Two lipase-catalyzed sequential synthesis of drug derivatives in organic media

Liu, Bo‐Kai; Qian, Xiaofei; Wu, Qi; Lin, Xianfu

doi:10.1016/j.enzmictec.2008.05.008

Cited by 23 publications

(9 citation statements)

References 33 publications

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“…They are resistant to solvents and are exploited in a broad spectrum of biotechnological applications [3]. Novel biotechnological applications, such as biopolymer synthesis [4], biodiesel production [5][6][7], treatment of fat-containing waste effluents [8], enantiopure synthesis of pharmaceuticals [9,10] and nutraceutical agents [11], have been established successfully.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of lipase from Candida rugosa on Sepabeads®: the effect of lipase oxidation by periodates

Prlainović

Knežević‐Jugović

Mijin

et al. 2011

Bioprocess Biosyst Eng

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The objective of this paper was the investigation of a suitable Sepabeads(®) support and method for immobilization of lipase from Candida rugosa. Three different supports were used, two with amino groups, (Sepabeads(®) EC-EA and Sepabeads(®) EC-HA), differing in spacer length (two and six carbons, respectively) and one with epoxy group (Sepabeads(®) EC-EP). Lipase immobilization was carried out by two conventional methods (via epoxy groups and via glutaraldehyde), and with periodate method for modification of lipase. The results of activity assays showed that lipase retained 94.8% or 87.6% of activity after immobilization via epoxy groups or with periodate method, respectively, while glutaraldehyde method was inferior with only 12.7% of retention. The immobilization of lipase, previously modified by periodate oxidation, via amino groups has proven to be more efficient than direct immobilization of lipase via epoxy groups. In such a way immobilized enzyme exhibited higher activity at high reaction temperatures and higher thermal stability.

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Section: Introductionmentioning

confidence: 99%

Immobilization of lipase from Candida rugosa on Sepabeads®: the effect of lipase oxidation by periodates

Prlainović

Knežević‐Jugović

Mijin

et al. 2011

Bioprocess Biosyst Eng

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“…While organic solvents aid in enhancement of enzyme selectivity, it is common for the enzymes to show lower activity and stability in non-aqueous organic solvents [13,[30][31][32][33][34][35][36]. In fact, other drawbacks have also been reported: i) inactivation of enzymes due to irreversible changes in protein conformation; ii) mass-transfer limitations in heterogeneous systems or viscous solvents; iii) poor stability and dispensability of enzymes; and v) the need for water activity control for processes involving condensation reactions [34,[37][38][39][40].…”

Section: Non-aqueous Green Solventsmentioning

confidence: 99%

Enzymatic processes in alternative reaction media: a mini review

et al. 2015

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Biocatalysis is a growing field in the production of fine chemicals and will most probably increase its share in the future. Enzymatic reactions are carried out under mild conditions, i.e., non-toxic solvents, low temperature and pressure, which eliminates most environmental drawbacks associated with conventional production methods. The superiority of chemo-, regio-and enantioselectivity of enzymes exhibit significant advantages over conventional catalysts for production of fine chemicals, flavors, fragrances, agrochemicals and pharmaceuticals. Enzymes can function both in aqueous and non-aqueous solvents. As a result of the growing scientific and industrial interest towards green chemistry, green solvent systems, which are mainly water, supercritical fluids, ionic liquids, fluorinated solvents, and solvent-free systems have become more popular in biocatalysis. However, the activity and selectivity of an enzyme is heavily dependent on solvent properties. In this review, various green solvents were classified and some of their influential features on enzyme activity were discussed.

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“…(O'Brien and Herschlag, 1999;Copley, 2003;Bornscheuer and Kazlauskas, 2004;Khersonsky et al, 2006;Hult and Berglund, 2007). For example, hydrolase can catalyze the formation of C-C (Branneby et al, 2002;Svedendahl et al, 2005;Xu et al, 2007;Liu et al, 2008;Li et al, 2008), C-N (Cai et al, 2004;Torre et al, 2004;Wu et al, 2005Wu et al, , 2006Rodrigo et al, 2009), C-O (Kitazume et al, 1986 and C-S (Carlqvist et al, 2005;Lou et al, 2008) through Michael addition, Markovnikov addition and aldol reaction; arylmalonate decarboxylase can catalyze aldol additions (Terao et al, 2007); racemase can catalyze PLP-dependent aldol additions (Seebeck and Hilvert, 2003). Recently, Herfried Griengl et al successfully reported the first biocatalytic asymmetric Henry reaction in the presence of hydroxynitrile lyase from hevea brasiliensis in two phases.…”

Section: Introductionmentioning

confidence: 99%