Preparation of Genipin by Hydrolysis of Geniposide with Co-Immobilized Enzyme

2011 ◽  
Vol 236-238 ◽  
pp. 1793-1798 ◽  
Author(s):  
Hua Zheng Liang ◽  
He Chen ◽  
Jian Feng Wang ◽  
Yu Lan He

Co-immobilize enzyme by cross-linking and embedding, optimize conditions for immobilizing, determinate the enzymatic properties of co-immobilized enzyme and study the methods for preparation of genipin using co-immobilized enzyme to hydrolyze geniposide. Optimized immobilizing conditions include glutaraldehyde concentration being 0.15%, cross-linking temperature being 20°C, cross-linking time being 2 hours, the activity of co-immobilized β-glucosidase and cell reaches to 65.33U/mg and the enzyme activity recovery being 52.63%. Enzymatic properties of co-immobilized enzyme are following: optimum temperature is 55°C and optimum pH is 5.0. The transformation experiments are carried out with co-immobilized enzyme. The results show that half-life of co-immobilized enzyme reaches around 40 days, higher than the normal immobilized enzyme. The conversion rate of geniposide is above 95% after 8 hours. The genipin is isolated, purified and recrystallized to reach more than 98% of purity by High Performance Liquid Chromatography. Advantages to prepare genipin using co-immobilized enzyme include low cost, high yield, environmental friendly and easy to manufacturing.

2010 ◽  
Vol 76 (11) ◽  
pp. 3554-3560 ◽  
Author(s):  
Joana Gangoiti ◽  
Marta Santos ◽  
Mar�a J. Llama ◽  
Juan L. Serra

ABSTRACT The extracellular medium-chain-length polyhydroxyalkanoate (MCL-PHA) depolymerase of Pseudomonas fluorescens GK13 catalyzes the hydrolysis of poly(3-hydroxyoctanoic acid) [P(3HO)]. Based on the strong tendency of the enzyme to interact with hydrophobic materials, a low-cost method which allows the rapid and easy purification and immobilization of the enzyme has been developed. Thus, the extracellular P(3HO) depolymerase present in the culture broth of cells of P. fluorescens GK13 grown on mineral medium supplemented with P(3HO) as the sole carbon and energy source has been tightly adsorbed onto a commercially available polypropylene support (Accurel MP-1000) with high yield and specificity. The activity of the pure enzyme was enhanced by the presence of detergents and organic solvents, and it was retained after treatment with an SDS-denaturing cocktail under both reducing and nonreducing conditions. The time course of the P(3HO) hydrolysis catalyzed by the soluble and immobilized enzyme has been assessed, and the resulting products have been identified. After 24 h of hydrolysis, the dimeric ester of 3-HO [(R)-3-HO-HO] was obtained as the main product of the soluble enzyme. However, the immobilized enzyme catalyzes almost the complete hydrolysis of P(3HO) polymer to (R)-3-HO monomers under the same conditions.


1999 ◽  
Vol 30 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Rubens Cruz ◽  
Vinícius D'Arcádia Cruz ◽  
Juliana Gisele Belote ◽  
Marcelo de Oliveira Khenayfes ◽  
Claudia Dorta ◽  
...  

<FONT FACE="Symbol">b</font>-Galactosidase or <FONT FACE="Symbol">b</font>-D-galactoside-galactohydrolase (EC. 3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalactosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of <FONT FACE="Symbol">b</font>-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in the 4.04.6 range and the optimum pH for galactosyltransferase activity was in the 6.07.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60°C and 50°C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67% of the lactose from milk and 84% of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40% lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55°C the enzyme converted 86.5% of the lactose to its component monosaccharides. When incubated with a 60% lactose solution in the same buffer but at pH 6.5 and 50°C, the enzyme can synthetize up to 30.5% TOS, with 39.5% lactose and 30% monosaccharides remaining in the preparation.


Micromachines ◽  
2020 ◽  
Vol 11 (2) ◽  
pp. 205
Author(s):  
Dan Xue ◽  
Jiachou Wang ◽  
Xinxin Li

In this paper, we present a novel thermoresistive gas flow sensor with a high-yield and low-cost volume production by using front-side microfabricated technology. To best improve the thermal resistance, a micro-air-trench between the heater and the thermistors was opened to minimize the heat loss from the heater to the silicon substrate. Two types of gas flow sensors were designed with the optimal thermal-insulation configuration and fabricated by a single-wafer-based single-side process in (111) wafers, where the type A sensor has two thermistors while the type B sensor has four. Chip dimensions of both sensors are as small as 0.7 mm × 0.7 mm and the sensors achieve a short response time of 1.5 ms. Furthermore, without using any amplification, the normalized sensitivity of type A and type B sensors is 1.9 mV/(SLM)/mW and 3.9 mV/(SLM)/mW for nitrogen gas flow and the minimum detectable flow rate is estimated at about 0.53 and 0.26 standard cubic centimeter per minute (sccm), respectively.


