Isolation of new limonoate dehydrogenase from Pseudomonas

Hasegawa, Shin; Maier, V. P.; King, Aleah D.

doi:10.1021/jf60193a009

Cited by 31 publications

(19 citation statements)

References 7 publications

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“…LDase from Arthrobacter (2,22), Pseudomonas (8), and Acinetobacter (23) species is inducible by limonoate, whereas the enzyme from R. fascians is constitutively expressed. However, overexpression of LDase has been obtained with R. fascians cells grown in disodium limonoate-containing media (5).…”

Section: Discussionmentioning

confidence: 99%

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Purification and characterization of limonoate dehydrogenase from Rhodococcus fascians

Humanes

Lopez‐Ruiz

Merino

et al. 1997

Appl Environ Microbiol

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Limonoate dehydrogenase from Rhodococcus fascians has been purified to electrophoretic homogeneity by a procedure that consists of ion-exchange, hydrophobic, and affinity chromatography. The native enzyme has a molecular mass of around 128,000 Da and appears to be composed of four similar subunits (30,000 Da each). The isoelectric point is 4.9 as determined by isoelectric focusing. The homogeneous enzyme was used to determine the NH 2-terminal amino acid sequence. The enzyme was purified from cells grown in either fructose or limonoate as a carbon source. Limonoate dehydrogenase activity was higher in limonoate-grown cultures. Additionally, the enzyme preparations differed in their affinity for limonoids but not for NAD ؉. In all cases limonoate dehydrogenase exhibited a higher catalytic rate and stronger affinity for limonoate A-ring lactone than for disodium limonoate, the limonoid traditionally used for in vitro activity assays. Our data confirm previous reports proposing that limonoate A-ring lactone is the physiological substrate for limonoate dehydrogenase. The increase in limonoate dehydrogenase activity observed in limonoate-grown cultures appears to be caused by a rise in protein levels, since chloramphenicol prevented such an effect.

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Section: Discussionmentioning

confidence: 99%

“…The enzyme has been isolated from Arthrobacter globiformis (2), Pseudomonas sp. strain 321-18 (8), and Rhodococcus fascians (5). In these studies a partial purification and characterization of LDase was described.…”

mentioning

confidence: 99%

Purification and characterization of limonoate dehydrogenase from Rhodococcus fascians

Humanes

Lopez‐Ruiz

Merino

et al. 1997

Appl Environ Microbiol

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“…, 1972a; 1973), Pseudomonas sp. Strain 321‐18 (Hasegawa et al. , 1974), Cornyebacterium fascians (Hasegawa & King, 1983), Rhodococcus fascians (Cánovas et al.…”

Section: Introductionmentioning

confidence: 99%

“…The bacterial genus that are known so far as limonin metabolizing micro-organisms are Arthrobacter globiformis (Hasegawa et al, 1972a;1973), Pseudomonas sp. Strain 321-18 (Hasegawa et al, 1974), Cornyebacterium fascians (Hasegawa & King, 1983), Rhodococcus fascians (Ca´novas et al, 1998). These micro-organisms have known to metabolize limonin via 17-dehydrolimonoid and deoxylimonoid pathways.…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of cellular locus of limonin biotransforming enzyme in Pseudomonas putida

Verma

Singh

Ghosh

et al. 2010

Int J of Food Sci Tech

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Limonin is a highly oxygenated triterpene derivative of class of limonoids which causes delayed bitterness in citrus. Pseudomonas putida (P. putida) is able to reduce 47% and 63% of limonin from juice serum extract and standard limonin, respectively. Biochemical studies with P. putida indicate that probably two metabolic pathways viz. 17-dehydrolimonoid and deoxylimonoid pathway exists in the test organism. Experimental results indicate that the enzyme limonoate dehydrogenase which is found to be localized in periplasmic space of P. putida plays a major role in conversion of limonin to 17-dehydrolimonoate A-ring lactone. Enzymatic studies have shown a 72% reduction in limonin. The experimental results show 9 folds reduction in limonin content in presence of NAD as cofactor. The molecular weight of one of its polypeptide is found to be 66 kDa. The optimum pH and temperature for enzyme activity is 8.5 and 30°C, respectively.

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“…When juices are prepared from Citrus tissues, LARL is chemically converted into limonin under the produced acidic conditions, generating the so called "delayed bitterness". It can be prevented by limonoate dehydrogenase, an enzyme described in different bacterial species and orange fruit tissues, that irreversibly converts LARL into its dehydro form, thus avoiding limonin production (Hasegawa et al, 1972, 1974a, 1974b, 1976, Hasegawa and King, 1983, Hasegawa and Maier, 1990. Additionally, an enzyme catalyzing the reversible conversion of LARL into limonin was isolated from Citrus seeds .…”

Section: Introductionmentioning

confidence: 99%

Production of limonoate A-ring lactone by immobilized limonin D-ring lactone hydrolase

et al. 1996

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Limonin D-ring lactone hydrolase, the enzyme catalysing the reversible lactonization/hydrolysis of D-ring in limonin, has been purified from Citrus seeds and immobilized on Q-Sepharose to produce homogeneous limonoate A-ring lactone solutions. The immobilized limonin D-ring lactone hydrolase showed a good operational stability and was stable after sixty-seventy operations and storing at 4°C for six months.

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Isolation of new limonoate dehydrogenase from Pseudomonas

Cited by 31 publications

References 7 publications

Purification and characterization of limonoate dehydrogenase from Rhodococcus fascians

Purification and characterization of limonoate dehydrogenase from Rhodococcus fascians

Identification and characterization of cellular locus of limonin biotransforming enzyme in Pseudomonas putida

Production of limonoate A-ring lactone by immobilized limonin D-ring lactone hydrolase

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