BibTex RIS Kaynak Göster

Bacillus subtilis α-amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu ile İncelenmesi.

Yıl 2009, Cilt: 23 Sayı: 1, 13 - 19, 01.04.2009

Öz

Kaynakça

  • Apinan, S., Yujiro, I.., Hidefumi, Y., Takeshi, F., Myllarinen, P., Forssell, P. and K., Poutanen. 2007. Visual observation of hydrolyzed potato starch granules by alpha- amylase with Confocal laser scanning microscopy. Starch-Starke, 59: 543-548. Baldwin, P.M., Davies, M.C. ve C.D., Melia.1997. Starch granule surface imaging using low-voltage scanning electron microscopy and atomic force microscopy. Intl. J Biol. Macromol., 21: 103-7.
  • Dettori-Campus, B.G., Priest, F.G. and J.R., Stark. 1992 Hydrolysis of starch granules by the amylase from B.stearothermophilus NCA. Process Biochem., 27:17-21.
  • Gallant, D.J, Bouchet, B., Buleon, A. and S., Perez. 1992. Physical characteristics of starch granules and suspectibility to enzymatic degradation. Eur. J Clin. Nutr.,46:3 -16.
  • Gawande, B.N. and A.Y., Patkar. 2001. Purification and properties of a novel raw starch degrading cyclodextrin glycosyltransferase from Klebsiella pneumoniae AS-22. Enzyme Microb. Technol., 22:735-743.
  • Hamilton, L.M., Kelly, C.T. and W.M., Fogarty. 1999. Purification and properties of the raw starch degradin amylase of Bacillus sp. IMD 434. Biotechnol. Lett., 21:111-115.
  • Helbert W., Schülerin, M. and B., Henrissat. 1996. Electron microscopic investigation of the diffusion of B.Licheniformis α-amylase into corn starch granules. Intl. J Biol Macromol., 19:165-9.
  • Hyun, H.H. and J.G., Zekius. 1985. Biochemical characterization of thermostable extracellular β-amylase from Clostridium thermosulfurogenes. Appl. Environ. Microbiol., 49:11627.
  • Jespersen, H.M., MacGregor, E.A., Sierks, M.R. and B., Svensson. 1991. Comparison of the domain-level organization of starch hdyrolyses and related enzymes. Biochem. J., 280: 51-5.
  • Jane ek, S., Svensson, B. and B., Henrissat.1997. Domain evolution in α-amylase family. J. Mol. Evol., 45:322-331.
  • Kimura, A. and J.F,. Robty.1995. Reaction of enzymes with starch granules: kinetcis and products of the reaction with glucoamylase. Carbohydr. Res., 227:87-107.
  • Kork, F., Szymonska, J., Tomasik, P. and M., Szymonski. 2000. Noncontact AFM investigation of influence of freezing process on the surface structure of potato starch granule. Appl. Surf. Sci., 157:382-386.
  • Lacerda, L.G.G., Filho, M.A.D.C., Demiate, I.M., Bannach, G., Ionashiro M. and E., Schnitzler. 2008. Thermal behaviour of corn starch granules under action of fungal alpha- amylase. Journal of Thermal Analysis and Calorimetry., 93:445-449.
  • Juszczak L., Fortuna, T. and F., Krok, 2003. Non-contact atomic force microscopy of starch granules surface: Part I. Potato and tapioca starches, Starch/Stärke., 55:1–7.
  • MacGregor, E., Janecek, A., S. and B., Svensson. 2001. Relationship of sequence and structure to specificity in α-amylase family of enzymes. Biochim. Biophys. Acta, 1546:1-20.
  • Manelius, R. and E., Bertoft .1996. The Effect of Ca2+-Ions on the α-Amylolysis of Granular Starches from Oats and Waxy-Maize. Journal of Cereal Science, 24:139-150.
  • Mikami B., Adachi, M., Kage, T., Sarikaya E., Nanmori T., Shinke, R. and S., Utsumi. 1999. Structure of raw-starch digesting Bacillus cereus β-amylase complexed with maltose. Biochemistry., 38(22):7050-7061.
  • Polaina, J. and A.P., MacCabe. 2007. Industrial Enzymes: Structure, Function and Applications. Springer. The Netherlands.
  • Rodríguez-Sanoja, R., Ruiz, B., Guyot, J. P. and S., Sanchez. 2005. Starch-Binding Domain Affects Catalysis in Two Lactobacillus α-Amylases. Appl. Environ. Microbiol. 71(1): 297–302.
  • Sarıkaya, E. and V., Gürgün. 2000. Increase of the α-amylase yield by some Bacillus strains Turk. J Biol., 24:299-308.
  • Sarikaya, E., Higasa, T., Adachi, M. and B., Mikami. 2000. Comparison of the abilities of α-and β-amylases to degrade raw starch granules. Process Biochem., 35:711-5.
  • Shariffa, Y.N, Karim, A.A., Fazilah, A. and I.S.M. Zaidul. 2009. Enzymatic hydrolysis of granular native and mildly heat treated tapioca and sweet potato starches at sub- gelatinization temperature. Food Hydrocolloids., 23: 434-440.
  • Sivak, MN. and J., Preiss. 1998. Starch: Basic Science to Biotechnology. Advanced in food and nutrition research., Vol. 41: 163-70. New York, Academic Pres.
  • Sorimachi, K., Le Gal-Coëffet, M. F., Williamson, Archer, G., D.B. and M.P., Williamson. 1997. Solution structure of the granular starch binding domain of Aspergillus nigerr glucoamylase bound to β-cyclodextrin. Structure., 5:647-661.
  • Southall, S. M., Simpson, P. J., Gilbert, H., J., Williamson, G. and M. P., Williamson. 1999. The starch binding domain from glucoamylase disrupts the structure of starch. FEBS Lett., 447:58-60.
  • Sujka, M, Udeh, K.O. and J., Jamroz .2006. Alpha-amylolysis of native corn, potato, wheat and rice starch granules. Italian Journal of Food Science., 18 (4): 433-439.
  • Sujka, M. and J., Jamroz, 2007.Starch granule porosity and its changes by means of amylolysis. International Agrophysics., 21:107-113.
  • Uhling, H. 1998. Industrial enzymes and their applications. Translated and update by Elfried M. Linsmaier-bednar, Ph. D. New York.
  • Van der Maarel, MJ., Uitdehaag, J.C., Leemhuis H. and L. Dijkhuizen. 2002. Properties and applications of starch-converting enzymes of the a-amylase family. J. Biotech. 94:137-155.
  • Yamamoto, K., Zhang, Z. Z. and S., Kobayashi. 2000. Cycloamylose (cyclodextrin) glucanotransferase degrades intact granules of potato raw starch. J. Agric. Food Chem., 48: 962-966.

