey)
Sayfa
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Yayın Tarihi
2007-04-01
DOI
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Yapay Zeka Hızlı Bakış & Çıkarımlar

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⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

Finally, additional glucosewas not effective on lactase production

📌 3 Maddede Bu Makale

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Amaç & Hipotez:T.viride was used to produce extracellular lactase in different media.
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Temel Bulgular & Veri:Among nitrogensources, NH4 H2PO4 was concluded to be the best nitrogen source, followed by NH4 2HPO4 and NH4 2SO4.
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Sonuç & Katkı:Finally, additional glucosewas not effective on lactase production
🔬Tür:Article
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:carbon source · lactase · nitrogen source

Abstract

T.viride was used to produce extracellular lactase in different media. Effect of various carbon sources lactose, glucose, galactose, sucrose, maltose, fructose and xylan on enzyme production was investigated. Among nitrogensources, NH4 H2PO4 was concluded to be the best nitrogen source, followed by NH4 2HPO4 and NH4 2SO4. Inaddition, increasing NH4 H2PO4 concentration to 0.250 M increased enzyme production. Finally, additional glucosewas not effective on lactase production

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Bu Makaleye Atıf Yap

Seyis, I., Aksöz, N. (2007). Effect of Some Medium Components on Lactase Production from T. Viride ATCC 32098. Hacettepe Journal of Biology and Chemistry, Volume: 35 Issue: 2. https://ajindex.com/articles/1271164

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Kaynakça (19)

  1. Harper, W.J. Milk components and their characteristics, Dairy Technology and Engineering, 2nd Ed., Harper W. J. and Hall C. W.(eds). Avi Publishing Company, Inc. Connecticut, 18-75, 1981.
  2. Apartin, C. and Ronco, A. Development of a free beta-galactosidase in vitro test for the assessment of heavy metal toxicity. Environ Toxicol Water Qual, 16, 117-120, 2001.
  3. Hatzinikolaou, D.G., Katsifas, E., Mamma, D., Karagouni, A.D., Christakopoulos, P. and Kekos, D. Modeling of the simultaneous hydrolysis–ultrafiltration of whey permeate by a thermostable β-galactosidase from Aspergillus niger, Biochem Eng J, 24(2), 161-172, 2005.
  4. Szczodrak, J. and Wiater, A. Selection of method for obtaining an active lactase preparation from Penicillium notatum, J Basic Microb, 38, 71-75, 1998.
  5. Fiedurek, J., Gromada, A. and Jamroz, J. Effect of medium components and metabolic inhibitors on β-galactosidase production and secretion by Penicillium notatum1, J Basic Microb, 36, 27-32, 1996.
  6. Pivarnik, L.F., Senecal, A.G. and Rand, A.G. Hydrolytic and transgalactolosylic activities of commercial beta-galactosidase (lactase) in food processing, Adv Food Nutr Res, 38, 1- 102, 1995.
  7. Fiedurek, J. and Ilczuk, Z. Screening of microorganisms for improvement of β galactosidase production, Acta Microbiol Polonica, 39, 37-42, 1990.
  8. Stainer, R.Y., Adelberg, E.A. and Ingraham, J.L. General Microbiology, Fourth Ed., MacMillan Press Ltd., London, 280-285, 1980. 9. Reczey, K., Stalbrand, H., Hahn-Hegerdal, B. and Tijernal, F. Mycelia-associated β-galactosidase activity in microbial pellets of Aspergillus and Penicillium strains, Appl Microbiol Biot, 38, 393-397, 1992.
  9. Lowry, O.H., Rosenbrough, N.J., Farr, A.L. and Randal, R.J. Protein measurement with the folin reagent, J Biol Chem, 193, 265-275, 1951.
  10. Gomes, J., Gomes, I., Steiner, W. and Esterbauer, H. Production of cellulase and xylanase by a wild strain of Trichoderma viride, Appl Microbiol Biot, 36, 701-707, 1992.
  11. Wong, K.K.Y. and Saddler, J.N. Trichoderma Xylanases, Their Properties and Application, Crit Rev Biotechnol, 12, 413-435, 1992.
  12. Seyis, I. and Aksoz, N. Determination of Some Physiological Factors Affecting Xylanase Production from Trichoderma harzianum 1073 D3, Microbiologica, 26, 75 81, 2003.
  13. Seyis, I. and Aksoz, N. Production of lactase by Trichoderma sp., Food Technol Biotechnol, 42, 121-124, 2004.
  14. Fantes, P.A. and Roberts, C.F. β-galactosidase activity and lactose utilization in Aspergillus nidulans, J Gen Microbiol, 77, 471-486, 1973.
  15. Deshpande, M.S., Deopurkar, R.L. and Rale, V.B. Beta-galactosidase from Auerobasidium pullulans, Lett Appl Microbiol, 9, 21-24, 1989.
  16. Ulezlo, I.V., Tsereteli, A.K., Portnaya, I.B. and Bezborodov, A.M. Beta-galactosidase of the extreme thermophilic anaerobic bacterium Thermoanaerobium sp. 2905 and its immobilization, Appl Biochem Microbiol, 37, 48-52, 2001.
  17. Ismail, S.A., Mabrouk, S.S. and Mahoney, R.R. Purification and characterization of β-galactosidases from Mucor pusillus, J Food Biochem, 21, 145-162, 1997.
  18. Park, Y.K., Santi, M.S.S. and Pastore, G.M. Purification and characterization of β-galactosidase from Aspergillus oryzae, J Food Sci, 44, 100-103, 1979.
  19. Nagy, Z., Kiss, T., Szentirmai, A. and Biro, S. β-galactosidase of Penicillium chrysogenum, purification, and characterization of the enzyme, Protein Expres Purif, 21, 24-29, 2001.