Soy protein isolate for enzymes bio-conjugation

Wahba, Marwa I.

doi:10.1016/j.bcab.2022.102390

Cited by 6 publications

(20 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Noteworthy, a 25% GA (2.5 M) was adopted while preparing the SPI-GA-functionalized Car beads. Nonetheless, the quantity of GA attached to the SPI-GA-functionalized Car beads was analogous to that attached to the agar-Car disks which were functionalized with only a 3% GA (0.3 M) solution (Wahba 2022a ). Moreover, a substantial fraction of the attached GA entities would already be covalently linked to the iβGL.…”

Section: Resultsmentioning

confidence: 99%

“…The acquired Car beads were kept in the KCl solution for at least 2 h. Afterward, they were meticulously washed and soaked overnight within 10% (w/w) SPI suspension of pH 5. The beads were then meticulously washed and soaked within GA solution (25%, v/v) for 1 h (Wahba 2022a). Finally, the SPI-GA-functionalized Car beads were washed and put in the fridge in distilled water till loading them with βGL.…”

Section: Preparation Of the Spi-ga-functionalized Car Beadsmentioning

confidence: 99%

“…Soy-protein isolate (SPI)-GA-functionalized carrageenan (Car) beads were formerly reported as immobilizers for the industrial enzyme β - d -galactosidase (βGL) (Wahba 2022a ). These SPI-GA-functionalized Car immobilizers were proficient.…”

Section: Introductionmentioning

confidence: 99%

“…During the functionalization of such immobilizers Car beads were coated with an SPI sheath. Afterward, they were allowed to interact with GA (Wahba 2022a ). SPI is a protein; thus, it would present cationic and anionic entities whose abundance would be dictated by the adopted pH value.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Boosting the stability of β-galactosidase immobilized onto soy-protein isolate-glutaraldehyde-functionalized carrageenan beads

Wahba

2023

3 Biotech

Self Cite

View full text Add to dashboard Cite

Uncontrolled enzyme-immobilizer interactions were evident after immobilizing β-galactosidase onto soy-protein isolate-glutaraldehyde-functionalized carrageenan beads. Such interactions triggered shortcomings in the immobilized β-galactosidase (iβGL) thermal and storage stabilities. The thermal stability of the iβGL was somewhat lesser than that of the free βGL. Moreover, the iβGL suffered an initial sharp fall-off in its activity after storing it. Thus, approaches were adopted to prevent the occurrence of such uncontrolled enzyme-immobilizer interactions, and accordingly, boost the stability of the iβGL. These approaches involved neutralizing the covalently reactive GA entities via glycine and also altering the functionalizing GA concentrations. Nonetheless, no improvement was recorded in the iβGL thermal stability and this indicated that the uncontrolled enzyme-immobilizer interactions were not mediated via GA. Another approach was then attempted which involved treating the iβGL with lactose. The lactose-treated iβGL (LT-iβGL) presented superior thermal stability as was verified from its smaller kd and bigger t1/2 and D-values. The LT-iβGL t1/2 values were 5.60 and 3.53 fold higher than those presented by the free βGL at 62 and 65 °C, respectively. Moreover, the LT- iβGL presented loftier ΔG than did the free βGL. The storage stability of the LT- iβGL was also superior as it offered 100.41% of its commencing activity on its 43rd storage day. Thus, it could be concluded that lactose prevented the uncontrolled enzyme-immobilizer interactions. Finally, advantageous galacto-oligosaccharides (GOS) were prepared via the iβGL. The GOS were then analyzed with mass spectrometry, and it was shown that their degree of polymerization reached up to 7.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Preparation Of the Spi-ga-functionalized Car Beadsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Boosting the stability of β-galactosidase immobilized onto soy-protein isolate-glutaraldehyde-functionalized carrageenan beads

Wahba

2023

3 Biotech

Self Cite

View full text Add to dashboard Cite

show abstract

“…In case of Carr, a 2% Carr solution was obtained after stirring the Carr powder in distilled water within a 70 °C water-bath. A thin syringe needle was then exploited to drip the hot Carr solution into 3% KCl solution 18 . The attained Carr beads were kept in the gelling KCl solution for at least 18 h before scrupulously washing them.…”

Section: Methodsmentioning

confidence: 99%

Glutaraldehyde-pea protein grafted polysaccharide matrices for functioning as covalent immobilizers

Wahba

2023

Sci Rep

Self Cite

View full text Add to dashboard Cite

Three polysaccharide matrices (κ-Carrageenan (Carr), gellan gum, and agar) were grafted via glutaraldehyde (GA) and pea protein (PP). The grafted matrices covalently immobilized β-d-galactosidase (β-GL). Nonetheless, grafted Carr acquired the topmost amount of immobilized β-GL (iβ-GL). Thus, its grafting process was honed via Box-Behnken design and was further characterized via FTIR, EDX, and SEM. The optimal GA-PP-Carr grafting comprised processing Carr beads with 10% PP dispersion of pH 1 and 25% GA solution. The optimal GA-PP-Carr beads acquired 11.44 Ug−1 iβ-GL with 45.49% immobilization efficiency. Both free and GA-PP-Carr iβ-GLs manifested their topmost activity at the selfsame temperature and pH. Nonetheless, the β-GL Km and Vmax values were reduced following immobilization. The GA-PP-Carr iβ-GL manifested good operational stability. Moreover, its storage stability was incremented where 91.74% activity was offered after 35 storage days. The GA-PP-Carr iβ-GL was utilized to degrade lactose in whey permeate with 81.90% lactose degradation efficiency.

show abstract

A comprehensive review on genipin: an efficient natural cross-linker for biopolymers

Wahba

2024

Polym. Bull.

View full text Add to dashboard Cite

Cross-linkers are pivotal to meliorate the attributes of the biopolymers, which are exploited in the biomedical industries, and also those intended as packaging supplies. Genipin (GN) is an efficacious cross-linker. Moreover, being naturally procured, biodegradable and biocompatible makes it an auspicious candidate for the biomedical and food industries. Accordingly, we attempted to provide a comprehensive review on GN as an efficient cross-linker for biopolymers. Initially, we presented the chief botanical sources of GN. The GN extraction strategies, which adopted safe solvents, were then discussed while highlighting their realized yields. The proposed GN structures, its possible modes of action, and the factors affecting its interactions, such as pH, temperature, and GN concentration were also reviewed. Afterward, the GN applications that mainly involved cross-linking biopolymers and biopolymers containing materials were discussed. These included tissue engineering, wound dressings, drug delivery, and packaging applications. GN capability to activate biopolymers, such as chitosan and gelatin, into covalently reactive enzyme immobilizers was also discussed. Moreover, other important GN applications, such as exploiting it as a colorant for foods and textiles and incorporating it in altered biosensors, were discussed.

show abstract

Soy protein isolate for enzymes bio-conjugation

Cited by 6 publications

References 28 publications

Boosting the stability of β-galactosidase immobilized onto soy-protein isolate-glutaraldehyde-functionalized carrageenan beads

Boosting the stability of β-galactosidase immobilized onto soy-protein isolate-glutaraldehyde-functionalized carrageenan beads

Glutaraldehyde-pea protein grafted polysaccharide matrices for functioning as covalent immobilizers

A comprehensive review on genipin: an efficient natural cross-linker for biopolymers

Contact Info

Product

Resources

About