Purification and characterization of an alkalistable phytase produced by Rhizopus microsporus var. microsporus in submerged fermentation

Ornela, Pedro Henrique de Oliveira; Guimarães, Luís Henrique Souza

doi:10.1016/j.procbio.2019.03.015

Cited by 16 publications

(5 citation statements)

References 40 publications

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“…thermophile and [ 48 ] Rhizopus microsporus var. microsporus [ 79 ], and R. pusillus [ 80 ] were optimally active at temperatures of 60, 65, and 70 °C, respectively. Furthermore, pH value had a significant effect on the phytase activity of P. adiposa .…”

Section: Discussionmentioning

confidence: 99%

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Bioprocessing of Agricultural Residues as Substrates and Optimal Conditions for Phytase Production of Chestnut Mushroom, Pholiota adiposa, in Solid State Fermentation

Jatuwong

Kumla

Suwannarach

et al. 2020

JoF

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Phytase is an enzyme that breaks down phytates to release phosphorus in an available form. This enzyme plays an important role in animals, especially monogastric animals. It serves to improve phytate digestion along with phosphorus absorption, which are required for optimal growth performance and health. In this study, five mushroom species (Amauroderma rugosum SDBR-CMU-A83, Ganoderma mastoporum SDBR-CMU-NK0244, Marusmius sp.1 SDBR-CMU-NK0215, Pholiota adiposa SDBR-CMU-R32 and Piptoporellus triqueter SDBR-CMU-P234) out of 27 mushroom species displayed positive phytase production by agar plate assay. Consequently, these five mushroom species were selected for determination of their potential ability to produce phytase under solid-state fermentation using five agricultural residues (coffee parchment, oil palm empty fruit bunches, rice bran, sawdust, and water hyacinth) as substrates. The highest yield of phytase production (17.02 ± 0.92 units/gram dry substrate) was obtained after one week of fermentation. Optimization for phytase production was determined by statistical approaches using a Plackett–Burman design to screen ten parameters of relevant substrate components. Two significant parameters, the amount of water hyacinth and the moisture content, were found to affect the production process of phytase. Furthermore, the optimal temperature, pH value, and fermentation period were evaluated. The results indicated that the highest degree of phytase production at 53.66 ± 1.68 units/gram dry substrate (3.15-fold increase) was obtained in water hyacinth containing 85% moisture content by addition with a suitable basal liquid medium at a pH value of 6.5 after being incubated at 30 °C for seven days. The crude phytase of P. adiposa was precipitated and the precipitated extract was then used to determine partial characterizations. The precipitated extract displayed high activities after exposure to conditions of 42 °C and pH 5.0. Furthermore, Fe2+ enhanced phytase activity and precipitated extract displayed the best stability at a pH value of 8.0 and a temperature of 4 °C.

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Section: Discussionmentioning

confidence: 99%

“…Nevertheless, pH values of 7.0 (neutral condition) and 9.5 (basic condition) were found to be optimally active for phytase obtained from A. flavus ITCC 6720 [ 71 ] and R. microsporus var. microsporus [ 79 ], respectively.…”

Section: Discussionmentioning

confidence: 99%

Bioprocessing of Agricultural Residues as Substrates and Optimal Conditions for Phytase Production of Chestnut Mushroom, Pholiota adiposa, in Solid State Fermentation

Jatuwong

Kumla

Suwannarach

et al. 2020

JoF

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“…Phytases are phosphatases that hydrolyze phytic acid preferentially into inositol and P i [50], whereas acid phosphatases hydrolyze phosphomonoester and amides substrates, thereby transforming organic phosphate into a soluble inorganic form [57]. Phytase activity has been observed in several beneficial fungi, including Rhizopus microsporus [58], Funneliformis mosseae, Claroideoglomus etunicatum [49], and Trichoderma spp. [51].…”

Section: T Atroviride Secretes Enzymes Involved In Oxidative Stress Response Cell Wall Degradation Hydrolysis Of Organic Phosphate Sourcementioning

confidence: 99%

Secretome Analysis of Arabidopsis–Trichoderma atroviride Interaction Unveils New Roles for the Plant Glutamate:Glyoxylate Aminotransferase GGAT1 in Plant Growth Induced by the Fungus and Resistance against Botrytis cinerea