2012 ◽  
Vol 512-515 ◽  
pp. 1699-1711 ◽  
Author(s):  
Chao Fan ◽  
Ji Lie Li ◽  
Xiao Yuan Zhu ◽  
Nan Li ◽  
Wei Wang ◽  
...  

The process conditions of immobilizing penicillin G acylase(PGA) by epoxy resin were studied. This experiment used the Box-Behnken experimental design and response surface methodology(RSM) to optimize the conditions of immobilizing PGA by epoxy resin. The results showed the best process conditions were pH 8.1, temperature 29°C, carrier of epoxy resin 1g and reaction time 24 h. On these conditions, the activity of the immobilized enzyme was 365.76 U g-1, activity recovery rate was 62.82%. The characteristics of the immobilized PGA under optimal conditions had been measured and found that the optimum pH of immobilized enzyme was 9.0, the optimum temperature was 60°C. It has better continuous operation stability.


Nanophotonics ◽  
2017 ◽  
Vol 7 (2) ◽  
pp. 371-391 ◽  
Author(s):  
Yan-Gang Bi ◽  
Jing Feng ◽  
Jin-Hai Ji ◽  
Fang-Shun Yi ◽  
Yun-Fei Li ◽  
...  

AbstractLightweight and low-cost organic photovoltaics (OPVs) hold great promise as renewable energy sources. The most critical challenge in developing high-performance OPVs is the incomplete photon absorption due to the low diffusion length of the carrier in organic semiconductors. To date, various attempts have been carried out to improve light absorption in thin photoactive layer based on optical engineering strategies. Nanostructure-induced light harvesting in OPVs offers an attractive solution to realize high-performance OPVs, via the effects of antireflection, plasmonic scattering, surface plasmon polarization, localized surface plasmon resonance and optical cavity. In this review article, we summarize recent advances in nanostructure-induced light harvesting in OPVs and discuss various light-trapping strategies by incorporating nanostructures in OPVs and the fabrication processing of the micro-patterns with high resolution, large area, high yield and low cost.


1998 ◽  
Vol 514 ◽  
Author(s):  
Simon Yang

ABSTRACTInterconnect delay is believed to have a dominating impact on the speed of large logic circuits (such as micro-processors) when the Si technology is scaled into sub- 0.25um generations. In this paper, we analyzed interconnect scaling issues based on leading micro-processor trend data, simple RC delay model and the “Rents' rule”. It was concluded that, in order to not limit the speed of large logic circuits, “fat” metal wires need to be used for upper metal layers, which will lead to a rapid increase of required number of metal layers (>10) for sub-0.25um technology generations. Introducing Cu and low ε interconnect system can delay this rapid increase by ∼1 generation. Creating multiple clock frequencies in large logic chips and reducing the size of high frequency islands appears effective in containing the interconnection delay problem. Therefore, the proposed interconnection scaling/development strategy is to introduce Cu and low ε dielectric into manufacturing in next 1∼3 generation (0.25um∼0.13um), develop low cost and high yield interconnect system to enable ∼10 interconnect layers, and improve circuit design methodology to reduce high frequency island size.


1969 ◽  
Vol 115 (4) ◽  
pp. 733-739 ◽  
Author(s):  
M. Cole

1. A method is given for the preparation of penicillin acylase by using Escherichia coli N.C.I.B. 8743 and a strain selected for higher yield. The enzyme is associated with the bacterial cells and removes the side chains of penicillins to give 6-amino-penicillanic acid and a carboxylic acid. 2. The rates of penicillin deacylation indicated that p-hydroxybenzylpenicillin was the best substrate, followed in diminishing order by benzyl-, dl-α-hydroxybenzyl-, 2-furylmethyl-, 2-thienylmethyl-, d-α-aminobenzyl-, n-propoxymethyl- and isobutoxymethyl-penicillin. Phenylpenicillin and dl-α-carboxybenzylpenicillin were not substrates and phenoxymethyl-penicillin was very poor. 3. Amides and esters of the above penicillins were also substrates for the deacylation reaction, as were cephalosporins with a thienylmethyl side chain. 4. For the deacylation of 2-furylmethylpenicillin at 21° the optimum pH was 8·2. The optimum temperature was 60° at pH7. 5. By using selection A of N.C.I.B. 8743 and determining reaction velocities by assaying yields of 6-amino-penicillanic acid in a 10min. reaction at 50° and pH8·2, the Km for benzylpenicillin was found to be about 30mm and the Km for 2-furylmethylpenicillin, about 10mm. The Vmax. values were 0·6 and 0·24μmole/min./mg. of bacterial cells respectively.


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