Online citations, reference lists, and bibliographies.

Whey Protein Isolate For The Preparation Of Covalent Immobilization Beads

Marwa I. Wahba, Tarik N. Soliman
Published 2018 · Chemistry
Cite This
Download PDF
Analyze on Scholarcy
Share
Abstract Whey protein isolate (WPI) was employed, for the first time, to activate carrageenan (Car) beads for the covalent immobilization of the Aspergillus oryzae β-D-galactosidase (β-gal). These Car beads were subjected to a WPI treatment step followed by a glutaraldehyde (GA) treatment step in order to enable such covalent immobilization. The WPI treatment was optimized via the Box-Behnken Design (BBD). The BBD anticipated that treating the Car beads with a 2.36% WPI solution of pH 5.25 for 7.04 h would allow for the attainment of an immobilized β-gal's activity recovery percent of 34.43%. A verification experiment was accomplished while employing the abovementioned conditions and an immobilized β-gal's activity recovery percent of 34.80 ± 1.11% was attained. It was also shown that the immobilization of β-gal onto the GA-WPI treated Car beads did not alter the enzyme's optimum temperature or optimum pH. Moreover, a reusability study was conducted and 93.84 ± 0.72% of the immobilized β-gal's initial observed activity was preserved during the 13th reusability cycle.
This paper references
10.1016/j.foodchem.2012.03.055
Optimisation of immobilisation conditions for chick pea β-galactosidase (CpGAL) to alkylamine glass using response surface methodology and its applications in lactose hydrolysis.
Devesh Kishore (2012)
10.1007/s13233-017-5123-8
Agar-carrageenan hydrogel blend as a carrier for the covalent immobilization of β-D-galactosidase
Marwa I. Wahba (2017)
10.1002/term.1683
Chondrogenic potential of injectable κ-carrageenan hydrogel with encapsulated adipose stem cells for cartilage tissue-engineering applications.
Elena Geta Popa (2015)
10.1016/j.enzmictec.2010.10.003
Control of protein immobilization: coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance.
Keven Hernandez (2011)
10.1016/j.foodchem.2014.10.076
Whey protein coating increases bilayer rigidity and stability of liposomes in food-like matrices.
Monika Frenzel (2015)
10.1016/j.ijbiomac.2016.06.044
Treated calcium pectinate beads for the covalent immobilization of β-d-galactosidase.
Marwa I. Wahba (2016)
10.1155/2014/163987
Immobilization of Aspergillus oryzae   β-Galactosidase on Cellulose Acetate-Polymethylmethacrylate Membrane and Its Application in Hydrolysis of Lactose from Milk and Whey
Shakeel Ahmed Ansari (2014)
10.1016/J.PROCBIO.2017.09.020
A new heterofunctional amino-vinyl sulfone support to immobilize enzymes: Application to the stabilization of β-galactosidase from Aspergillus oryzae
Hadjer Zaak (2018)
10.1021/acs.jpcc.5b09606
pH-Dependent Selective Protein Adsorption into Mesoporous Silica
Sebastian T. Moerz (2015)
10.3390/molecules190914139
Inorganic Materials as Supports for Covalent Enzyme Immobilization: Methods and Mechanisms
Paolo Zucca (2014)
10.1016/j.ijbiomac.2011.03.011
Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism.
Qayyum Husain (2011)
10.1590/S0104-66322012000200010
SYNTHESIS OF A BIOCOPOLYMER CARRAGEENAN-g-POLY(AAm-co-IA)/ MONTMORILONITE SUPERABSORBENT HYDROGEL COMPOSITE
Mohammad Sadeghi (2012)
10.1002/tcr.201600007
Chemical Modification in the Design of Immobilized Enzyme Biocatalysts: Drawbacks and Opportunities.
Nazzoly Rueda (2016)
10.1039/C3RA45991H
Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization
Oveimar Barbosa (2014)
10.1039/c2cs35231a
Modifying enzyme activity and selectivity by immobilization.
Rafael C Rodrigues (2013)
