2016
DOI: 10.3390/molecules21050646
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Reversible Immobilization of Lipases on Heterofunctional Octyl-Amino Agarose Beads Prevents Enzyme Desorption

Abstract: Abstract:Two different heterofunctional octyl-amino supports have been prepared using ethylenediamine and hexylendiamine (OCEDA and OCHDA) and utilized to immobilize five lipases (lipases A (CALA) and B (CALB) from Candida antarctica, lipases from Thermomyces lanuginosus (TLL), from Rhizomucor miehei (RML) and from Candida rugosa (CRL) and the phospholipase Lecitase Ultra (LU). Using pH 5 and 50 mM sodium acetate, the immobilizations proceeded via interfacial activation on the octyl layer, after some ionic bri… Show more

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Cited by 60 publications
(37 citation statements)
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“…Another alternative is to maintain all enzyme-support interactions reversible, mixing interfacial activation (mainly hydrophobic) with other physical interactions of a fully different nature. Although this additional interaction could involve immobilized chelates (Zucca et al, 2016), thiol disulfide reactive groups (Brena et al, 1993;Grazú et al, 2003;Pavlovic et al, 2003), dyes (Yakup Arıca et al, 1998), etc., the only one that we have been able to find is the use of long acyl moieties mixed with anion or cation groups, using agarose beads (Rueda et al, 2016d(Rueda et al, , 2016a.…”
Section: Maintaining the Reversibility Of The Immobilizationmentioning
confidence: 99%
“…Another alternative is to maintain all enzyme-support interactions reversible, mixing interfacial activation (mainly hydrophobic) with other physical interactions of a fully different nature. Although this additional interaction could involve immobilized chelates (Zucca et al, 2016), thiol disulfide reactive groups (Brena et al, 1993;Grazú et al, 2003;Pavlovic et al, 2003), dyes (Yakup Arıca et al, 1998), etc., the only one that we have been able to find is the use of long acyl moieties mixed with anion or cation groups, using agarose beads (Rueda et al, 2016d(Rueda et al, , 2016a.…”
Section: Maintaining the Reversibility Of The Immobilizationmentioning
confidence: 99%
“…CALA has a large lid able to isolate the active center from the medium, undergoes conventional interfacial activation upon adsorption on hydrophobic surfaces, and has been immobilized in many hydrophobic supports . CALB is a lipase having a very small lid that does not isolate the activity center from the medium .…”
Section: Introductionmentioning
confidence: 99%
“…CALA has a large lid able to isolate the active center from the medium, 49,50 undergoes conventional interfacial activation upon adsorption on hydrophobic surfaces, 51 and has been immobilized in many hydrophobic supports. [52][53][54] CALB is a lipase having a very small lid that does not isolate the activity center from the medium. 51,55,56 That way, the hydrophobic pocket surrounding the active center is smaller than in the case of CALA, and the enzyme may be immobilized on hydrophobic surfaces, [57][58][59][60][61] but not in the open form of other lipases.…”
Section: Introductionmentioning
confidence: 99%
“…However, some issues, such as the limited range of temperature, recyclability, and long‐term stability, stand as challenges for the utilization of these biocatalysts in large‐scale productions . A widely used strategy to overcome these problems is the immobilization of the enzyme into a solid substrate . Reported for the first time in 1916, this method has grown significantly over the past decades allowing for the economic viability of the use of several enzymes in industrial processes, causing a great economic and scientific impact.…”
Section: Introductionmentioning
confidence: 99%
“…[27,28] Aw idely used strategy to overcome these problems is the immobilizationo ft he enzyme into as olid substrate. [29,30] Reported for the first time in 1916, [31] this methodhas grown significantly over the past decades allowing for the economicv iability of the use of several enzymes in industrial processes, causing ag reat economic and scientific impact.T he immobilization of enzymes on ah eterogeneous substrate promotes ac onvenient handling and af acile separation of the biocatalyst from the reaction medium. [32] Additionally,i to ften enhances enzyme stabilityt owards denaturation by autolysis, decomposition by organic solvents or by heat, as well as boosting the enzyme activity.…”
Section: Introductionmentioning
confidence: 99%