Immobilization of invertase on celite and on polyacrylamide by an absorption procedure

Mansour, E. H.; Dawoud, Fathy M

doi:10.1002/jsfa.1390

Cited by 30 publications

(16 citation statements)

References 13 publications

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“…The highest activity for invertase and glucose oxidase was observed at pH 4.5 (0.041 mg TRS/min mL) and pH 5.5 (11.5×10 −4 mg H 2 O 2 /min mL), respectively. Both pH values are in agreement with those found in the literature [17][18][19][20].…”

Section: Resultssupporting

confidence: 92%

Multienzymatic Sucrose Conversion into Fructose and Gluconic Acid through Fed-Batch and Membrane-Continuous Processes

Taraboulsi

Tomotani²,

Vítolo³

2011

Appl Biochem Biotechnol

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Multienzymatic conversion of sucrose into fructose and gluconic acid was studied through fed-batch and continuous (in a membrane reactor) processes. The law of substrate addition (sucrose or glucose) for the fed-batch process which led to a yield superior to 80% was the decreasing linear type, whose feeding rate (ϕ; L/h) was calculated through the equation: ϕ = ϕ(o) - k.t, where ϕ(o) (initial feeding rate, L/h), k (linear addition constant, L/h (2)), and t (reaction time, h). In the continuous process, the yield of conversion of sucrose (Y) was superior to 70% under the following conditions: dilution rate = 0.33 h(-1), total duration of 15 h, pH 5.0, 37 °C and initial sucrose concentration of 64 g/L (Y = 92%), 100 g/L (Y = 83%), or 150 g/L (Y = 76%).

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Section: Resultssupporting

confidence: 92%

Multienzymatic Sucrose Conversion into Fructose and Gluconic Acid through Fed-Batch and Membrane-Continuous Processes

Taraboulsi

Tomotani²,

Vítolo³

2011

Appl Biochem Biotechnol

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“…Since it is well known that all the protein that added to the matrix is not bound. Mansour and Dawoud (2003) suggested that increasing the enzyme loading above the saturation level resulted in the gradual decrease in the enzyme activity. This is because a high concentration of enzyme on the external surface can contribute to internal diffusional restrictions, thus leading to the underestimation of the initial activity of the immobilized enzyme (Wilson et al .…”

Section: Resultsmentioning

confidence: 99%

Optimization of Immobilization Process on Crab Shell Chitosan and Its Application in Food Processing

Dhananjay

Mulimani

2008

Journal of Food Biochemistry

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Optimization of immobilization process on crab shell chitosan was carried out. The chitosan purified from the crab shell was used as the matrix for the immobilization of α‐galactosidase. The prepared matrix was activated with glutaraldehyde at different concentrations and different time intervals and coupling time was determined. Immobilization of α‐galactosidase on crab shell chitosan resulted in 72% immobilization yield. The parameters like the effect of pH, temperature, thermal stability and storage stability were determined. The study revealed that immobilized enzyme shows better thermal and storage stability than the free enzyme. The performance of the free and immobilized α‐galactosidase was tested in continuous stirred batch reactor to hydrolyze raffinose family oligosaccharides in soymilk. The oligosaccharide content of the soymilk was reduced by 77% in continuous reaction by immobilized α‐galactosidase. PRACTICAL APPLICATIONS Chitosan used for the immobilization of α‐galactosidase offers several advantages for enzyme immobilization and it contains all characteristic features for use as industrial material. Immobilization of one of the industrial important enzyme α‐galactosidase, as it has many potential application in hydrolyzing raffinose series of oligosaccharides. The hydrolyzed soymilk after processing by immobilized α‐galactosidase is free from flatus‐inducing factors like raffinose and stachyose. It can be used as an alternative means for cow's milk for lactose intolerance, particularly among individuals in developing countries. As chitosan used is from the crustacean waste from the crab shell, the production and utilization of chitosan provides an economical alternative means of crustacean shell waste disposal sought worldwide.

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“…This is probably due to optimal adsorption of the enzyme on the matrix surface at 250 μg/5 ml for MCM-41. Mansour and Dawoud (2003) suggested that the gradual decrease in the enzyme activity is probably due to hindrance between the adsorbed enzyme molecules on the matrix, at higher concentrations of enzyme.…”

Section: Effect Of the Variation Of The Tyrosinase Concentration On Imentioning

confidence: 98%

Tyrosinase-Immobilized MCM-41 for the Detection of Phenol

Mangrulkar

Yadav

Meshram

et al. 2011

Water Air Soil Pollut

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In the present investigation, we report the immobilization of the enzyme tyrosinase on mesoporous silica material, i.e. MCM-41 to serve as a tool for the detection of phenol. The enzyme immobilized onto the MCM-41 matrix has shown to retain its activity and is quite stable. The immobilization of enzyme has been discussed, and the various factors that affect the loading of enzyme onto MCM-41 were studied and optimized. The applicability of tyrosinase-immobilized MCM-41 was then demonstrated for the detection of phenol. The lowest detectable concentration of phenol by tyrosinaseimmobilized MCM-41 was observed to be 1 mg l −1 . The factors influencing the detection of phenol were then studied in detail.

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Immobilization of invertase on celite and on polyacrylamide by an absorption procedure

Cited by 30 publications

References 13 publications

Multienzymatic Sucrose Conversion into Fructose and Gluconic Acid through Fed-Batch and Membrane-Continuous Processes

Multienzymatic Sucrose Conversion into Fructose and Gluconic Acid through Fed-Batch and Membrane-Continuous Processes

Optimization of Immobilization Process on Crab Shell Chitosan and Its Application in Food Processing

Tyrosinase-Immobilized MCM-41 for the Detection of Phenol

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