Preparation and characterization of gelatin hydrogel support for immobilization of Candida Rugosa lipase


PULAT M., Akalin G. O.

ARTIFICIAL CELLS NANOMEDICINE AND BIOTECHNOLOGY, cilt.41, sa.3, ss.145-151, 2013 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 41 Sayı: 3
  • Basım Tarihi: 2013
  • Doi Numarası: 10.3109/10731199.2012.696070
  • Dergi Adı: ARTIFICIAL CELLS NANOMEDICINE AND BIOTECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.145-151
  • Anahtar Kelimeler: Hydrogels, gelatin, swelling, degradation, lipase immobilization, CONTROLLED-RELEASE, DRUG-DELIVERY, CHITOSAN, MICROSPHERES, DEGRADATION, HYDROLYSIS, BEHAVIOR
  • Gazi Üniversitesi Adresli: Evet

Özet

A series of gelatin hydrogels were prepared by crosslinking method using glutaraldehyde (GA). The hydrogels were characterized by gel formation, swelling/degradation tests, and FTIR analysis. The variations of swelling percentages (S%) with time, temperature, and pH were determined. It is found that the increasing amount of GA causes the decreasing in S% values from 366 to 213% and G-1 was found to be the most swollen hydrogel at pH 7.4 and 37 degrees C. Degradation tests of hydrogel samples were carried out and G-1 hydrogel, which contained the least amount of GA, degraded more rapidly than the others. G-2 hydrogel was chosen for immobilization studies and this procedure was carried out by activation of the hydrogel disc with N-(3-dimethylaminopropyl)-N-ethylcarbodiimid (CDI) coupling agent. The kinetic parameters, K-m and V-max, were calculated. K-m values of free and immobilized lipases were found to be 0.290, 0.422 mM while V-max values were calculated as 0.089, 0.080 mM.min(-1), respectively. For the free and immobilized system, the enzymes retained 32% and 92% of their initial activities, respectively, at the end of 48 days of storage. After using the mentioned immobilized system repeatedly 10 times, it retained 68% of its original activities.