10.3390/molecules19078995
Immobilization as a Strategy for Improving Enzyme Properties-Application to Oxidoreductases
Urszula Guzik (2014)
10.1002/app.30535
Covalent Immobilization of β-Galactosidase on Carrageenan Coated with Chitosan
Magdy Elnashar (2009)
10.1590/S1516-89132011000600002
Galactans: an overview of their most important sourcing and applications as natural polysaccharides
Cédric Delattre (2011)
10.1016/J.FOODHYD.2014.12.027
Characterising the secondary structure changes occurring in high density systems of BLG dissolved in aqueous pH 3 buffer
Jc Ioannou (2015)
10.4061/2010/473137
Potential Applications of Immobilized β-Galactosidase in Food Processing Industries
Parmjit S. Panesar (2010)
10.1002/CCTC.201500310
Importance of the Support Properties for Immobilization or Purification of Enzymes
Jose C.S. dos Santos (2015)
10.4236/JBNB.2010.11008
Review Article: Immobilized Molecules Using Biomaterials and Nanobiotechnology
Magdy Elnashar (2010)
10.1089/ten.TEB.2009.0639
Controlling the porosity and microarchitecture of hydrogels for tissue engineering.
Nasim Annabi (2010)
10.1007/s00396-015-3754-x
Characterization of protein adsorption onto silica nanoparticles: influence of pH and ionic strength
Jens Meissner (2015)
10.2478/v10026-011-0043-4
Immobilization of Aspergillus oryzae β galactosidase on concanavalin A-layered calcium alginate-cellulose beads and its application in lactose hydrolysis in continuous spiral bed reactors
Shakeel Ahmed Ansari (2011)
10.1021/la053528w
Electrostatically driven protein aggregation: beta-lactoglobulin at low ionic strength.
Pinaki R. Majhi (2006)
10.1016/j.jdermsci.2009.06.016
In vitro impact of a whey protein isolate (WPI) and collagen hydrolysates (CHs) on B16F10 melanoma cells proliferation.
Gilson Araújo Castro (2009)
10.1016/j.biotechadv.2015.07.002
Cheese whey: A potential resource to transform into bioprotein, functional/nutritional proteins and bioactive peptides.
Jay Shankar Singh Yadav (2015)
10.1021/la402729g
pH effects on the molecular structure of β-lactoglobulin modified air-water interfaces and its impact on foam rheology.
Kathrin Engelhardt (2013)
10.1016/j.enzmictec.2007.01.018
Improvement of enzyme activity, stability and selectivity via immobilization techniques
César Mateo (2007)
10.1007/s12010-008-8453-3
Lactose Hydrolysis by β-Galactosidase Covalently Immobilized to Thermally Stable Biopolymers
Magdy Elnashar (2009)
10.1016/J.MOLCATB.2011.04.008
Effect of the immobilization protocol on the properties of lipase B from Candida antarctica in organic media: Enantiospecifc production of atenolol acetate
Oveimar Barbosa (2011)
10.3390/CATAL7090250
Exploiting the Versatility of Aminated Supports Activated with Glutaraldehyde to Immobilize β-galactosidase from Aspergillus oryzae
Hadjer Zaak (2017)
10.1016/j.ijbiomac.2017.07.102
Porous chitosan beads of superior mechanical properties for the covalent immobilization of enzymes.
Marwa I. Wahba (2017)
10.1016/J.MOLCATB.2014.01.012
Nylon 6 film and nanofiber carriers: Preparation and laccase immobilization performance
Enrico Fatarella (2014)
10.1111/j.1472-765X.2012.03247.x
Whey protein coating bead improves the survival of the probiotic Lactobacillus rhamnosus CRL 1505 to low pH.
Carla Luciana Gerez (2012)
10.2144/04375RV01
Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking.
Isabelle Migneault (2004)
10.1002/APP.40295
Application of Plackett-Burman Screening Design to the Modeling of Grafted Alginate-Carrageenan Beads for the Immobilization of Penicillin G Acylase
Magdy Elnashar (2014)



This paper is referenced by
Semantic Scholar Logo Some data provided by SemanticScholar