Comparison of the performance of entrapped and covalently immobilized lipase in the synthesis of pear flavor
Yükleniyor...
Dosyalar
Tarih
2017
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Walter De Gruyter Gmbh
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Introduction: Although aroma esters are produced mostly by a chemical method that requires the use of aggressive chemical catalysts, enzymatic esterification has been very favored during previous two decades. The main aim of this study was to investigate the commercially important pear flavor, hexyl acetate (HAc), by the catalysis of immobilized lipase samples and to optimize the immobilization and operational conditions in detail. Methods: Lipases from Candida rugosa (CRL) and porcine pancreas (PPL) were immobilized using biodegradable polysaccharides, by entrapment in calcium alginate/chitosan composite gel (CRLCa-Alg/Chi and PPLCa-Alg/Chi) and by covalent binding onto the chitosan (CRLChi and PPLChi) carrier. Results: Among the several organic media, the highest esterification activites were observed in heptane. HAc yield decreased when substrate concentrations were higher than 50 or 75 mM. Yield increased with increase in reaction time up to the 5th hour in the batch type reactor while it increased during the 8 h reaction time for fixed bed reactors with lower yields. Discussion and conclusions: As well as synthesis conditions, immobilization parameters also affected HAc productivity. The amount of water in the microenvironment of lipase is so important not only for gaining its active conformation but only for the reaction direction.
Açıklama
Anahtar Kelimeler
Lipase, Hexyl acetate, Pear flavor, Alginate, Chitosan, Immobilization, Response surface methodology
Kaynak
Turkish Journal of Biochemistry-Turk Biyokimya Dergisi
WoS Q Değeri
Q4
Scopus Q Değeri
Q3
Cilt
42
Sayı
3
