Use of microbial enzyme and cell preparations to synthesise oligopeptide antibiotics

Vandamme, Erick

doi:10.1002/jctb.280310187

Cited by 17 publications

(1 citation statement)

References 114 publications

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“…The biosynthesis of the antibiotic peptides gramicidin S and tyrocidine produced by different strains of Bacillus brevis has been elucidated by several groups (Roskoski et al, 1970;Lipmann, 1980;Kurahashi, 1981; Kleinkauf & Von Dohren, 1983). It was observed that the synthesizingenzyme system, which happened to be present in the soluble supernatant in the early stage of growth, changed from a soluble to a membranebound form with the age of the culture in the case of tyrocidine (Lee, 1974), gramicidin S (Vandamme & Demain, 1976;Vandamme, 1981;Nimi et al, 1982) andbacitracin (Fr0yshov, 1977), whereas in case of polymyxin (Balakrishnan et al, 1980;Vasantha et al, 1980) the reverse phenomenon occurred. However, in the case of edeine, the synthesizing-polyenzyme system has been shown to be associated with a membrane-DNA complex (Kurylo-Borowska, 1975) in the post-exponentialphase cells of Bacillus brevis Vm 4.…”

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Translocation of mycobacillin synthetase in Bacillus subtilis

Mukhopadhyay¹,

Ghosh²,

Majumder³

et al. 1985

Biochemical Journal

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The extracellular release of mycobacillin from Bacillus subtilis first occurred in the medium at the onset of stationary phase and continued at a high rate even after 6 days. Mycobacillin synthetase activity appeared earlier than late-exponential phase in the cytosol of producer cells and was not sedimentable even at 105 000 g. The activity then quickly reached the maximum late in the stationary phase. With further increase in the age of the culture, the activity gradually disappeared from the cytosol, to reappear concomitantly in the membrane in an insoluble particulate form, even in absence of protein synthesis. The membrane-bound synthetase activity was sedimentable at 10 000 g and was fairly active even after 5 days.

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Translocation of mycobacillin synthetase in Bacillus subtilis

Mukhopadhyay¹,

Ghosh²,

Majumder³

et al. 1985

Biochemical Journal

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The immobilization of penicillin G acylase on chitosan

Braun

Chanu

Goffic

1989

Biotech & Bioengineering

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The conversion of penicillin G into 6-aminopenicillanic acid (6-APA) is a very important reaction, 6-APA being the basic raw material for the industrial production of semisynthetic penicillins. Bulk 6-APA can be achieved either by chemical' or enzymatic hydrolysis. Each system has its advantage. However, because of improvements in immobilization techniques that promote stability and prolonged high activity, enzymatic hydrolysis has become a major alternative to chemical hydrolysis. The industrial route for 6-APA bioproduction was developed ca. 1960 and it can be assumed that almost all 6-APA is produced today by the immobilized enzymatic route.Numerous immobilization techniques for penicillin acylase have been tried on a laboratory scale. For instance, adsorption, crosslinking, covalent and physical attachment, and entrapment methods have been described.' However, more efficient procedures to obtain 6-APA are still being investigated and the immobilization of penicillin G acylase on a polysaccharide matrix, such as chito~an,~ by an economical and simple procedure could undergo an interesting biocatalyst .We have prepared different physical forms of chitosan (powder, particules, and beads), glyoxal reticulated or not, and used them as carriers to immobilize penicillin G acylase either by adsorption followed by reticulation with glutaraldehyde or by direct crosslinking to the matrix pretreated with glutaraldehyde. The first results of our experiments as well as the catalytic evaluation of the resins obtained are described in the present communication. MATERIALS AND METHODSPenicillin G and penicillin G acylase were a gift from Rhone-Poulenc; penicillin G acylase (0.25 U/mg protein) from E . coli was an acetone precipitate where no detectable p-lactamase activity was found (see below). Crab-shell chitosan was supplied by Rousselot (France); the degree of deacetylation was estimated by titrimetry4 to be more than 64%. Different reagents were synthetic grade products and were * To whom all correspondence should be addressed used without further purification: buffer A -0.005M phosphate buffer, pH 7.5, and buffer B -0.1 M phosphate buffer, pH 8 .00. Spectrophotometric measurements were made with a DU-8 Beckman spectrometer and the pH was regulated either with a Metrohm pH-stat or with a home-made regulation unit connected to a microcomputer (Apple IIe). Preparation of SupportsDifferent physical forms of matrices were prepared from the same chitosan solution (1 g chitosan dissolved in 15 mL of 5% acetic acid in water and filtered to remove insoluble materials). Powder was obtained by pouring dissolved chitosan into excess solution of 0.5M sodium hydroxide; it was collected by centrifugation and thoroughly washed with distilled water until neutrality.Particles were prepared at 25°C by addition of 0.1M sodium hydroxide to a stabilized (0.1-0.5% Tween SO) emulsion obtained by mixing the acetic acid solution of chitosan with cyclohexane (1 : 1). The particles were then washed in distilled water until neutrality and sized (0....

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ChemInform Abstract: USE OF MICROBIAL ENZYME AND CELL PREPARATIONS TO SYNTHESIZE OLIGOPEPTIDE ANTIBIOTICS

Vandamme¹

1982

Chemischer Informationsdienst

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Use of microbial enzyme and cell preparations to synthesise oligopeptide antibiotics

Cited by 17 publications

References 114 publications

Translocation of mycobacillin synthetase in Bacillus subtilis

Translocation of mycobacillin synthetase in Bacillus subtilis

The immobilization of penicillin G acylase on chitosan

ChemInform Abstract: USE OF MICROBIAL ENZYME AND CELL PREPARATIONS TO SYNTHESIZE OLIGOPEPTIDE ANTIBIOTICS

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