Practical application of different enzymes immobilized on sepabeads

Hilterhaus, Lutz; Minow, B.; Müller, Jens; Berheide, Marco; Quitmann, Hendrich; Katzer, Moritz; Thum, Oliver; Antranikian, G.; Zeng, An‐Ping; Liese, Andreas

doi:10.1007/s00449-008-0199-3

Cited by 72 publications

(56 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In another study, kinetics in a fluidized system have a slightly better esterification profile (90.2% yields after 14 h) compared to a batch system [5]. Several esters such as amyl caprylate, ethyl cinnamate, and polyglycerol ester have been reported and synthesized in such reactors [7,23,24].…”

Section: Discussionmentioning

confidence: 99%

Lipase-Catalyzed Synthesis of Kojic Acid Derivative in Bioreactors and the Analysis of Its Depigmenting and Antioxidant Activities

et al. 2017

View full text Add to dashboard Cite

Abstract:In this study, 7-O-kojic acid monopalmitate (7-O-KAP) was synthesized using palmitic acid and kojic acid where the yield and biological activities were analyzed. The highest yield of 7-O-KAP (43%) can be obtained at molar ratio of 1:1, enzyme loading of 5% (w/v), temperature of 70 • C, using immobilized lipase N435 in solvent-free system. Stirred tank reactor (STR) provides better mixing of the substrates and biocatalyst with better yield of 7-O-KAP, compared to fluidized tank reactor (FTR) and packed bed reactor (PBR). The 7-O-KAP exhibited pseudoplastic behavior with flow behavior index (n) being less than 1. The 7-O-KAP showed better depigmenting activity with the reduction of melanin content in Danio rerio embryo to 18.70%, significantly lower than the positive control, kojic acid (60.39%) at highest concentration tested (250 µg/mL). Intracellular tyrosinase in Danio rerio embryo was also reduced when treated with 7-O-KAP (12.53%), compared to kojic acid (37.36%) at concentration of 250 µg/mL. In FRAP assay, 7-O-KAP had antioxidant activity of 8156 AAE/mL, which was higher than kojic acid (6794 AAE/mL) at concentration of 2 mg/mL. The 7-O-KAP also reduced peroxidation activity to 12.21%, which was better compared to kojic acid (31.68%) at 2 mg/mL. Moreover, it was found that lipid peroxidation activity of 7-O-KAP (12.21%) was comparable to BHT (11.56%) at 2 mg/mL. Based on this study, 7-O-KAP could be an alternative compound for whitening agent and antioxidant compared to kojic acid and BHT, respectively.

show abstract

Section: Discussionmentioning

confidence: 99%

Lipase-Catalyzed Synthesis of Kojic Acid Derivative in Bioreactors and the Analysis of Its Depigmenting and Antioxidant Activities

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Lipases from different sources are currently used in various biochemical reactions including triacylglycerols hydrolysis, esterification between fatty acid and alcohol, and other enzymatic reactions [4,5]. Lipases have been utilized in a large number of practical applications, including detergent formulation, oil/fat degradation, pharmaceuticals synthesis, and production of cosmetics [6,7].…”

Section: Introductionmentioning

confidence: 99%

Reversible immobilization of Candida rugosa lipase on fibrous polymer grafted and sulfonated p(HEMA/EGDMA) beads

Arıca

Soydogan

Bayramoğlu

2009

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

Poly(2-hydroxyethyl methacrylate/ethylenglycol dimethacrylate) beads were grafted with poly(glycidylmethacrylate) via surface initiated atom transfer radical polymerization. Epoxy groups of the grafted polymer were modified in to sulfone groups. Sulfonated beads were characterized by swelling studies, FT-IR, SEM and elemental analysis, and were used for reversible immobilization of lipase. Under given experimental conditions, the beads had an adsorption capacity of 44.7 mg protein/g beads. The adsorbed lipase on beads retained up to 67.4% of its initial activity. The immobilized lipase exhibited improved thermal and storage stabilities over those of the free enzyme. The immobilized lipase could desorb 1.0 M NaCl solution at pH 8.0, and the sulfonated beads can be repeatedly charged with fresh enzyme after inactivation upon use.

show abstract

“…It has a highly porous methacrylic polymer matrix and shows low swelling tendency. Different types of Sepabeads have been successfully used for enzyme immobilization [20]. The maximal loading of Sepabeads EC-EP is, according to the manufacturer, 100 mg enzyme per gram carrier [21].…”

Section: Biocatalytic Synthesismentioning

confidence: 99%

Chemically and enzymatically catalyzed synthesis of C₆–C₁₀ alkyl benzoates

Krause

Hilterhaus

Fieg

et al. 2009

Euro J Lipid Sci & Tech

View full text Add to dashboard Cite

The esterification of benzoic acid with n-hexanol, n-octanol, 2-ethyl hexanol and n-decanol was investigated in detail. An analysis of the reaction kinetics of esterification in the presence of different commercially available chemical catalysts was carried out. The effects of catalyst type and loading on the reaction rate were studied. Although the considered reaction is bimolecular, it showed a first-order behavior, and a linear dependence with respect to the catalyst concentration was observed. Hence, a new approach is presented to describe the reaction kinetics accurately over a wide range. The application of biotechnological synthesis applying different enzymes as catalysts offers an interesting alternative besides chemical synthesis. Especially an esterase from Bacillus subtilis immobilized on Sepabeads EC-EP showed high stability and was applied for 2 days in the synthesis of hexyl benzoate. Nevertheless, the chemical reaction route remains superior with respect to the catalyst activities under the applied conditions, which were 25 kU/g for the chemical reaction and 0.7 kU/g for the best enzymatic conversion.

show abstract

Practical application of different enzymes immobilized on sepabeads

Cited by 72 publications

References 37 publications

Lipase-Catalyzed Synthesis of Kojic Acid Derivative in Bioreactors and the Analysis of Its Depigmenting and Antioxidant Activities

Lipase-Catalyzed Synthesis of Kojic Acid Derivative in Bioreactors and the Analysis of Its Depigmenting and Antioxidant Activities

Reversible immobilization of Candida rugosa lipase on fibrous polymer grafted and sulfonated p(HEMA/EGDMA) beads

Chemically and enzymatically catalyzed synthesis of C₆–C₁₀ alkyl benzoates

Contact Info

Product

Resources

About

Practical application of different enzymes immobilized on sepabeads

Cited by 72 publications

References 37 publications

Lipase-Catalyzed Synthesis of Kojic Acid Derivative in Bioreactors and the Analysis of Its Depigmenting and Antioxidant Activities

Lipase-Catalyzed Synthesis of Kojic Acid Derivative in Bioreactors and the Analysis of Its Depigmenting and Antioxidant Activities

Reversible immobilization of Candida rugosa lipase on fibrous polymer grafted and sulfonated p(HEMA/EGDMA) beads

Chemically and enzymatically catalyzed synthesis of C6–C10 alkyl benzoates

Contact Info

Product

Resources

About

Chemically and enzymatically catalyzed synthesis of C₆–C₁₀ alkyl benzoates