2010
DOI: 10.1007/s00726-010-0768-z
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Bioconversion of l-tyrosine to l-DOPA by a novel bacterium Bacillus sp. JPJ

Abstract: L-DOPA is an amino acid derivative and most potent drug used against Parkinson's disease, generally obtained from Mucuna pruriens seeds. In present communication, we have studied the in vitro production of L-DOPA from L-tyrosine by novel bacterium Bacillus sp. JPJ. This bacterium produced 99.4% of L-DOPA from L-tyrosine in buffer (pH 8) containing 1 mg ml(-1) cell mass incubated at 40°C for 60 min. The combination of CuSO(4) and L-ascorbic acid showed the inducing effect at concentrations of 0.06 and 0.04 mg m… Show more

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Cited by 74 publications
(59 citation statements)
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“…Laccase activity was determined in a reaction mixture of 2 ml containing 10 % ABTS in 0.1 M acetate buffer (pH 4.9), and increase in optical density was measured at 420 nm (Telke et al 2010). Tyrosinase activity was determined as described by Surwase and Jadhav (2010). NADH-DCIP reductase was measured in cell-free extract as per the earlier report (Salokhe and Govindwar 1999).…”
Section: Enzyme Assaysmentioning
confidence: 99%
“…Laccase activity was determined in a reaction mixture of 2 ml containing 10 % ABTS in 0.1 M acetate buffer (pH 4.9), and increase in optical density was measured at 420 nm (Telke et al 2010). Tyrosinase activity was determined as described by Surwase and Jadhav (2010). NADH-DCIP reductase was measured in cell-free extract as per the earlier report (Salokhe and Govindwar 1999).…”
Section: Enzyme Assaysmentioning
confidence: 99%
“…Stemonitis herbicola 50 mg [25] Aspergillus oryzae ( mutant) 1.28 mg/ml [26] Aspergillus oryzae 1.28 mg/ml [27] Aspergillus oryzae UV7( double mutant) 1.28 mg ml [28] Aspergillus oryzae 1.86 mg/ml [29] Aspergillus oryzae UV-7 444 g cells [30] Aspergillus oryzae ME2 (Illite) 1.686 mg/ml [31] Aspergillus oryzae ME2 (Celite) 0.428 mg/ml [32] Aspergillus oryzae (Double mutant) 300 mg [33] Aspergillus oryzae IIB-6 1.34 mg/ml [34] Acremonium retilum 0.89 mg/ml [35] Aspergillus niger 0.365 mg/ml [36] Actinomycetes 28.6% [37] Yeast Yarrowia lipolytica NRRL-143 2.96 mg/ml [38] Egyptian halophilic black yeast 66 ug/ml [39] Bacteria Vibrio tyrosinaticus 4 mg/ml [40] Pseudomonas melanogenum 8 mg/ml [41] E. coli W(ATCC 11105) (p-hydroxyphenyl acetate 3-hydroxylase) 48 mM in reaction mixture [42] Bacillus sp. JPJ 0.497 mg/ml [7] Recombinant The production of L-DOPA from biological sources involves the oxidation of L-tyrosine by enzyme tyrosinase (E.C.1.14.18.1), which is copper containing enzyme widely distributed in plants, animals and microorganisms [13]. Oxidation product of tyrosinase subsequently converted in to melanin; as it functions like alternative substrate for tyrosinase ultimately stimulate catalytic efficiency.…”
Section: Biological Sourcesmentioning
confidence: 99%
“…Initially, the medium optimization was performed in order to maximum production of L-DOPA. To overcome the tedious downstream processing after production of L-DOPA by this process, use of acclimatized cells with buffer gave the best results within less time and experimentation [7,[40][41][42][43][44]. In case of L-DOPA production using enzymatic process of recombinant E. herbicola cells carrying a mutant transcripttional regulator TyrR yield obtained was near about 15 g·l…”
Section: Bacterial Sourcesmentioning
confidence: 99%
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“…l -DOPA have been produced earlier by several biological sources that include Erwinia herbicola [8], Aspergillus oryzae [9], Yarrowia lipolytica NRRL-143 [10] , Bacillus sp. JPJ [11] and Brevundimonas sp. SGJ [12] , Acremonium rutilum [13] and Egyptian halophilic black yeast [14].…”
Section: Introductionmentioning
confidence: 99%