Poly(acrylamide/vinylsulfonic acid) hydrogel for invertase immobilization

ÖZTOP H. N., Akyildiz F., SARAYDIN D.

MICROSCOPY RESEARCH AND TECHNIQUE, cilt.83, sa.12, ss.1487-1498, 2020 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 83 Sayı: 12
  • Basım Tarihi: 2020
  • Doi Numarası: 10.1002/jemt.23542
  • Dergi Adı: MICROSCOPY RESEARCH AND TECHNIQUE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Aerospace Database, Agricultural & Environmental Science Database, Aquatic Science & Fisheries Abstracts (ASFA), Biotechnology Research Abstracts, CAB Abstracts, Communication Abstracts, EMBASE, MEDLINE, Metadex, Veterinary Science Database, Civil Engineering Abstracts
  • Sayfa Sayıları: ss.1487-1498
  • Anahtar Kelimeler: acrylamide, hydrogel, invertase immobilization, SEM, vinylsulfonic acid, CEREVISIAE EXTERNAL INVERTASE, VINYL-SULFONIC-ACID, SACCHAROMYCES-CEREVISIAE, THERMAL-STABILITY, VINYLSULFONIC ACID, CHITOSAN, ADSORPTION, COMPOSITE, DIFFUSION, CATALASE
  • Sivas Cumhuriyet Üniversitesi Adresli: Evet

Özet

Poly (acrylamide/vinylsulfonic acid) PA/VSA and poly (acrylamide) PA hydrogels were prepared by free radical polymerization in the presence of a crosslinker, to be used as a support for the invertase enzyme. Spectrophotometric, thermal analysis methods, swelling, and diffusion experiments were used for the characterization of hydrogels. SEM images show that the hydrogels have a smooth, homogeneous, highly porous and spongy morphology. The swelling of PA/VSA was higher than that of PA in water. The diffusion of water within the hydrogel was found to be non-Fickian. Invertase was immobilized onto PA and PA/VSA (immobilized invertases named PA-I and PA/VSA-I, respectively). The optimum pH values were found to be; 5.0, 3.0, and 3.0 for free invertase, PA-I, and PA/VSA-I, respectively. The optimum temperature values were 40 degrees C, 50 degrees C, and 60 degrees C for free invertase, PA-I and PA/VSA-I respectively. Michaelis Constant,K-m; for free invertase and PA-I and PA/VSA-I were found to be 11.80, 21.40, and 18.42 mM, respectively. Maximum reaction rate;V(max)value for free invertase and PA-I and PA/VSA-I were found to be 7.46 mu mol min(-1), 5.91 mu mol min(-1), and 6.35 mu mol min(-1), respectively. PA/VSA-I showed excellent thermal, operational, storage, and pH stability.