Dataset Information

Fungal phytases: from genes to applications.

ABSTRACT: Phytic acid stores 60-90% of the inorganic phosphorus in legumes, oil seeds, and cereals, making it inaccessible for metabolic processes in living systems. In addition, given its negative charge, phytic acid complexes with divalent cations, starch, and proteins. Inorganic phosphorous can be released from phytic acid upon the action of phytases. Phytases are phosphatases produced by animals, plants, and microorganisms, notably Aspergillus niger, and are employed as animal feed additive, in chemical industry and for ethanol production. Given the industrial relevance of phytases produced by filamentous fungi, this work discusses the functional characterization of fungal phytase-coding genes/proteins, highlighting the physicochemical parameters that govern the enzymatic activity, the development of phytase super-producing strains, and key features for industrial applications.

SUBMITTER: Correa TLR

PROVIDER: S-EPMC7455620 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature

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Fungal phytases: from genes to applications.

Corrêa Thamy Lívia Ribeiro TLR de Araújo Elza Fernandes EF

Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] 20200514 3

Phytic acid stores 60-90% of the inorganic phosphorus in legumes, oil seeds, and cereals, making it inaccessible for metabolic processes in living systems. In addition, given its negative charge, phytic acid complexes with divalent cations, starch, and proteins. Inorganic phosphorous can be released from phytic acid upon the action of phytases. Phytases are phosphatases produced by animals, plants, and microorganisms, notably Aspergillus niger, and are employed as animal feed additive, in chemic ...[more]

PMID: 32410091

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Project description:Phytases (myo-inositol hexakisphosphate phosphohydrolases) are found naturally in plants and microorganisms, particularly fungi. Interest in these enzymes has been stimulated by the fact that phytase supplements increase the availability of phosphorus in pig and poultry feed and thereby reduce environmental pollution due to excess phosphate excretion in areas where there is intensive livestock production. The wild-type phytases from six different fungi, Aspergillus niger, Aspergillus terreus, Aspergillus fumigatus, Emericella nidulans, Myceliophthora thermophila, and Talaromyces thermophilus, were overexpressed in either filamentous fungi or yeasts and purified, and their biophysical properties were compared with those of a phytase from Escherichia coli. All of the phytases examined are monomeric proteins. While E. coli phytase is a nonglycosylated enzyme, the glycosylation patterns of the fungal phytases proved to be highly variable, differing for individual phytases, for a given phytase produced in different expression systems, and for individual batches of a given phytase produced in a particular expression system. Whereas the extents of glycosylation were moderate when the fungal phytases were expressed in filamentous fungi, they were excessive when the phytases were expressed in yeasts. However, the different extents of glycosylation had no effect on the specific activity, the thermostability, or the refolding properties of individual phytases. When expressed in A. niger, several fungal phytases were susceptible to limited proteolysis by proteases present in the culture supernatant. N-terminal sequencing of the fragments revealed that cleavage invariably occurred at exposed loops on the surface of the molecule. Site-directed mutagenesis of A. fumigatus and E. nidulans phytases at the cleavage sites yielded mutants that were considerably more resistant to proteolytic attack. Therefore, engineering of exposed surface loops may be a strategy for improving phytase stability during feed processing and in the digestive tract.

Project description:A total of 420 day old chicks were divided into seven groups (5 replicates of 12 chicks/group) fed isoproteic and isoenergetic diets. The control group was fed diets containing 0.50%, 0.45% and 0.40% of non-phytic phosphorous (nPP) in starter (1-35), grower (37-56) and finisher (57-64 d) periods, respectively. The three intermediate nPP (IntnPP) groups were fed diets with 0.40%, 0.35% and 0.30% nPP according to the growth period and were submitted to three dietary treatments: unsupplemented; supplemented with 500 FTU/kg diet of an Aspergillus niger phytase (IntnPP_fp) and supplemented with 500 FTU/kg diet of an Escherichia coli phytase (IntnPP_bp). The three low nPP groups fed diets contained 0.30%, 0.25% and 0.20% nPP and were submitted to the same dietary treatments than IntnPP to obtain LnPP, LnPP_fp and LnPP_bp groups. IntnPP and LnPP groups had lower body weight gain and feed, crude protein (CP) and metabolizable energy (ME) intake (p < 0.05) than the control. Feed conversion ratio of IntnPP was more favorable (p < 0.01) than the LnPP group. CP and ME conversion ratios worsened (p < 0.01) in IntnPP and LnPP groups in comparison to the control. The nPP conversion ratio improved (p < 0.01) from the control to the LnPP group. Fungal phytase reduced (p < 0.05) feed, CP, ME and nPP intake than the bacterial one. IntnPP and LnPP diets had a lower digestibility of CP (p < 0.01) and CF (p = 0.01) than the control. IntnPP and LnPP groups showed a higher (p < 0.05) economic efficiency than the control. Blood total protein was the lowest (p < 0.05) in the LnPP group, the control group showed the lowest (p < 0.05) level of albumin and IntnPP group had the lowest (p < 0.01) globulin level. The use of bacterial phytase increased (p < 0.01) total protein and globulin and decreased (p < 0.05) the plasma cholesterol in comparison to fungal phytase. Decreasing nPP levels in colored slow-growing broilers diet negatively affects growth performance and the use of phytase can partly alleviate these negative effects, but the efficiency of different enzyme sources (bacterial or fungal) was tied to the dietary nPP levels.

Dataset Information

Fungal phytases: from genes to applications.

Publications

Fungal phytases: from genes to applications.

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