RETRACTED: Thermostable phytase in feed and fuel industries

Vasudevan, Ushasree Mrudula; Jaiswal, Amit K.; Krishna, Sudhir; Pandey, Ashok

doi:10.1016/j.biortech.2019.01.065

Cited by 65 publications

(17 citation statements)

References 95 publications

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“…This treatment permits also the incorporation of ingredients in the feed to “lock” the feed mixture. Unfortunately, heat treatment could reduce phytase activity, and for this reason, it is important to select a thermostable enzyme ( Mrudula Vasudevan et al, 2019 ).…”

Section: Resultsmentioning

confidence: 99%

“…Phytate degradation in food is mediated mainly by fermentation processes led by phytate-degrading microorganisms ( De Angelis et al, 2003 ; Rizzello et al, 2010 ) or during the food processing by endogenous phytases present in food matrix ( Leenhardt et al, 2005 ). For the reasons described above, science community has focused attentions on phytate-degrading enzymes ( Lei et al, 2013 ; Mrudula Vasudevan et al, 2019 ; Pires et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

“…In particular, to work properly in the digestive tract, phytase needs to have a pH optimum between 3.5 and 5.5 and optimum of temperature in the range 37–40°C. Furthermore, phytases should actively work also at higher temperatures, required in feed production processes, as during pelletting and heat treatment to control Salmonella spoilage ( Mrudula Vasudevan et al, 2019 ). In addition, it would need to be resistant to protease activity and to show low sensitivity to ions ( Wyss et al, 1999 ).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Screening For Yeast Phytase Leads to the Identification of a New Cell-Bound and Secreted Activity in Cyberlindnera jadinii CJ2

Capusoni

Serra

Donzella

et al. 2021

Front. Bioeng. Biotechnol.

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Phytic acid is an anti-nutritional compound able to chelate proteins and ions. For this reason, the food industry is looking for a convenient method which allows its degradation. Phytases are a class of enzymes that catalyze the degradation of phytic acid and are used as additives in feed-related industrial processes. Due to their industrial importance, our goal was to identify new activities that exhibit best performances in terms of tolerance to high temperature and acidic pH. As a result of an initial screening on 21 yeast species, we focused our attention on phytases found in Cyberlindnera jadinii, Kluyveromyces marxianus, and Torulaspora delbrueckeii. In particular, C. jadinii showed the highest secreted and cell-bound activity, with optimum of temperature and pH at 50°C and 4.5, respectively. These characteristics suggest that this enzyme could be successfully used for feed as well as for food-related industrial applications.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Screening For Yeast Phytase Leads to the Identification of a New Cell-Bound and Secreted Activity in Cyberlindnera jadinii CJ2

Capusoni

Serra

Donzella

et al. 2021

Front. Bioeng. Biotechnol.

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“…Sitedirected mutagenesis, random mutation, molecular dynamic simulation, and protein glycosylation are methods of structural modification that are commonly employed when disulfide bonds, hydrogen bonds, ionic interaction and N/O-linked glycosylation are introduced in the phytases. Notably, this effectively improved their thermostability characteristics (Mullaney et al, 2010;Vasudevan et al, 2019). Mullaney et al (2010) removed disulfide bridge site-directed mutagenesis number 2 from A. ficuum 1 http://www.expasy.ch/cgi-bin/get-prodoc-entry?PDOC00538 FIGURE 3 | Multiple alignments of histidine acid phytase (HAPs) from genus Aspergillus.…”

Section: Crystal Structure and Protein Engineering Of Fungal Phytasesmentioning

confidence: 99%

Bioprocess for Production, Characteristics, and Biotechnological Applications of Fungal Phytases

et al. 2020

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Phytases are a group of enzymes that hydrolyze the phospho-monoester bonds of phytates. Phytates are one of the major forms of phosphorus found in plant tissues. Fungi are mainly used for phytase production. The production of fungal phytases has been achieved under three different fermentation methods including solid-state, semi-solid-state, and submerged fermentation. Agricultural residues and other waste materials have been used as substrates for the evaluation of enzyme production in the fermentation process. Nutrients, physical conditions such as pH and temperature, and protease resistance are important factors for increasing phytase production. Fungal phytases are considered monomeric proteins and generally possess a molecular weight of between 14 and 353 kDa. Fungal phytases display a broad substrate specificity with optimal pH and temperature ranges between 1.3 and 8.0 and 37-67 • C, respectively. The crystal structure of phytase has been studied in Aspergillus. Notably, thermostability engineering has been used to improve relevant enzyme properties. Furthermore, fungal phytases are widely used in food and animal feed additives to improve the efficiency of phosphorus intake and reduce the amount of phosphorus in the environment.

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“…Resistance to proteolytic degradation in the digestive tract and the high activity of phytase are additional advantages [12]. Therefore, the desired phytase should have stability against high temperature, acidic pH and proteases (pepsin and trypsin) [13,14]. So, to use phytase as an industrial enzyme, stability should be increased.…”

Section: Introductionmentioning

confidence: 99%

Integrative Structural and Computational Biology of Phytases for the Animal Feed Industry

et al. 2020

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Resistance to high temperature, acidic pH and proteolytic degradation during the pelleting process and in the digestive tract are important features of phytases as animal feed. The integration of insights from structural and in silico analyses into factors affecting thermostability, acid stability, proteolytic stability, catalytic efficiency and specific activity, as well as N-glycosylation, could improve the limitations of marginal stable biocatalysts with trade-offs between stability and activity. Synergistic mutations give additional benefits to single substitutions. Rigidifying the flexible loops or inter-molecular interactions by reinforcing non-bonded interactions or disulfide bonds, based on structural and roof mean square fluctuation (RMSF) analyses, are contributing factors to thermostability. Acid stability is normally achieved by targeting the vicinity residue at the active site or at the neighboring active site loop or the pocket edge adjacent to the active site. Extending the positively charged surface, altering protease cleavage sites and reducing the affinity of protease towards phytase are among the reported contributing factors to improving proteolytic stability. Remodeling the active site and removing steric hindrance could enhance phytase activity. N-glycosylation conferred improved thermostability, proteases degradation and pH activity. Hence, the integration of structural and computational biology paves the way to phytase tailoring to overcome the limitations of marginally stable phytases to be used in animal feeds.

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RETRACTED: Thermostable phytase in feed and fuel industries

Cited by 65 publications

References 95 publications

Screening For Yeast Phytase Leads to the Identification of a New Cell-Bound and Secreted Activity in Cyberlindnera jadinii CJ2

Screening For Yeast Phytase Leads to the Identification of a New Cell-Bound and Secreted Activity in Cyberlindnera jadinii CJ2

Bioprocess for Production, Characteristics, and Biotechnological Applications of Fungal Phytases

Integrative Structural and Computational Biology of Phytases for the Animal Feed Industry

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