Preparation and characterization of a green nano-support for the covalent immobilization of glucoamylase from Neurospora sitophila

Syed, Fatima; Ali, Khurshid; Asad, Muhammad Javaid; Fraz, Muhammad Gul; Khan, Zahid; Imran, Muhammad; Taj, Raheela; Ahmad, Aftab

doi:10.1016/j.jphotobiol.2016.07.002

Cited by 13 publications

(4 citation statements)

References 43 publications

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“…Similarly, Lactoperoxidase immobilized AgNPs were synthesized immediately upon addition of a chemical reductant NaBH 4 in the reaction mixture of AgNO 3 and lactoperoxidase, where the enzyme acted as the capping reagent (Sheikh et al 2018). Syed et al (2016) reported green synthesis of AgNPs via Fagonia indica plant material and used them as immobilization support to immobilize glucoamylase from Neurospora sitophila using covalent immobilization linker EDC (1-(3 (dimethylamino) propyl) 3-ethylcarbodiimidehydrochloride) coupling reaction.…”

Section: Enzyme-nanocomplex Recyclingmentioning

confidence: 99%

Characterization of biogenically synthesized silver nanoparticles for therapeutic applications and enzyme nanocomplex generation

2020

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The present study describes green synthesis of silver nanoparticles (AgNPs) and inulin hydrolyzing enzyme nanocomplexes (ENC) using Azadirachta indica (Ai) and Punica granatum (Pg) leaf extracts. Surface topology and physico-chemical characteristics of AgNPs were studied using surface plasmon resonance (SPR), FTIR, SEM, AFM and EDX analyses. Particle size analysis using dynamic light scattering and AFM studies revealed that Ai-AgNPs (76.4 nm) were spherical in shape having central bigger nano-regime with smaller surroundings while Pg-AgNPs (72.1 nm) and ENCs (Inulinase-Pg-AgNPs ~ 145 nm) were spherical particles having smooth surfaces. Pg-AgNPs exhibited significant photocatalysis of a thiazine dye, methylene blue. Both Ai-and Pg-AgNPs showed selective antibacterial action by inhibiting pathogenic Bacillus cereus, while the probiotic Lactobacillus strains remained unaffected. Ai-AgNPs showed potential anti-biofilm effect (30% viability) on B. cereus biofilms. Pg-AgNPs showed anti-cancer effect against human colon cancer cell lines (Caco-2) resulting in 40% cell death in 48 h. Enzymes (inulinase, L-asparaginase and glucose oxidase) were successfully immobilized onto nanoparticles together with the biogenic synthesis of AgNPs and recyclability of the Inulinase-Pg-AgNPs complex was demonstrated. The study elaborates characteristics of green synthesized nanoparticles and their potential applications as anti-cancer, antibacterial and antioxidant nano drugs that could be used in food and nutraceutical industries. Enzyme immobilization on AgNPs without any toxic cross-linker opens up newer possibilites in enzyme-nanocomplex research.

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Section: Enzyme-nanocomplex Recyclingmentioning

confidence: 99%

Characterization of biogenically synthesized silver nanoparticles for therapeutic applications and enzyme nanocomplex generation

2020

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“…Sojitra et al reported that pectinase immobilized onto chitosan magnetic nanoparticles retained 85% of initial activity after seven successive cycles of reuse (Sojitra, Nadar, & Rathod, 2017). It was reported that glucoamylase immobilized onto biogenic silver nanoparticles retained 70% and 49% of initial activity after 4 and 8 times of recycling, respectively (Syed et al, 2016).…”

Section: Reusabilitymentioning

confidence: 99%

Co-immobilization of pectinase and glucoamylase onto sodium aliginate/graphene oxide composite beads and its application in the preparation of pumpkin-hawthorn juice

et al. 2018

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Co‐immobilization of pectinase and glucoamylase onto sodium alginate/graphene oxide beads was achieved by N,N′‐dicyclohexylcarbodiimide/N‐hydroxysuccinimide as activating agent. The co‐immobilized pectinase‐glucoamylase (I‐PG) prepared under optimal conditions (pH 4.0, 40°C and 35 min) possessed pectinase activity of 1,227.5 ± 36.5U/g and glucoamylase activity of 1,027.2 ± 29.2U/g, with activity recovery of 73.8% and 85.2%, respectively. Both pectinase and glucoamylase in I‐PG possessed wider pH tolerance and superior thermal stability to those of their free counterparts. Reusability studies indicated that both enzymes in I‐PG retained over 60% of initial activity after six times of reuse. Conditions for the hydrolysis of the pumpkin–hawthorn compound juice by I‐PG were optimized using orthogonal experiments. After treatment with I‐PG, light transmittance, soluble solids, and reducing sugar content in the resulting juice increased significantly, whereas soluble protein and pectin content decreased appreciably. Therefore, the use of I‐PG provided an effective and feasible method for improving quality of the pumpkin–hawthorn juice. Practical applications In order to overcome the drawbacks of using free pectinase and glucoamylase, an effective method for the co‐immobilization of these two enzymes onto sodium alginate/graphene oxide beads was developed. The co‐immobilized pectinase/glucoamylase developed in this study could be applied in the clarification of juice rich in pectin and starch.

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“…In addition, the immobilized enzyme maintained about 60% activity after 10-repeated uses [95]. Syed et al [96] covalently immobilized glucoamylase from Neurospora sitophila on the phytochemicals coated AgNPs via EDC (1-(3-(dimethylamino) propyl) 3-ethylcarbodiimidehydrochloride) coupling reaction. The immobilized enzyme showed higher pH and thermal stabilities, K m and V max values compared to soluble enzyme.…”

Section: α-Amylasementioning

confidence: 99%

“…Glucoamylases immobilized on/ in nanosupports retained remarkably high stability against the inactivation mediated by pH, heat, inhibitors, products, and storage as compared to soluble enzyme. Such immobilized enzyme preparations were found highly stable on prolonged use in the reactors and on repeated uses in batch processes [92][93][94][95][96].…”

Section: α-Amylasementioning

confidence: 99%

Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review

Husain¹

2017

Biocatalysis

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Numerous types of nanoparticles and nanocomposites have successfully been employed for the immobilization and stabilization of amylolytic enzymes; α-amylases, β-amylases, glucoamylases and pullulanases. Nano-support immobilized amylolytic enzymes retained very high activity and yield of immobilization. The immobilization of these enzymes, particularly α-amylases and pullulanases, to the nanosupports is helpful in minimizing the problem of steric hindrances during binding of substrate to the active site of the enzyme. The majority of nano-support immobilized amylolytic enzymes exhibited very high resistance to inactivation induced by different kinds of physical and chemical denaturants and these immobilized enzyme preparations maintained very high activity on their repeated and continuous uses. Amylolytic enzymes immobilized on nano-supports have successfully been applied in food, fuel, textile, paper and pulp, detergent, environmental, medical, and analytical fields.

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Preparation and characterization of a green nano-support for the covalent immobilization of glucoamylase from Neurospora sitophila

Cited by 13 publications

References 43 publications

Characterization of biogenically synthesized silver nanoparticles for therapeutic applications and enzyme nanocomplex generation

Characterization of biogenically synthesized silver nanoparticles for therapeutic applications and enzyme nanocomplex generation

Co-immobilization of pectinase and glucoamylase onto sodium aliginate/graphene oxide composite beads and its application in the preparation of pumpkin-hawthorn juice

Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review

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