Bacillus subtilis α-amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu ile İncelenmesi.

Yıl 2009, Cilt: 23 Sayı: 1, 13 - 19, 01.04.2009

Öz

Bacillus subtilis α-amilazının bitkisel kaynaklı çeşitli nişasta granülleri (patates, buğday, pirinç ve mısır) üzerindeki hidroliz etkisi taramalı elektron mikroskobu kullanılarak incelenmiştir. Amilaz ile muamele edilmemiş patates, buğday ve pirinç granüllerinin yüzeylerinin düzgün ya da hafif pürüzlü olduğu, mısır granüllerinin yüzeyinde küçük görünür porlara sahip olduğu gözlenmiştir. Granüller çok ya da daha az hasara sahipti. Patates sentrifugal tip çevresel parçalanma gösterirken, mısır, buğday ve pirinç granülleri sentipental tip parçalanma göstermiştir. Taramalı elektron mikroskop sonuçları enzimatik hidrolizin esasen mısır, buğday ve pirinç granüllerinin yüzeyinde meydana geldiğini ve amilaz ile nişasta parçalanmasında uzun bir hidroliz periyodunun gerektiğini göstermiştir. Çünkü 24 saat sonunda granüllerde büyük ve derin delikler görülmüştür. Buna karşın, patates granüllerin de ise fazla bir hidroliz saptanmamıştır

