Modification of zeolite with metallic ions improves the immobilization of phytase

Lopes, Marina Momesso; Coutinho, Thamara Carvalho; Farinas, Cristiane S.

doi:10.1016/j.bcab.2021.102137

Cited by 7 publications

(2 citation statements)

References 71 publications

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“…The CLPA was then kept at room temperature. For a new reaction cycle, the CLPA was then resuspended in fresh aliquots of substrates, and in the first cycle, CLPA was considered to have 100% relative activity 22 …”

Section: Methodsmentioning

confidence: 99%

Dephytinization of wheat and rice bran by cross‐linked enzyme aggregates of Mucor indicus phytase: a viable prospect for food and feed industries

Venkataraman

Vaidyanathan

2022

J Sci Food Agric

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BACKGROUND Novel feeds for improved feed intake and for enhanced nutrient bioavailability have recently attracted attention. Insoluble dietary fibers, especially rice and wheat bran, have generated much interest due to their nutritional value. Incorporating insoluble dietary fiber into diets could be a viable way to maximize the feed conversion ratio. RESULTS Cross‐linked phytase aggregates (CLPA) were synthesized by precipitating enzymes followed by cross‐linking with 5 mmol L−1 glutaraldehyde, yielding 88.24 (U g−1) of enzyme load without the assistance of a proteic feeder. The epitome of the study is the dephosphorylation of wheat bran and rice bran by varying pH, enzyme concentration, and temperature. The highest inorganic phosphorus liberation by 150 U L‐‐1of free phytase was 23.72 (wheat bran) and 48.08 mg g−1 (rice bran) after 12 h of incubation. Furthermore, 150 U L‐1 of CLPA liberated 28.72 (wheat bran) and 52.08 mg g−1 (rice bran) of inorganic phosphorus with an incubation time of 12 h. CONCLUSION Thermostable free phytase was insolubilized to dephosphorylate the agro‐residue, namely, wheat bran and rice bran, to reduce the anti‐nutritional factor (the phytate content) of these insoluble dietary fibers. © 2022 Society of Chemical Industry.

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Section: Methodsmentioning

confidence: 99%

Dephytinization of wheat and rice bran by cross‐linked enzyme aggregates of Mucor indicus phytase: a viable prospect for food and feed industries

Venkataraman

Vaidyanathan

2022

J Sci Food Agric

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“…In particular, insertion of transition metal species in porous materials such as zeolites by either impregnation or ion exchange results in novel environment-friendly [8] or catalyst materials [9,10] such as the ones used in organic-chemistry processes (e.g., methane-to-methanol conversion [11], ethylene oligomerization [12,13], l-butene dimerization [14] acetylene hydrogenation [15], phytase immobilization [16]). In addition, zeolites incorporating transition metal ions are key precursors of nanocomposites containing ferromagnetic nanoparticles of transition metals such as Fe 0 , Ni 0 , Co 0 obtained by suitable thermal treatments.…”

Section: Introductionmentioning

confidence: 99%

Magnetic clustering of weakly interacting Ni-ions in Ni-exchanged zeolites

Barrera

Allia

Tiberto

et al. 2022

Microporous and Mesoporous Materials

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Cross-linked phytase aggregates for improved phytate degradation at low pH in animal feed

Henninger

Hoferer

Ochsenreither

et al. 2023

Eur Food Res Technol

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Phytases are widely used food and feed enzymes to improve phosphate availability and reduce anti-nutritional factors. Despite the benefits, enzyme usage is restricted by the harsh conditions in a gastrointestinal tract (pH 2–6) and feed pelleting conditions at high temperatures (60–90 °C). The commercially available phytase Quantum® Blue has been immobilized as CLEAs using glutardialdehyde and soy protein resulting in a residual activity of 33%. The influence of the precipitating agent, precipitant concentration, cross-linker concentration and cross-linking time, sodium borohydride as well as the proteic feeders gluten, soy protein and bovine serum albumin (BSA) has been optimized. The best conditions were 90% (v/v) ethyl lactate as precipitating reagent, 100 mM glutardialdehyde and a soy protein concentration of 227 mg/L with a cross-linking time of 1 h. The intrinsically stable phytase remained its high thermal stability and temperature optimum. The phytase-CLEA achieved a 425% increase of residual activity under harsh acidic conditions between pH 2.2 and 3.5 compared to the free enzyme. The free and immobilized phytase were deployed in an in vitro assay simulating the acidic conditions in the gizzard of poultry at pH 2. The hydrolysis of phytate was monitored using a novel high-performance thin-layer chromatography (HPTLC) analysis and DAD scanner to study the InsPx fingerprint. All lower inositol phosphate pools (InsP1–InsP6) and free phosphate were separated and analyzed. The phytase-CLEA efficiently released 80% of the total phosphate within 180 min, whereas the free enzyme only released 6% in the same time under the same conditions.

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Modification of zeolite with metallic ions improves the immobilization of phytase

Cited by 7 publications

References 71 publications

Dephytinization of wheat and rice bran by cross‐linked enzyme aggregates of Mucor indicus phytase: a viable prospect for food and feed industries

Dephytinization of wheat and rice bran by cross‐linked enzyme aggregates of Mucor indicus phytase: a viable prospect for food and feed industries

Magnetic clustering of weakly interacting Ni-ions in Ni-exchanged zeolites

Cross-linked phytase aggregates for improved phytate degradation at low pH in animal feed

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