Spectrophotometric Determination of Protein with DBC-Chlorophosphonazo

Wang, Qingshuang; Zhai, Qing-Zhou; Luo, Jie

doi:10.14233/ajchem.2013.14820

Cited by 6 publications

(4 citation statements)

References 1 publication

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“…To one of the volumetric flasks, 2-7 mg of the protein standard solution was added and diluted with water to the mark and shaken. The solution was allowed to stand for 35 min at room temperature and using the corresponding reagent blank as a reference and with 1 cm cell absorbance was measured at 600 nm 16 .…”

Section: Methodsmentioning

confidence: 99%

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Characterization of (SBA-15)-Lipase Composite Material

Sun¹,

Zhai²

2014

Asian J. Chem.

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Santa Barbara Amorphous (SBA)-15 mesoporous material was synthesized by hydrothermal method using tri-block copolymer poly(ethylene glycol)-block-poly(propylene glycol)-block-poly(ethylene glycol) (Pluronic P123) as a structure-directing agent and then phenyltriethoxysilane was used to to obtain phenylated SBA-15. Then physical adsorptive method was employed to immobilize lipase to the host material. The immobilized efficiency of enzyme was improved to some extent for the phenylated SBA-15. For structural characterization of prepared samples, powder X-ray diffraction, Fourier transform infrared spectroscopy and low temperature N2 adsorptiondesorption at 77 K were used. The study confirmed that the enzyme went into the pore channels of the SBA-15. Scanning electron microscopic studies showed that the average particle diameter of (SBA-15)-lipase was 337 ± 10 nm, while the average particle diameter of (phenylated SBA-15)-lipase was 340 ± 10 nm. Luminescent spectra showed that the enzyme had already successfully been immobilized to the host materials and after the enzyme was immobilized into host materials the configuration had not been changed. The experimental results of activity on the hydrolysis of glycerol triacetate catalyzed by lipase indicated that compared the immobilized lipase with free lipase the catalytic activity was enhanced and the catalytic use rate of lipase was improved and the ability of resistance to temperature was improved. The repeated use number of the phenylated SBA-15 immobilized lipase as catalyst was improved compared with that of SBA-15 immobilized lipase.

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Section: Methodsmentioning

confidence: 99%

“…The content of lipase was determined by using dibromo-p-chloro-chlorophosphonazo spectrophotometry 16 . According to Beer's law,working curve for the determination of lipase was obtained.…”

Section: Lipase Determination Working Curve and Immobilization Amount...mentioning

confidence: 99%

Characterization of (SBA-15)-Lipase Composite Material

Sun¹,

Zhai²

2014

Asian J. Chem.

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“…Calculative method for the immobilization amount of α α α α α-amylase: Determination method for α-amylase used dibromo-p-chloro-chlorophosphonazo spectrophotometry 11 . The pepsin amount adsorbed in SBA-15 is equals to the total amount of α-amylase minus the α-amylase amount in supernatant, which can be calculated by the following formula:…”

Section: Synthesis Of Materialsmentioning

confidence: 99%

“…An ASAP 2020 surface and porosity analyzer (Micromeritics Instrument Corporation, USA) was used to determine the N2 adsorption-desorption isotherm curve of sample at 77 K. By means of BET (Brunauer-Emmett-Teller) method 13 and BJH (Barrett-Joyner-Halenda) method 14 , the specific surface area and average pore size of sample were calculate, respectively. α-Amylase component content determination in (SBA-15)-(α-amylase) was obtained by the spectrophotometry 11 with subtraction method with a 722S type spectrophotometer (Shanghai Lengguang Technology Co., Ltd., China).…”

Section: Synthesis Of Materialsmentioning

confidence: 99%

Immobilization of a-Amylase by SBA-15

Zhai¹

2014

Asian J. Chem.

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; AJC-15110 SBA (Santa Barbara Amorphous)-15 mesoporous material was prepared by hydrothermal synthesis and the sample was characterized by X-ray diffraction and scanning electron microscopy. The immobilization of α-amylase by SBA-15 was made by physical adsorption method and the optimal conditions of immobilization of α-amylase by SBA-15 were obtained as follows: pH = 5.4, α-amylase concentration:2 mg/mL, immobilization time:27 h, temperature:30 °C. At the same time, it is concluded that the maximum amount of αamylase immobilized by SBA-15 was 87.5 mg/g. By studying of chemical analysis, scanning electron microscopy, infrared spectroscopy, X-ray diffraction, low temperature N2 adsorption-desorption analysis characterization, the α-amylase was immobilized on the SBA-15 carrier was proved. Catalytic experimental results indicated that (SBA-15)-(α-amylase) composite material has the advantages of high pH value resistance and high temperature resistance compared with the free enzyme and has a higher potential applied value.

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