Manufacture of l-amino acids with bioreactors

Hamilton, Bruce K.; Hsiao, Humg-Yu; Swann, Wayne E.; Anderson, David M.; Delente, Jacques

doi:10.1016/0167-7799(85)90079-4

Cited by 88 publications

(17 citation statements)

References 12 publications

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“…Since the reaction is reversible, PAL can be used in a large-scale bio-conversion to produce L-phenylalanine from trans -cinnamic acid and ammonium salts acid [84]. Commercial production of PAL is available from R. glutinis (Sigma-Aldrich, St. Louis, MO, USA).…”

Section: Commercial and Medical Potential Of Palmentioning

confidence: 99%

Fungal and Plant Phenylalanine Ammonia-lyase

et al. 2011

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L-Phenylalanine is one of the essential amino acids that cannot be synthesized in mammals in adequate amounts to meet the requirements for protein synthesis. Fungi and plants are able to synthesize phenylalanine via the shikimic acid pathway. L-Phenylalanine, derived from the shikimic acid pathway, is used directly for protein synthesis in plants or metabolized through the phenylpropanoid pathway. This phenylpropanoid metabolism leads to the biosynthesis of a wide array of phenylpropanoid secondary products. The first step in this metabolic sequence involves the action of phenylalanine ammonia-lyase (PAL). The discovery of PAL enzyme in fungi and the detection of 14CO2 production from 14C-ring-labeled phenylalanine and cinnamic acid demonstrated that certain fungi can degrade phenylalanine by a pathway involving an initial deamination to cinnamic acid, as happens in plants. In this review, we provide background information on PAL and a recent update on the presence of PAL genes in fungi.

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Section: Commercial and Medical Potential Of Palmentioning

confidence: 99%

Fungal and Plant Phenylalanine Ammonia-lyase

et al. 2011

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“…Since the discovery of Corynebacterium glutamicum (originally named Micrococcus glutamicus) as an efficient glutamate-secreting microorganism in 1957 [1,2], the production of L-amino acids by fermentative procedures has become an important aspect of industrial microbiology [2][3][4][5][6][7][8][9][10][11][12][13][14]. In the course of the years, by various screening methods, many different amino acid-producing bacteria have been isolated.…”

Section: Introductionmentioning

confidence: 99%

Secretion of amino acids by bacteria: Physiology and mechanism

Krämer

1994

FEMS Microbiology Reviews

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Although representing a common property of microorganisms and being widely used for biotechnological purposes, solute secretion has been relatively poorly studied in terms of biochemistry. In this review, various examples of metabolite secretion processes by bacteria are discussed with the emphasis on the mechanisms of amino acid secretion by coryneform bacteria. Among the metabolic concepts which may be applied to explain the physiological meaning of metabolite secretion, mainly two concepts are dealt with, i.e. the so‐called 'overflow metabolism' on the one hand and the situation where non‐metabolizable intermediates are accumulated and finally secreted on the other. In the central part of this review, the different concepts are discussed which have been put forward to mechanistically explain amino acid secretion under particular metabolic conditions and in particular strains of bacteria, i.e. secretion mediated (i) by diffusion, (ii) by the participation of amino acid uptake systems, and (iii) by the use of specific secretion systems. These concepts are then applied to amino acid secretion in Corynebacterium glutamicum, and emplified by detailed studies on the mechanism and regulation of the secretion of lysine, isoleucine and glutamate by C. glutamicum.

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“…The enzyme has received considerable interest as a possible candidate in oral enzyme therapy of patients suffering from phenylketonuria (Inoue et al 1986;Hoskins et al 1980) and in quantitative analysis of serum phenylalanine (Koyama 1984). Furthermore, the reverse reaction has been exploited commercially in the production of L-phenylalanine, which is a precursor for the high powered artificial sweetener Aspartame (Hamilton et al 1985;Evans et al 1987a). …”

mentioning

confidence: 99%

Expression in E. coli of the gene encoding phenylalanine ammonia-lyase from Rhodosporidium toruloides

Ørum¹,

Rasmussen²

1992

Appl Microbiol Biotechnol

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The active sites of the enzyme phenylalanine ammonia-lyase (Pal) from Rhodosporidium toruloides contains a dehydroalanine residue that is believed to be essential for catalytic activity. Furthermore, the dehydroalanine is believed to be added post-translationally as part of a prosthetic group covalently attached to the enzyme. Perhaps for this reason no attempts to produce Pal in foreign host cells have been reported. We have inserted the entire uninterupted pal gene from R. toruloides into the Escherichia coli expression vector pKK 223-3. E. coli cells containing this vector synthesize a protein of the expected size, and extracts prepared from these cells contain a Pal-like activity. The potential implications of this finding are discussed.

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Manufacture of l-amino acids with bioreactors

Cited by 88 publications

References 12 publications

Fungal and Plant Phenylalanine Ammonia-lyase

Fungal and Plant Phenylalanine Ammonia-lyase

Secretion of amino acids by bacteria: Physiology and mechanism

Expression in E. coli of the gene encoding phenylalanine ammonia-lyase from Rhodosporidium toruloides

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