Kaynakça

  • Apinan, S., Yujiro, I.., Hidefumi, Y., Takeshi, F., Myllarinen, P., Forssell, P. and K., Poutanen. 2007. Visual observation of hydrolyzed potato starch granules by alpha- amylase with Confocal laser scanning microscopy. Starch-Starke, 59: 543-548. Baldwin, P.M., Davies, M.C. ve C.D., Melia.1997. Starch granule surface imaging using low-voltage scanning electron microscopy and atomic force microscopy. Intl. J Biol. Macromol., 21: 103-7.
  • Dettori-Campus, B.G., Priest, F.G. and J.R., Stark. 1992 Hydrolysis of starch granules by the amylase from B.stearothermophilus NCA. Process Biochem., 27:17-21.
  • Gallant, D.J, Bouchet, B., Buleon, A. and S., Perez. 1992. Physical characteristics of starch granules and suspectibility to enzymatic degradation. Eur. J Clin. Nutr.,46:3 -16.
  • Gawande, B.N. and A.Y., Patkar. 2001. Purification and properties of a novel raw starch degrading cyclodextrin glycosyltransferase from Klebsiella pneumoniae AS-22. Enzyme Microb. Technol., 22:735-743.
  • Hamilton, L.M., Kelly, C.T. and W.M., Fogarty. 1999. Purification and properties of the raw starch degradin amylase of Bacillus sp. IMD 434. Biotechnol. Lett., 21:111-115.
  • Helbert W., Schülerin, M. and B., Henrissat. 1996. Electron microscopic investigation of the diffusion of B.Licheniformis α-amylase into corn starch granules. Intl. J Biol Macromol., 19:165-9.
  • Hyun, H.H. and J.G., Zekius. 1985. Biochemical characterization of thermostable extracellular β-amylase from Clostridium thermosulfurogenes. Appl. Environ. Microbiol., 49:11627.
  • Jespersen, H.M., MacGregor, E.A., Sierks, M.R. and B., Svensson. 1991. Comparison of the domain-level organization of starch hdyrolyses and related enzymes. Biochem. J., 280: 51-5.
  • Jane ek, S., Svensson, B. and B., Henrissat.1997. Domain evolution in α-amylase family. J. Mol. Evol., 45:322-331.
  • Kimura, A. and J.F,. Robty.1995. Reaction of enzymes with starch granules: kinetcis and products of the reaction with glucoamylase. Carbohydr. Res., 227:87-107.
  • Kork, F., Szymonska, J., Tomasik, P. and M., Szymonski. 2000. Noncontact AFM investigation of influence of freezing process on the surface structure of potato starch granule. Appl. Surf. Sci., 157:382-386.
  • Lacerda, L.G.G., Filho, M.A.D.C., Demiate, I.M., Bannach, G., Ionashiro M. and E., Schnitzler. 2008. Thermal behaviour of corn starch granules under action of fungal alpha- amylase. Journal of Thermal Analysis and Calorimetry., 93:445-449.
  • Juszczak L., Fortuna, T. and F., Krok, 2003. Non-contact atomic force microscopy of starch granules surface: Part I. Potato and tapioca starches, Starch/Stärke., 55:1–7.
  • MacGregor, E., Janecek, A., S. and B., Svensson. 2001. Relationship of sequence and structure to specificity in α-amylase family of enzymes. Biochim. Biophys. Acta, 1546:1-20.
  • Manelius, R. and E., Bertoft .1996. The Effect of Ca2+-Ions on the α-Amylolysis of Granular Starches from Oats and Waxy-Maize. Journal of Cereal Science, 24:139-150.
  • Mikami B., Adachi, M., Kage, T., Sarikaya E., Nanmori T., Shinke, R. and S., Utsumi. 1999. Structure of raw-starch digesting Bacillus cereus β-amylase complexed with maltose. Biochemistry., 38(22):7050-7061.
  • Polaina, J. and A.P., MacCabe. 2007. Industrial Enzymes: Structure, Function and Applications. Springer. The Netherlands.
  • Rodríguez-Sanoja, R., Ruiz, B., Guyot, J. P. and S., Sanchez. 2005. Starch-Binding Domain Affects Catalysis in Two Lactobacillus α-Amylases. Appl. Environ. Microbiol. 71(1): 297–302.
  • Sarıkaya, E. and V., Gürgün. 2000. Increase of the α-amylase yield by some Bacillus strains Turk. J Biol., 24:299-308.
  • Sarikaya, E., Higasa, T., Adachi, M. and B., Mikami. 2000. Comparison of the abilities of α-and β-amylases to degrade raw starch granules. Process Biochem., 35:711-5.
  • Shariffa, Y.N, Karim, A.A., Fazilah, A. and I.S.M. Zaidul. 2009. Enzymatic hydrolysis of granular native and mildly heat treated tapioca and sweet potato starches at sub- gelatinization temperature. Food Hydrocolloids., 23: 434-440.
  • Sivak, MN. and J., Preiss. 1998. Starch: Basic Science to Biotechnology. Advanced in food and nutrition research., Vol. 41: 163-70. New York, Academic Pres.
  • Sorimachi, K., Le Gal-Coëffet, M. F., Williamson, Archer, G., D.B. and M.P., Williamson. 1997. Solution structure of the granular starch binding domain of Aspergillus nigerr glucoamylase bound to β-cyclodextrin. Structure., 5:647-661.
  • Southall, S. M., Simpson, P. J., Gilbert, H., J., Williamson, G. and M. P., Williamson. 1999. The starch binding domain from glucoamylase disrupts the structure of starch. FEBS Lett., 447:58-60.
  • Sujka, M, Udeh, K.O. and J., Jamroz .2006. Alpha-amylolysis of native corn, potato, wheat and rice starch granules. Italian Journal of Food Science., 18 (4): 433-439.
  • Sujka, M. and J., Jamroz, 2007.Starch granule porosity and its changes by means of amylolysis. International Agrophysics., 21:107-113.
  • Uhling, H. 1998. Industrial enzymes and their applications. Translated and update by Elfried M. Linsmaier-bednar, Ph. D. New York.
  • Van der Maarel, MJ., Uitdehaag, J.C., Leemhuis H. and L. Dijkhuizen. 2002. Properties and applications of starch-converting enzymes of the a-amylase family. J. Biotech. 94:137-155.
  • Yamamoto, K., Zhang, Z. Z. and S., Kobayashi. 2000. Cycloamylose (cyclodextrin) glucanotransferase degrades intact granules of potato raw starch. J. Agric. Food Chem., 48: 962-966.
Toplam 29 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Bölüm Araştırma Makaleleri
Yazarlar

