Effect of salt hydrate pair on lipase-catalyzed regioselective monoacylation of sucrose

Kim, Jae Eun; Han, Jeong Jun; Yoon, Jinsu; Rhee, Jae-Sung

doi:10.1002/(sici)1097-0290(19980105)57:1<121::aid-bit15>3.0.co;2-n

Cited by 48 publications

(12 citation statements)

References 24 publications

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“…Filled circle CALB was not pre-incubated and MS were not added selectivities of the lipases. In agreement, it was suggested that CALB displayed lower regioselectivity than that of RML when sucrose was used as acyl acceptor [37,50,51]. In agreement with Fig.…”

Section: Effect Of High-speed Homogenization (H) And/ or Ultrasound (supporting

confidence: 87%

Effects of Particle Size of Sucrose Suspensions and Pre‐incubation of Enzymes on Lipase‐Catalyzed Synthesis of Sucrose Oleic Acid Esters

Hayes

Burton³

2014

J Americ Oil Chem Soc

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The effects of high‐speed homogenization, high‐intensity ultrasound, and their combination were evaluated for the reduction of the particle size of sucrose crystals to enhance solvent‐free lipase‐catalyzed synthesis of sucrose oleate at 65 °C. The combination of homogenization and ultrasound greatly decreased the particle size of suspended sucrose crystals in mixtures of oleic acid/sucrose oleate (86 wt% monoester and 14 wt% diester at a ratio of 90/10 w/w) from 88 to 18 μm. The suspension‐based medium was charged to a stirred tank bioreactor that also contained immobilized lipase from Rhizomucor miehei or Candida antarctica (Lipozyme®IM and Novozym® 435, respectively; Novozymes, Franklinton, NC, USA), that was pre‐incubated in oleic acid for several different temperatures (23–60 °C), durations (4–24 h), and stir rates (50–400 rpm, radius of 3 cm), prior to use. The optimal performance was achieved using C. antarctica lipase (83.3 wt% ester, consisting of 46 wt% monoester) in the presence of molecular sieves (18 wt%). The low water concentration (~0.12 wt%) did not affect the activity of C. antarctica lipase.

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Section: Effect Of High-speed Homogenization (H) And/ or Ultrasound (supporting

confidence: 87%

Effects of Particle Size of Sucrose Suspensions and Pre‐incubation of Enzymes on Lipase‐Catalyzed Synthesis of Sucrose Oleic Acid Esters

Hayes

Burton³

2014

J Americ Oil Chem Soc

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“…This regioselective performance is quite distinct from the one exhibited by other enzymes in sugar acylation described in the literature. For example, several proteases from the subtilisin family acylate sucrose preferentially at the 1′-OH (7,17,(19)(20)(21) with shortchain ester donors, whereas lipases from Mucor miehei (22), Candida antarctica (23), and Humicola lanuginosa (11) acylate sucrose preferentially at the 6-OH in the glucose ring, yielding a mixture of 6-and 6′-monoesters. Furthermore, it has been shown that Proleather FG-F (15 mg/mL) catalyzed the acylation of sucrose with vinyl acrylate (pyridine, 5 days, 45°C) yielding sucrose 1′-Oacrylate as the main product (isolated yield of 28%) (7).…”

Section: Resultsmentioning

confidence: 99%

Exquisite Regioselectivity and Increased Transesterification Activity of an Immobilized Bacillus subtilis Protease

