One-step purification and immobilization of His-tagged rhamnosidase for naringin hydrolysis

Puri, Munish; Kaur, Aneet; Singh, Ram Sarup; Schwarz, Wolfgang H.; Kaur, Amrit Pal

doi:10.1016/j.procbio.2009.11.001

Cited by 23 publications

(27 citation statements)

References 34 publications

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“…Naringin hydrolysis was estimated with minor modification to the Davis method [12]. After fermentation, the biomass was harvested by centrifugation (3000 × g for 10 min at 4 • C) and supernatant was analyzed for enzyme activity.…”

Section: Enzyme and Protein Assaymentioning

confidence: 99%

“…To optimize the naringin concentration, kinnow peel powder extracts (1-7%, w/v) were prepared by taking in 100 ml distilled water under shaking at 100 rpm, boiling (90 • C) for 5 and 10 min and cold conditions. Kinnow peel extracts filtered through double layered muslin cloth were characterized for total naringin content as per a modified Davis method [12]. All the results show average of three experiments.…”

Section: Naringin Recovery From Kinnow Peelmentioning

confidence: 99%

“…The plasmid pET21d-ramA with an N-terminal His-tag was constructed and transformed into E. coli BL21 to produce soluble ␣-l-rhamnosidase [12]. The recombinant enzyme adsorbed on Ni 2+ -NTA supports was eluted by increasing the concentration of the imidazole to 200 mM.…”

Section: Purification Of Enzymementioning

confidence: 99%

“…␣-l-Rhamnosidase (EC 3.2.1.40) catalyzes the cleavage of terminal rhamnoside groups from naringin to prunin and rhamnose [12] (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

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Molecular characterization and enzymatic hydrolysis of naringin extracted from kinnow peel waste

Puri

Kaur

Schwarz³

et al. 2011

International Journal of Biological Macromolecules

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Section: Enzyme and Protein Assaymentioning

confidence: 99%

Section: Naringin Recovery From Kinnow Peelmentioning

confidence: 99%

Section: Purification Of Enzymementioning

confidence: 99%

“…␣-l-Rhamnosidase (EC 3.2.1.40) catalyzes the cleavage of terminal rhamnoside groups from naringin to prunin and rhamnose [12] (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

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Molecular characterization and enzymatic hydrolysis of naringin extracted from kinnow peel waste

Puri

Kaur

Schwarz³

et al. 2011

International Journal of Biological Macromolecules

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“…IMAC has been reported as a promissing technology for purification of proteins with an "N-terminal metal biding tag" (e.g., histidine tail and NT1A) (Puri et al, 2010;Petzold et al, 2014;Cheung et al, 2012), including on a large scale (Gaberc-Porekar and Menart, 2005), due to its low cost and the high purity of the eluate, even in a single step process (Puri et al, 2010;Carvalho et al, 2014). However, when approaching the purification of natural pro-teins, IMAC may present some challenges since the amount of histidine on the surface accounts for only 1% of the total number of amino acids (Ueda et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Steric Mass Action Model for Lactoferrin Adsorption in Cryogel With Immobilized Copper Ions

Carvalho

Júnior

Carvalho

et al. 2016

Braz. J. Chem. Eng.

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-Parameters of equilibrium adsorption obtained from experiments using immobilized metal affinity chromatography (IMAC) were used to evaluate the applicability of the steric mass-action (SMA) model to describe the adsorption of lactoferrin to cryogel resin under different conditions. The adsorption of lactoferrin on continuous supermacroporous cryogel with immobilized Cu 2+ ions was evaluated in batch adsorption experiments at different pH (6-8) and temperature (293-313 K) values. Estimated values of the equilibrium constant (K) and characteristic number of binding sites (n) showed that these parameters decreased with increasing ionic strength, pH and temperature, while the nonlinear parameter, the steric factor (), increased with increasing ionic strength and temperature. Expressions correlating these parameters with pH, ionic strength and temperature were then derived.

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Hydrolysis of citrus peel naringin by recombinant α‐L‐rhamnosidase from Clostridium stercorarium

Kaur

Singh

et al. 2010

J of Chemical Tech & Biotech

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The citrus fruit processing industry generates substantial quantities of waste rich in glycosylated phenolic substances such as naringin, which are a valuable natural source of polyphenols as well as L-rhamnopyranose. Naringin is the major polyphenol in bitter orange peel and its hydrolysis by α-L-rhamnosidase (EC 3.2.1.40) catalyzes the cleavage of the terminal rhamnosyl groups to form prunin and rhamnose. In this work, a recombinant α-L-rhamnosidase from C. stercorarium was shown to be suitable for narigin hydrolysis. The recombinant rhamnosidase was found to be relatively stable at 60• C, and a residual activity close to 50% after 180 min of incubation was demonstrated. The purified enzyme established hydrolysis of naringin extracted from citrus peel waste (CPW). The result indicated that recombinant α-L-rhamnosidase has industrial applicability and is an interesting candidate for producing rhamnose from citrus peel.

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One-step purification and immobilization of His-tagged rhamnosidase for naringin hydrolysis

Cited by 23 publications

References 34 publications

Molecular characterization and enzymatic hydrolysis of naringin extracted from kinnow peel waste

Molecular characterization and enzymatic hydrolysis of naringin extracted from kinnow peel waste

Steric Mass Action Model for Lactoferrin Adsorption in Cryogel With Immobilized Copper Ions

Hydrolysis of citrus peel naringin by recombinant α‐L‐rhamnosidase from Clostridium stercorarium

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