Elif Demirkan Bu kişi benim

Yayımlanma Tarihi 1 Nisan 2009
Yayımlandığı Sayı Yıl 2009 Cilt: 23 Sayı: 1

Kaynak Göster

APA Demirkan, E. (2009). Bacillus subtilis α-amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu ile İncelenmesi. Uludağ Üniversitesi Ziraat Fakültesi Dergisi, 23(1), 13-19.
AMA Demirkan E. Bacillus subtilis α-amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu ile İncelenmesi. Uludag Üniv. Ziraat Fak. Derg. Nisan 2009;23(1):13-19.
Chicago Demirkan, Elif. “-Amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu Ile İncelenmesi”. Uludağ Üniversitesi Ziraat Fakültesi Dergisi 23, sy. 1 (Nisan 2009): 13-19.
EndNote Demirkan E (01 Nisan 2009) Bacillus subtilis α-amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu ile İncelenmesi. Uludağ Üniversitesi Ziraat Fakültesi Dergisi 23 1 13–19.
IEEE E. Demirkan, “-amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu ile İncelenmesi”., Uludag Üniv. Ziraat Fak. Derg., c. 23, sy. 1, ss. 13–19, 2009.
ISNAD Demirkan, Elif. “-Amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu Ile İncelenmesi”. Uludağ Üniversitesi Ziraat Fakültesi Dergisi 23/1 (Nisan 2009), 13-19.
JAMA Demirkan E. Bacillus subtilis α-amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu ile İncelenmesi. Uludag Üniv. Ziraat Fak. Derg. 2009;23:13–19.
MLA Demirkan, Elif. “-Amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu Ile İncelenmesi”. Uludağ Üniversitesi Ziraat Fakültesi Dergisi, c. 23, sy. 1, 2009, ss. 13-19.
Vancouver Demirkan E. Bacillus subtilis α-amilaz Enziminin Nişasta Granüllerine Etkisinin Taramalı Elektron Mikroskobu ile İncelenmesi. Uludag Üniv. Ziraat Fak. Derg. 2009;23(1):13-9.