Ferreira

Ramos

Gil

et al. 2002

Biotechnology Progress

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Commercially available proteases and lipases were screened for their ability to acylate regioselectively sucrose with divinyladipate either in pyridine or dimethylformamide (DMF). The protease (EC 3.4.21.62) from Bacillus subtilis (Proleather FG‐F) exhibited the highest conversion (100% in 24 h of reaction in DMF) yielding sucrose 2‐ O‐vinyladipate as main product. The enzyme preference for a secondary hydroxyl group is a distinct feature of this biocatalyst compared to others described in the literature. Two sets of chemically distinct silica supports were used for Proleather immobilization presenting terminal amino (SAPTES) or hydroxyl groups (STESPM‐pHEMA). The percentage of immobilized enzyme was smaller in SAPTES (7–17%) than in STESPM‐pHEMA (52–56%), yet Proleather immobilized into SAPTES supports presented higher total and specific hydrolytic activity. The highest total and specific activities were obtained with STESPM‐pHEMA and SAPTES, respectively. Silicas with large pore (bimodal distribution of pores, 130/1200 Å, denoted as S1000) presented higher specific activities relative to those with smaller pore sizes. Furthermore, the synthetic specific activity of S1000SAPTES immobilized protease was ca. 10‐fold higher than that of the free enzyme. In addition to sucrose, the immobilized protease was used to acylate methyl α‐d‐glucopyranoside, trehalose, and maltose in nearly anhydrous DMF. Finally, immobilized Proleather was reasonably stable, retaining ca. 55% activity after six reaction cycles.

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“…These results suggest that both substrates, TLN and TC, may have been adsorbed on the binary salts, which may have affected their availability to the enzyme. The mass diffusion limitation, which is due to the high viscosity of the reaction mixture at high salt content, could result by a low productivity [35]. The experimental findings may also indicate that the enzyme could not maintain its active conformation in the reaction system at extreme low a w (0.02), which may limit the formation of CLnC.…”

Section: Effect Of Water Activity On Clnc Productivitymentioning

confidence: 94%

Lipase‐Catalyzed Synthesis of Medium‐Long‐Medium Type Structured Lipids Using Tricaprylin and Trilinolenin as Substrate Models

Bai

Khodadadi

Bou-Mitri

et al. 2012

J Americ Oil Chem Soc

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The synthesis of medium‐long‐medium type structured lipids (SL) by the interesterification of tricaprylin (TC) and trilinolenin (TLN), using selected commercial lipases from Rhizomucor miehei (Lipozyme RM IM) and Candida antarctica (Novozym 435) was investigated. Although the bioconversion yield (BY) for Lipozyme RM IM (24.7 %) was close to that for Novozym 435 (24.0 %), the initial enzyme activity was 6.3 μmol CLnC/g enzyme/min and 1.6 μmol CLnC/g enzyme/min, respectively. Lipozyme RM IM was subsequently selected for further investigation. The structural analyses of SL indicated that the major products were 1,3‐dicapryl‐2‐linolenyl glycerol (CLnC) and 1(3)‐capryl‐2,3(1)‐dilinolenyl glycerol (CLnLn). In order to optimize the BY, selected parameters were investigated. The experimental results showed that using hexane as the reaction medium, at an initial water activity (aw) of 0.06, 10 mg solid enzyme/mL, substrate molar ratio of TC to TLN of 6:1 and a reaction time of 9 h, resulted in the highest BY (73.2 %). Using the optimized conditions, the effects of TLN concentration and other selective parameters, including the denaturation of the enzyme, controlling the aw and the addition of silica gel, on the mass productivity (PM), enzymatic productivity (PE) and volumetric productivity (PV) of the interesterification reaction, were also investigated.

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Effect of salt hydrate pair on lipase-catalyzed regioselective monoacylation of sucrose

Cited by 48 publications

References 24 publications

Effects of Particle Size of Sucrose Suspensions and Pre‐incubation of Enzymes on Lipase‐Catalyzed Synthesis of Sucrose Oleic Acid Esters

Effects of Particle Size of Sucrose Suspensions and Pre‐incubation of Enzymes on Lipase‐Catalyzed Synthesis of Sucrose Oleic Acid Esters

Exquisite Regioselectivity and Increased Transesterification Activity of an Immobilized Bacillus subtilis Protease

Lipase‐Catalyzed Synthesis of Medium‐Long‐Medium Type Structured Lipids Using Tricaprylin and Trilinolenin as Substrate Models

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