Synthesis of variable enzyme spectrum by immobilized mycelium of A. niger

Leuchtenberger, A.; Friese, E.; Ruttloff, H.

doi:10.1016/s0232-4393(89)80094-0

Cited by 12 publications

(2 citation statements)

References 5 publications

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“…Fungal PGs also have industrial uses, such as processing aids for extraction, clarification, and depectinization of fruit juices, for maceration of fruits and vegetables, and for extraction of vegetable oils (16,19,27,28).…”

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confidence: 99%

Common amino acid domain among endopolygalacturonases of ascomycete fungi

Keon

Waksman

1990

Appl Environ Microbiol

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The endopolygalacturonase (EC 3.2.1.15) enzymes produced in vitro by three ascomycete fungi, Aspergillus niger, Sckerotinia scierotiorum, and Colletotrichum lindemuthianum were studied by using thin-layer isoelectric focusing and activity stain overlay techniques. The polygalacturonases from A. niger and S. sclerotiorum consisted of numerous isoforms, whereas the endopolygalacturonase from C. lindemuthianum consisted of a single protein species. The most abundant endopolygalacturonase isoform produced by each of these organisms was purified and characterized. Biochemical parameters, including molecular weight, isoelectric point, kinetic parameters, temperature and pH optima, and thermal stability, were determined. Considerable differences in physical and chemical properties were demonstrated among these fungal polygalacturonases. Antibodies raised against individual proteins exhibited little cross-reaction, suggesting that these enzymes differ structurally as well as biochemically. In contrast, the analysis of the N-terminal amino acid sequences of the three proteins showed extensive homology, particularly in a region labeled domain 1 in which 84% of the amino acids were conserved.

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confidence: 99%

Common amino acid domain among endopolygalacturonases of ascomycete fungi

Keon

Waksman

1990

Appl Environ Microbiol

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“…The use of the immobilized cell preparations in biotechnological processes allows easier separation of the cells from the fermentation broth, the isolation and refinement of the products and allows the repeated use of the entrapped cells. Many papers and reviews on immobilization of microbial cells have been published ; however, no ideal general method applicable to the immobilization of all types of microbial cells has yet been worked out (Linko and Linko 1984;Chibata et al 1986;Scoot 1987;Turker and Mavituna 1987 ;Leuchtenberger et al 1989). Biotechnologists need to develop a cell immobilization procedure which must be simple, inexpensive and would achieve a good retention of important enzyme activities in a good operational stability.…”

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confidence: 99%

Seeds as natural matrices for immobilization of Aspergillus niger mycelium producing pectinases

Fiedurek

Szczodrak²,

Rogalski

1995

Journal of Applied Bacteriology

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A simple method for the immobilization of Aspergillus niger mycelium producing polygalacturonase (PG) and pectinesterase (PE) is described. Fungal conidia were immobilized on wheat, rye, barley, peas, buckwheat and mustards seeds. Spongy mycelia overgrowing the seed surfaces on mineral medium with pectin produced extracellular PG and PE; the highest production was reached on the wheat carrier. Some of the variables influencing the enzymatic activity have been optimized. After every 24 h, a culture liquid with 6.8-7.8 U of PG ml-1 and 7.0-10.1 U of PE ml-1 was obtained. This procedure also made possible repeated batch enzyme production and, as many as eight subsequent 24-h batches could be fermented by using the same carrier without any loss of PG activity. The addition of sodium orthovanadate (1 mmol) into the medium with pectin caused a significant increase in PG and PE activity produced by free cells of A. niger (by 1.59-fold and 1.67-fold respectively), and only 0.47-fold of PG activity in case of the immobilized mycelium.

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