Immobilization of<i>Bacillus licheniformis</i><scp>L</scp>-Arabinose Isomerase for Semi-Continuous<scp>L</scp>-Ribulose Production

Zhang, Ye-Wang; Prabhu, Ponnandy; Lee, Jung-Kul

doi:10.1271/bbb.90330

Cited by 22 publications

(8 citation statements)

References 34 publications

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“…The immobilization yield was found to be 72.5% and enzyme loading efficiency was calculated as 87.52%. Similar approach was used to calculate the loading efficiency and immobilization yield (Zhang et al 2009).…”

Section: Laccase Immobilization On To Z-pvp Nano Fibrous Membranementioning

confidence: 99%

Optimization and efficacy studies of Laccase immobilized on Zein-Polyvinyl pyrrolidone nano fibrous membrane in decolorization of Acid Red 1

Paul²,

Sunkar

2021

Water Science and Technology

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Azo dyes are widely used in textile industries. A significant portion of these recalcitrant dyes are being discharged to the natural waters. Due to their low biodegradability they pose serious pollution problems if untreated. In this work, decolourization studies of Acid Red 1 (AR1) by laccase enzyme immobilized onto Zein – Polyvinyl pyrrolidone composite nanofiber is done. The nanofibers were characterized by SEM and FTIR analysis. pH and temperature profiles of immobilized enzyme were found to be broader than its free counterpart. The Km value was found to be 0.243 mM for free laccase and 0.958 mM for immobilized laccase. Similarly Vmax for the free enzyme was 3.572 U/mg compared to 2.48 U/mg of immobilized laccase. The relative activity of immobilized laccase was 64.91% after storage for 30 days at room temperature while it was 28.64% for free laccase. The temperature and pH for AR 1 decolorization were optimized and was found to be 60 °C and 5 respectively. Also decolorization percentage was found to be 91.67% for immobilized laccase and 72.03% of free laccase in the presence of natural mediators like vanillin. From phytotoxicity studies it was found that the germination rate, shoot and root length was increased compared to untreated dye. Therefore, Zein-PVP nanofiber immobilized laccase could be an ideal candidate for the textile dye decolorization.

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Section: Laccase Immobilization On To Z-pvp Nano Fibrous Membranementioning

confidence: 99%

Optimization and efficacy studies of Laccase immobilized on Zein-Polyvinyl pyrrolidone nano fibrous membrane in decolorization of Acid Red 1

Paul²,

Sunkar

2021

Water Science and Technology

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“…l -Arabinose isomerase (EC 5.3.1.4) is an intracellular enzyme that catalyzes the partial isomerization of l -arabinose to l -ribulose in vivo [ 17 , 18 , 19 , 20 , 21 , 22 ]. In vitro experiments have shown that this biocatalyst can also convert d -galactose to d -tagatose, a rare sugar with promising nutraceutical properties [ 23 , 24 ].…”

Section: Introductionmentioning

confidence: 99%

Immobilized Trienzymatic System with Enhanced Stabilization for the Biotransformation of Lactose

Torres

Batista‐Viera

2017

Molecules

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The use of ketohexose isomerases is a powerful tool in lactose whey processing, but these enzymes can be very sensitive and expensive. Development of immobilized/stabilized biocatalysts could be a further option to improve the process. In this work, β-galactosidase from Bacillus circulans, l-arabinose (d-galactose) isomerase from Enterococcus faecium, and d-xylose (d-glucose) isomerase from Streptomyces rubiginosus were immobilized individually onto Eupergit C and Eupergit C 250 L. Immobilized activity yields were over 90% in all cases. With the purpose of increasing thermostability of derivatives, two post-immobilization treatments were performed: alkaline incubation to favor the formation of additional covalent linkages, and blocking of excess oxirane groups by reacting with glycine. The greatest thermostability was achieved when alkaline incubation was carried out for 24 h, producing l-arabinose isomerase-Eupergit C derivatives with a half-life of 379 h and d-xylose isomerase-Eupergit C derivatives with a half-life of 554 h at 50 °C. Preliminary assays using immobilized and stabilized biocatalysts sequentially to biotransform lactose at pH 7.0 and 50 °C demonstrated improved performances as compared with soluble enzymes. Further improvements in ketohexose productivities were achieved when the three single-immobilizates were incubated simultaneously with lactose in a mono-reactor system.

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“…Chemically, chitosan is a linear polysaccharide composed of β‐(1‐4)‐linked D‐glucosamine and N ‐acetyl‐D‐glucosamine . The presence of amine and hydroxyl groups in the chitosan molecule makes it an attractive support for enzyme immobilization and in fact several immobilization methods using chitosan as support have been developed, including encapsulation, entrapment, physical adsorption, and covalent attachment . Additionally, the nontoxicity and biocompatibility of chitosan make it an appropriate support for producing immobilized biocatalysts, especially for food and pharmaceutical processes …”

Section: Introductionmentioning

confidence: 99%

Influence of chitosan derivatization on its physicochemical characteristics and its use as enzyme support

Urrutia

Bernal

Escobar

et al. 2013

J of Applied Polymer Sci

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Chitosan was derivatized by two methodologies for analyzing their effect on chitosan physicochemical characteristics and its applicability as carrier for Bacillus circulans b-galactosidase immobilization. Glutaraldehyde (GA) and epichlorohydrin (EPI) were used for crosslinking and activation of chitosan, producing the corresponding supports (C-GA and C-EPI-EPI) after a one-step and a twostep process, respectively. The spherical shape and mean diameter of chitosan particles was not significantly affected by polymer derivatization, while Fourier transform infrared analysis showed that in both cases, chitosan polymer was chemically modified. TGA analysis indicated that C-EPI-EPI was the most thermally stable. The high degree of activation of C-EPI-EPI (586 lmol of aldehydes/g) resulted in the highest loss of activity during immobilization; hence a support with 100 lmol of aldehydes/g was produced (C-EPI-EPI 100 ). The highest expressed activity (89.3 IU/g) was obtained with the enzyme immobilized in C-GA, while the biocatalyst with highest thermal stability at 60 C was obtained with C-EPI-EPI 100 (half-life was 84-fold higher than the one of the soluble enzyme). The best compromise between biocatalyst expressed activity and thermal stability corresponded to b-galactosidase immobilized in C-EPI-EPI 100 . According to this study, chitosan derivatized with EPI is a thermally stable carrier appropriate for producing highly stable immobilized B. circulans b-galactosidase. V C 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014, 131, 40171.

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Immobilization ofBacillus licheniformisL-Arabinose Isomerase for Semi-ContinuousL-Ribulose Production

Cited by 22 publications

References 34 publications

Optimization and efficacy studies of Laccase immobilized on Zein-Polyvinyl pyrrolidone nano fibrous membrane in decolorization of Acid Red 1

Optimization and efficacy studies of Laccase immobilized on Zein-Polyvinyl pyrrolidone nano fibrous membrane in decolorization of Acid Red 1

Immobilized Trienzymatic System with Enhanced Stabilization for the Biotransformation of Lactose

Influence of chitosan derivatization on its physicochemical characteristics and its use as enzyme support

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