Evaluation of free and immobilized Aspergillus niger NRC1ami pectinase applicable in industrial processes

Esawy, Mona A.; Gamal, Amira A.; Kamel, Zeinat; Ismail, Abdel‐Mohsen S.; Abdelfattah, Ahmed

doi:10.1016/j.carbpol.2012.10.061

Cited by 66 publications

(52 citation statements)

References 31 publications

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“…Th is could be attributed to the fact that most enzyme protein successfully bound to the carrier leaving proteins, of any other origin, in the solution [16].…”

Section: Enzyme-specifi C Activity and Protein Content Determinationmentioning

confidence: 99%

Comparative studies of free and immobilized phytase, produced by Penicillium purpurogenu GE1, using grafted alginate/carrageenan beads

Awad¹,

Esawy²,

El-Gammal³

et al. 2015

Egypt Pharmaceut J

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“…Th is could be attributed to the fact that most enzyme protein successfully bound to the carrier leaving proteins, of any other origin, in the solution [16].…”

Section: Enzyme-specifi C Activity and Protein Content Determinationmentioning

confidence: 99%

Comparative studies of free and immobilized phytase, produced by Penicillium purpurogenu GE1, using grafted alginate/carrageenan beads

Awad¹,

Esawy²,

El-Gammal³

et al. 2015

Egypt Pharmaceut J

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“…Immobilization of pectinase using calcium alginate (Rehman et al 2013), entrapment in polyvinyl alcohol (PVA) sponge (Esawy et al 2013), immobilization in silicacoated magnetite nanoparticles (Mosafa et al 2014), and magnetic cornstarch microspheres were studied for juice production. It is showed that for immobilization stability, pH and temperature tolerance of enzyme were enhanced.…”

Section: Food Industrymentioning

confidence: 99%

Principles, techniques, and applications of biocatalyst immobilization for industrial application

Eş

Vieira

Amaral

2015

Appl Microbiol Biotechnol

328

109

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Immobilization is one of the most effective and powerful tools used in industry, which has been studied and improved since the last century. Various immobilization techniques and support materials have been used on both laboratory and industrial scale. Each immobilization technique is applicable for a specific production mostly depending on the cost and sensibility of process. Compared to free biocatalyst systems, immobilization techniques often offer better stability, increased activity and selectivity, higher resistance, improved separation and purification, reuse of enzymes, and consequently more efficient process. Recently, many reviews have been published about immobilization systems; however, most of them have focused on a specific application or not emphasized in details. This review focuses on most commonly used techniques in industry with many recent applications including using bioreactor systems for industrial production. It is also aimed to emphasize the advantages and disadvantages of the immobilization techniques and how these systems improve process productivity compared to non-immobilized systems.

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“…Beads of AGOCa-enzyme extract were kept in touch for different times (3,5,10,20,30 and 60 min) with calcium chloride solution (75 mM) and gelatin. After each established time, 0.5 g of sample was withdrawn and the enzyme activity was determined.…”

Section: Effect Of Contact Time Of the Beads With The Calcium Chloridmentioning

confidence: 99%

Synthesis of a hybrid polymer-inorganic biomimetic support incorporating in situ pectinase from Aspergillus niger ATCC 9642

Bustamante-Vargas

Mignoni

Oliveira

et al. 2015

Bioprocess Biosyst Eng

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The hybrid alginate/gelatin/calcium oxalate (AGOCa) support was successfully synthesized through the biomimetic mineralization method for immobilization in situ of a pectinolytic extract from Aspergillus niger ATCC 9642 via entrapment technique. The efficiency of immobilization reached 72.7%. Sodium oxalate buffer (100 mM, pH 5.5) was selected as adjuvant of the immobilization process by allowing the formation of a calcified shell around the calcium alginate capsule, significantly increasing the stability to storage, thermal and recycling of the enzymatic immobilized pectinolytic extract. The pH and temperature for maximum activity were from 5.0 to 6.0 and 60 to 80 °C, respectively. The new hybrid support can be a potential alternative to obtain immobilized pectinases with properties for advantageous industrial applications.

show abstract

Evaluation of free and immobilized Aspergillus niger NRC1ami pectinase applicable in industrial processes

Cited by 66 publications

References 31 publications

Comparative studies of free and immobilized phytase, produced by Penicillium purpurogenu GE1, using grafted alginate/carrageenan beads

Comparative studies of free and immobilized phytase, produced by Penicillium purpurogenu GE1, using grafted alginate/carrageenan beads

Principles, techniques, and applications of biocatalyst immobilization for industrial application

Synthesis of a hybrid polymer-inorganic biomimetic support incorporating in situ pectinase from Aspergillus niger ATCC 9642

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