Phytase from <i>Weissella halotolerans</i>: purification, partial characterisation and the effect of some metals

Demir, Yeliz; Kotan, Merve Şenol; Dikbaş, Neslihan; Beydemır, Şükrü

doi:10.1080/10942912.2017.1368547

Cited by 23 publications

(14 citation statements)

References 40 publications

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“…Phytase purification procedures were performed according to previous studies [4,13]. The phytase obtained at the end of the seventh day from L. plantarum was centrifuged at 24,000g for 30 Min.…”

Section: Phytase Purificationmentioning

confidence: 99%

Purification of the phytase enzyme fromLactobacillus plantarum: The effect on pansy growth and macro–micro element content

Karagöz

Demir

Kotan

et al. 2020

Biotech and App Biochem

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In the present study, the phytase enzyme was purified from Lactobacillus plantarum with a 3.08% recovery, 9.57-purification fold, and with a specific activity of 278.82 EU/mg protein. Then, the effects of the 5 EU and 10 EU purified phytase was determined on the plant growth, quality, the macro-micro nutrient content of pansy (Viola × wittrockiana), which is of great importance in ornamental plants industry. The research was established under greenhouse conditions with natural light in 2017. The pansy seeds were coated with phytase enzyme solution, sown in a peat environment, and transferred to pots at the seedling period. In general, the 5 EU and 10 EU applications increase plant height, the number of leaves per plant, the number of side branches per plant, and flower height parameters compared to control. Also, microand macronutrient values in soil and plant samples were examined. According to the results, the phytase application on pansy cultivation positively affected the properties and yielded high quality of plants.

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Section: Phytase Purificationmentioning

confidence: 99%

Purification of the phytase enzyme fromLactobacillus plantarum: The effect on pansy growth and macro–micro element content

Karagöz

Demir

Kotan

et al. 2020

Biotech and App Biochem

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“…However, although microbial phytases are used intensively in animal nutrition and have huge industrial implications, there has been no attention given to potential plant proteinaceous inhibitors of microbial phytases. So far, the inactivation of microbial phytases by metal cations has been mainly focused (Demir et al, 2017(Demir et al, , 2018. However, pathogens require phytase activity to utilize grain phytate-bound P, and plants require proteinaceous inhibitors of microbial phytases to protect themselves from pathogen invasion.…”

Section: Discussionmentioning

confidence: 99%

Barley Nepenthesin-Like Aspartic Protease HvNEP-1 Degrades Fusarium Phytase, Impairs Toxin Production, and Suppresses the Fungal Growth

et al. 2021

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Nepenthesins are categorized under the subfamily of the nepenthesin-like plant aspartic proteases (PAPs) that form a distinct group of atypical PAPs. This study describes the effect of nepenthesin 1 (HvNEP-1) protease from barley (Hordeum vulgare L.) on fungal histidine acid phosphatase (HAP) phytase activity. Signal peptide lacking HvNEP-1 was expressed in Pichia pastoris and biochemically characterized. Recombinant HvNEP-1 (rHvNEP-1) strongly inhibited the activity of Aspergillus and Fusarium phytases, which are enzymes that release inorganic phosphorous from phytic acid. Moreover, rHvNEP-1 suppressed in vitro fungal growth and strongly reduced the production of mycotoxin, 15-acetyldeoxynivalenol (15-ADON), from Fusarium graminearum. The quantitative PCR analysis of trichothecene biosynthesis genes (TRI) confirmed that rHvNEP-1 strongly repressed the expression of TRI4, TRI5, TRI6, and TRI12 in F. graminearum. The co-incubation of rHvNEP-1 with recombinant F. graminearum (rFgPHY1) and Fusarium culmorum (FcPHY1) phytases induced substantial degradation of both Fusarium phytases, indicating that HvNEP-1-mediated proteolysis of the fungal phytases contributes to the HvNEP-1-based suppression of Fusarium.

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“…Effect of metal ions and inhibitors on fungal phytase activity was investigated [ 22 , 35 , 81 ]. In the present study, the activity of phytase from P. adiposa decreased in the presence of Ca 2+ , Co 2+ , Cu 2+ , K + , Mg 2+ , Mn 2+ , Na + , and Zn 2+ at concentrations of 1 and 5 mM and increased in the presence of Fe 2+ .…”

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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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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Phytase from Weissella halotolerans: purification, partial characterisation and the effect of some metals

Cited by 23 publications

References 40 publications

Purification of the phytase enzyme fromLactobacillus plantarum: The effect on pansy growth and macro–micro element content

Purification of the phytase enzyme fromLactobacillus plantarum: The effect on pansy growth and macro–micro element content

Barley Nepenthesin-Like Aspartic Protease HvNEP-1 Degrades Fusarium Phytase, Impairs Toxin Production, and Suppresses the Fungal Growth

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

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