Modification of chitosan-bead support materials with l-lysine and l-asparagine for α-amylase immobilization
 
Yazarlar (6)
Prof. Dr. İdris YAZGAN Kastamonu Üniversitesi, Türkiye
Elizabeth G. Turner Binghamton University State University Of New York, Amerika Birleşik Devletleri
Lauren E. Cronmiller
Binghamton University State University Of New York, Amerika Birleşik Devletleri
Dr. Öğr. Üyesi Muammer Tepe Manisa Celâl Bayar Üniversitesi, Türkiye
Taylan K. Ozturk
Ege Üniversitesi, Türkiye
Prof. Dr. Murat Elibol Ege Üniversitesi, Türkiye
Makale Türü Açık Erişim Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı Bioprocess and Biosystems Engineering
Dergi ISSN 1615-7591 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler SCI
Makale Dili İngilizce Basım Tarihi 03-2018
Kabul Tarihi Yayınlanma Tarihi 08-12-2017
Cilt / Sayı / Sayfa 41 / 3 / 423–434 DOI 10.1007/s00449-017-1876-x
Makale Linki http://link.springer.com/10.1007/s00449-017-1876-x
Özet
Maltose syrups have got wide-range utilizations in a variety of applications from bakery to drug-development. α-Amylases are among the most widely utilized industrial enzymes due to their high specificity in production of maltose syrup from starch. However, enzymes are not stable in ex vivo conditions towards alteration in pH, temperature, and such other parameters as high salt concentrations and impurities, where immobilization is required to advance the stability of the enzyme with which approach the requirement of isolation of the enzyme from media is eliminated as well. In this study, Termamyl® α-amylase was immobilized on the none-modified chitosan beads (NMCB), l-lysine-modified chitosan beads (LMCB), and l-asparagine-modified chitosan beads (AMCB) to assess effects of the support material on optimum conditions and kinetic parameters of the α-amylase activity in production of maltose from starch. Immobilization on NMCB, LMCB, and AMCB puts a strong influence on optimum pH, optimum temperature, stability, and kinetic parameters of α-amylase. Modification of chitosan beads with l-lysine and l-asparagine dramatically altered the overall immobilization yield, and enzyme’s response to pH and temperature variations and the kinetic parameters. AMCB provided the best immobilization yield (49%), while LMCB only improved the yield by 2% from 22 to 24%.
Anahtar Kelimeler
Bacillus licheniformis α-amylases | Chitosan beads | Immobilization | Maltose syrup