Production, purification, and characterization of the debittering enzyme naringinase

Puri, Munish; Banerjee, Uttam Chand

doi:10.1016/s0734-9750(00)00034-3

Cited by 139 publications

(103 citation statements)

References 25 publications

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“…This enzyme is also used for aroma enhancement in wine making and for preparation of many drugs as well as L-rhamnose. The latter plays the role of chiral intermediate in the organic synthesis of pharmaceutically important and plant protective agents [3][4][5][6][7].…”

Section: Discussionmentioning

confidence: 99%

“…1.40] are glycoside hydrolases, which catalyze the hydrolysis of terminal, non-reducing a-L-rhamnose residues in a-L-rhamnosides including glycolipids and glycosides, such as plant pigments, flavonoid glycosides, pectic polysaccharides, and gums [3][4][5][6][7]. The enzyme has wide occurrence in nature and has been reported from animals, plants, yeasts, fungi, and bacteria [4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

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Lateral gene transfer between the Bacteroidetes and Acidobacteria: The case of α‐l‐rhamnosidases

Naumoff

Dedysh

2012

FEBS Letters

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a b s t r a c t a-L-Rhamnosidases catalyze the hydrolysis of the terminal a-L-rhamnose residues in various carbohydrates. The catalytic domains in most of these enzymes belong to the families GH78 and GH106 of glycoside hydrolases. In this study, we show that almost all genes encoding the GH78-and GH106-containing proteins from members of the poorly characterized bacterial phylum Acidobacteria originated from precursors belonging to the phylum Bacteroidetes. Members of the Acidobacteria and Bacteroidetes display similar functional capabilities and specialize on degradation of plant-derived organic matter. Several proposed lateral gene transfers between the Acidobacteria and Bacteroidetes occurred presumably during specialization of these bacteria for their environments.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Lateral gene transfer between the Bacteroidetes and Acidobacteria: The case of α‐l‐rhamnosidases

Naumoff

Dedysh

2012

FEBS Letters

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“…because of its industrial application in debittering of fruit juices. However, in most cases these optima are related to the debittering action by stepwise breakdown of the bitter tasting compound naringin (4,5,7-trihydroxyflavanone-7-rhamnoglucoside) and so do not distinguish between rhamnosidase and glucosidase activitiy of the naringinase complex or focus on [15][16][17] but also here few data concerning the glucosidase activity are published. In studies on NPG as a substrate for P. decumbens naringinase, the same pH optimum of 3.0 was reported by Gabor and Pittner [15], in contrast to…”

Section: Ph and Temperature Optimum For Production Of Glucolipidsmentioning

confidence: 99%

Production of glucolipids and specialty fatty acids from sophorolipids by Penicillium decumbens naringinase: Optimization and kinetics

Saerens

Bogaert

Soetaert

et al. 2009

Biotechnology Journal

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In view of global environmental concerns and the awakening to the exhaustibility of our natural resources, an increasing importance of biologically derived surfactants can be expected in the near future. Enzymatic modification of these biosurfactants allows to improve their characteristics and so extend their application field. In view of this, glucolipids are interesting substrates e.g., for the synthesis of new glycolipids with increased biological activity. Here, we describe the optimization of glucolipid production from Candida bombicola sophorolipids by Penicillium decumbens naringinase and show that the enzyme might be useful for production of specialty fatty acids as well. Optimum conditions for production of glucolipids were found to be pH 7.0 and 50°C with a yield of 80% (w/w) glucolipids after 3 h of incubation. The Km for sophorolipids was 1.67 mM, while Vmax was 0.035 mM sophorolipids/min. At pH 3.0, glucolipids were immediately further hydrolyzed and completely converted to fatty acids after 24 h of incubation, offering a biological route to the synthesis of unique specialty fatty acids. The Km for glucolipids was 11 mM while Vmax was 0.21 mM glucolipids/min. Glucose inhibited the enzyme in a competitive way with KI around 10‐15 mM glucose. Surfactant properties of the produced glucolipids were comparable to those of the acidic sophorolipids.

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“…Cellulase and pectinase are used for the clarification of squeezed citrus juice and for the treatment of byproducts such as hydrolysis of peel waste, which is produced in citrus fruit squeezing factories (Wilkins et al, 2007). Naringinase is used as a debittering enzyme, to improve the bitter taste caused by high naringin content in grapefruit juice and bitter orange juice (Barm and Solomons 1965;Puri and Banerjee 2000). It can suppress the bitter taste, because the bitter naringin is converted to naringenin 7-O-β-glucoside or naringenin of no taste.…”

Section: Resultsmentioning

confidence: 99%

Preparation of a Lemon Flavonoid Aglycone and its Suppressive Effect on the Susceptibility of LDL to Oxidation Following Human Ingestion

Miyake

Sakurai

Usuda

et al. 2009

FSTR

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Lemon flavonoid (LF) prepared from lemon peel predominantly contains eriocitrin as an antioxidant. It is indicated to have low bioavailability compared with lemon flavonoid aglycone (LFA), which predominantly contains eriodictyol. This study attempted to prepare LFA which has high bioavailability, using enzymes that are commonly used in the citrus industry, such as cellulase, naringinase, hesperidinase, and pectinase. LFA containing the highest amount of eriodictyol (19.4%) was prepared with naringinase, a debittering enzyme for citrus juice. Ten male normolipidemic subjects ingested LFA (3.7 g) after an overnight fast, and low-density lipoprotein (LDL) was prepared from 0-4 h plasma after intake of LFA. The LDL oxidizability was measured with lag time of the conjugated diene formation induced by an oxidative inducer. LDL in 0.5 h plasma after ingestion of LFA was shown to have a significantly longer lag time for oxidation than that before ingestion (P<0.05). LFA was suggested to have the resistance effect of LDL to oxidation ex vivo. Eriodictyol, homoeriodictyol, and hesperetin were not detected in plasma by HPLC analysis, but they were detected in plasma treated with β-glucuronidase and sulfatase. The flavonoids were suggested to be glucuro-and/or sulfo-conjugates and to be metabolites in plasma after ingestion of LEA.

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Production, purification, and characterization of the debittering enzyme naringinase

Cited by 139 publications

References 25 publications

Lateral gene transfer between the Bacteroidetes and Acidobacteria: The case of α‐l‐rhamnosidases

Lateral gene transfer between the Bacteroidetes and Acidobacteria: The case of α‐l‐rhamnosidases

Production of glucolipids and specialty fatty acids from sophorolipids by Penicillium decumbens naringinase: Optimization and kinetics

Preparation of a Lemon Flavonoid Aglycone and its Suppressive Effect on the Susceptibility of LDL to Oxidation Following Human Ingestion

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