Engineering of thermostable phytase–xylanase for hydrolysis of complex biopolymers

Patel, Dharti Keyur; Patel, Kirankumar G.; Patel, Darshan H.; Dave, Gayatri

doi:10.1007/s13205-021-02936-z

Cited by 7 publications

(3 citation statements)

References 35 publications

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“…In pure citrus pectin (available commercially, PectaSol-C, curve A), the first step at 60 • C corresponds to the water molecules and some volatile compounds loss, which confirms a loss of 3.7% of the weight of the PectaSol-C sample. The next steps with three endothermic effects at 200 • C, 229 • C, and 882.7 • C are associated with pyrolytic decomposition, consisting of primary and secondary decarboxylation with an acid side group and carbon in the ring [38,[41][42][43]. The successive mass loss (87.4%) may lead to pectin residue formation.…”

Section: Mass Spectrometry (Esi-ms)mentioning

confidence: 99%

Structural Determination of Pectins by Spectroscopy Methods

et al. 2022

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Plant polysaccharides include pectins, which are responsible for an important role in plant physiology and are part of the plant cell wall. These compounds are known as gelling and stabilizing agents, which are widely used in the food industry. The scientific literature lacks precise information on the spectroscopy of apple pectin and citrus pectin. Therefore, the aim of this work was to test and compare the physicochemical properties of these compounds. The curves of FT-IR, NMR, ESI-MS, and thermogravimetric analysis (TGA) of pectin samples were measured and discussed. The analysis of the spectroscopic results confirms that the isolated pectins using various enzymes (xylanase and cellulase) have a structure similar to the commercially available pectin (PectaSol-C), with a noticeable change in morphology. These characteristics are helpful for further basic research and application.

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Section: Mass Spectrometry (Esi-ms)mentioning

confidence: 99%

Structural Determination of Pectins by Spectroscopy Methods

et al. 2022

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“…The animal feed industry requires enzymes with high thermostability and pH stability (Patel et al 2021).…”

Section: Effect Of Ph On Enzyme Activity and Stabilitymentioning

confidence: 99%

“…protein or protein-substrate interactions; hence, its presence may alter the microenvironment and in uence interaction between hydrophobic molecules in the enzyme structure, resulting in changes in enzyme conformation and in uence its active sites (de Oliveira Ornela and Guimarães 2019). PhyL from B. licheniformis with addition of Zn2+ showed increased activity, whereas Mg 2+ , Ca 2+ , and Mn 2+ signi cantly limited phytase activity(Patel et al 2021). Co 2+ , Cu 2+ , and Zn 2+ signi cantly reduced the activity of puri ed phytase from B. subtilis P6 by more than 50%, whereas EDTA had no effect on phytase activity(Trivedi et al 2022).…”

mentioning

confidence: 99%

Screening, expression, and characterization of recombinant phytase from Bacillus subtilis KM-BS for biodegradation of phytic acid in animal feeds

Ho,

Huynh,

Nguyen

et al. 2023

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Two extracellular phytases derived from Bacillus subtilis KM-BS were cultured at 37 and 55°C. These phytases were successfully expressed in Escherichia coli BL21 (DE3) cells and biochemically characterized for potential industrial applications. Recombinant PhyC-37 and PhyC-55 were shown to be catalytically active, with activities of 3.73 and 2.51 U/ml and specific activities of 4.12 and 1.43 U/mg, respectively. SDS-PAGE analysis indicated that the purified enzymes had a theoretical molecular weight of 58 kDa. Similar to other Bacillus phytases, the optimal temperature of the recombinant enzymes was 55°C. Purified PhyC-37 and PhyC-55 were optimally active at pH 7.0 and 5.0, respectively. They exhibited good stability at their optimal pH values and showed possible thermostability, retaining 46.22 and 50.05% of their activity after incubation for 360 min at 55°C. Addition of 1 mM of metal ions such as Na+, K+, Mg2+, Ca2+, Mn2+, Co2+, and Zn2+ stimulated PhyC-37 and PhyC-55, while enzyme activities were moderately to completely inhibited in the presence of Cu2+, SDS, EDTA, Triton X-100, and Tween-80. The Km and Vmax values of PhyC-37 were determined as 0.18 mM and 448.60 µmol/min, while for PhyC-55 the values were 0.19 mM and 355.60 µmol/min, respectively. Crude PhyC-37 and PhyC-55 also demonstrated remarkable rice bran digestion efficiency. Overall, findings highlighted the appealing features of these two purified phytase enzymes, which showed significant potential as candidates for application in the animal feed industry to mitigate environmental eutrophication.

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