González-López

Jijón-Moreno

Dautt-Castro

et al. 2021

IJMS

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The establishment of plant–fungus mutualistic interaction requires bidirectional molecular crosstalk. Therefore, the analysis of the interacting organisms secretomes would help to understand how such relationships are established. Here, a gel-free shotgun proteomics approach was used to identify the secreted proteins of the plant Arabidopsis thaliana and the mutualistic fungus Trichoderma atroviride during their interaction. A total of 126 proteins of Arabidopsis and 1027 of T. atroviride were identified. Among them, 118 and 780 were differentially modulated, respectively. Bioinformatic analysis unveiled that both organisms’ secretomes were enriched with enzymes. In T. atroviride, glycosidases, aspartic endopeptidases, and dehydrogenases increased in response to Arabidopsis. Additionally, amidases, protein-serine/threonine kinases, and hydro-lyases showed decreased levels. Furthermore, peroxidases, cysteine endopeptidases, and enzymes related to the catabolism of secondary metabolites increased in the plant secretome. In contrast, pathogenesis-related proteins and protease inhibitors decreased in response to the fungus. Notably, the glutamate:glyoxylate aminotransferase GGAT1 was secreted by Arabidopsis during its interaction with T. atroviride. Our study showed that GGAT1 is partially required for plant growth stimulation and on the induction of the plant systemic resistance by T. atroviride. Additionally, GGAT1 seems to participate in the negative regulation of the plant systemic resistance against B. cinerea through a mechanism involving H2O2 production.

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“…Such enzymes are responsible for mineralization of organic phosphate, once the level of free inorganic phosphate becomes low in the soil. 1 Phytases (myo-inositol hexakisphosphate phosphohydrolases) are a special class of acid phosphatases that catalyze the hydrolysis of phytate to less phosphorylated myo-inositol derivatives (in some cases to free myoinositol) and releasing of inorganic phosphate. 2 These enzymes act to hydrolyze phytic acid, the main form of the accumulated phosphorus in most of cereal oil seeds, grains, and plants, 1 to release inorganic phosphate.…”

Section: Introductionmentioning

confidence: 99%

“…5 Additionally, the biochemical categorization of enzymes is an imperative stage for their efficient exploitation in various biotechnological applications. 1 The present study aims to purify and characterize the phytase enzyme produced by an isolated fungal strain, and study its application in cereal dephytinization.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Phytase Enzyme Extracted from Aspergillus niger SF58 and its Application in Cereal Dephytinization

2021

TJNPR

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Phytases are the group of enzymes that catalyze phytate hydrolysis and release a utilizable form of inorganic phosphorus. So, they are used to improve the nutritive value of animal feed. The current study aims to purify, characterize the phytase enzyme, and to study its application in cereal dephytinization. Molecular identification of the fungal isolate was achieved using the 18S rRNA and phytase activity was determined using phytic acid as substrate. Phytase from Aspergillus niger SF58 was purified using dialysis and Sephadex G 100 column chromatography to get enzyme recovery and purification fold of 72.74% and 2.303, respectively. The purity of purified phytase was confirmed through SDS-PAGE technique which showed a one protein band corresponding to phytase activity at 22 kDa. The optimum reaction time for phytase activity was revealed to be 15 min, whereas the optimal temperature and pH values were found to be 60 o C and pH 5.5. The purified enzyme was able to retain 46.93% of its initial activity after 4 months of storage at 4 o C. Metal ions (Co 2+ , Cu 2+ , Mn 2+ , Fe 2+ , Zn +2) acted as activators for the purified phytase, whereas Mg 2+ , Ni 2+ and Al 3+ served as inhibitors. The purified phytase showed the highest substrate specificity toward wheat bran, followed by the wheat flour, soybean , and corn-flower, respectively. The use of Aspergillus niger SF58 phytase in dephytinization of wheat bran and soybean indicated the possibility of applying the enzyme to increase the nutritional values of feed and food additives.

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Purification and characterization of an alkalistable phytase produced by Rhizopus microsporus var. microsporus in submerged fermentation

Cited by 16 publications

References 40 publications

Bioprocessing of Agricultural Residues as Substrates and Optimal Conditions for Phytase Production of Chestnut Mushroom, Pholiota adiposa, in Solid State Fermentation

Bioprocessing of Agricultural Residues as Substrates and Optimal Conditions for Phytase Production of Chestnut Mushroom, Pholiota adiposa, in Solid State Fermentation

Secretome Analysis of Arabidopsis–Trichoderma atroviride Interaction Unveils New Roles for the Plant Glutamate:Glyoxylate Aminotransferase GGAT1 in Plant Growth Induced by the Fungus and Resistance against Botrytis cinerea

Purification and Characterization of Phytase Enzyme Extracted from Aspergillus niger SF58 and its Application in Cereal Dephytinization

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