Results 121 to 130 of about 4,548 (168)

Characterization of pectate lyase produced by Pseudomonas marginalis and cloning of pectate lyase genes

Physiological and Molecular Plant Pathology, 1995
Abstract Pseudomonas marginalis produced two pectate lyase isozymes in a medium containing sodium polypectate. Of the two, one had alkaline pI, 9·5, and the other had neutral pI, 7·0. Extracellular pectate lyase secretion started during mid-log phase and reached a maximum during the stationary phase of growth.
R.P. Elumalai, A. Mahadevan
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Bacterial pectate lyases, structural and functional diversity

Environmental Microbiology Reports, 2014
Summary Pectate lyases are enzymes involved in plant cell wall degradation. They cleave pectin using a β‐elimination mechanism, specific for acidic polysaccharides. They are mainly produced by plant pathogens and plant‐associated organisms, and only rarely by animals.
Nicole, Hugouvieux-Cotte-Pattat, Guy, Condemine, Vladimir E, Shevchik   +2 more
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Expression of anErwinia pectate lyase in three species ofAspergillus

Current Genetics, 1996
Transgenic filamentous fungi of the species Aspergillus niger, A. nidulans and A. awamori expressing and secreting Erwinia carotovora subsp. atroseptica pectate lyase 3 (PL3) were generated. Correct processing of the pre-enzyme was achieved using the A. niger pectin lyase A (PEL A) signal peptide. With the prepro-peptide of A.
Bartling, S., van den Hombergh, J.P.T.W., Olsen, O., von Wettstein, D., Visser, J.   +4 more
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The structure of Bacillus subtilis pectate lyase in complex with calcium

Nature Structural & Molecular Biology, 1994
We have solved the structure of the Bacillus subtilis pectate lyase (BsPel) in complex with calcium. The structure consists of a parallel beta-helix domain and a loop region. The alpha L-bounded beta-strand seen in BsPel is a new element of protein structure and its frequent occurrence suggests it is an important characteristic of the parallel beta ...
R, Pickersgill, J, Jenkins, G, Harris, W, Nasser, J, Robert-Baudouy   +4 more
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Characterization of Aspergillus niger Pectate Lyase A^,

Biochemistry, 2000
The Aspergillus niger plyA gene encoding pectate lyase A (EC 4.2.99. 3) was cloned from a chromosomal lambda(EMBL4) library using the Aspergillus nidulans pectate lyase encoding gene [Dean, R. A., and Timberlake, W. E. (1989) Plant Cell 1, 275-284] as a probe. The plyA gene was overexpressed using a promoter fusion with the A.
J A, Benen, H C, Kester, L, Parenicová, J, Visser   +3 more
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Pectate lyases: Their role in plants and importance in fruit ripening

Food Chemistry, 2020
Plant cell walls are complex structures that are modified throughout development. They are a major contributor to the properties of plant structure and act as barriers against pathogens. The primary cell walls of plants are composed of polysaccharides and proteins.
Selman, Uluisik, Graham B, Seymour
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Characterization of the N‐linked glycosylation site of recombinant pectate lyase

Rapid Communications in Mass Spectrometry, 1999
Recombinant pectate lyase from Aspergillus niger was overexpressed in Aspergillus nidulans. The two recombinant proteins produced differed in molecular mass by 1200 Da, which suggested that the larger molecular weight protein was glycosylated. The deduced amino acid sequence was searched for potential N-linked glycosylation sites, and one potential ...
Colangelo, J., Licon, V., Benen, J.A.E., Visser, J., Bergmann, C., Orlando, R.   +5 more
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Pectate lyase production by Bacillus subtilis in a membrane bioreactor

Applied Microbiology and Biotechnology, 1988
An environmental strain ofBacillus subtilis was cultivated in a membrane bioreactor. Microbial cells were trapped by an upright membrane module fitted in the vessel reactor. Cell biomass and pectate lyase activity were increased about 5–6 times in comparison to a batch process. Clogging of the membrane module appears to be a major problem.
A. Jauneau, C. Morvan, J. C. Fenyo, M. Demarty   +3 more
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Pectate lyase activity during ripening of banana fruit

Phytochemistry, 2003
Pectate lyase (PEL) activity was demonstrated in ripe banana fruits on supplementing the homogenizing medium with cysteine and Triton X-100. The enzyme was characterized on the basis of alkaline pH optimum, elimination of the activity by EDTA and activation by Ca(2+). PEL activity was not detected in preclimacteric banana fruits. PEL activity increased
Anurag, Payasi, G G, Sanwal
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Organization of a pectate lyase gene family in Erwinia chrysanthemi

Gene, 1986
The pelA, pelD and pelE genes encode three of the five major pectate lyase (PL) isoenzymes (PLa, PLd and PLe) in Erwinia chrysanthemi strains B374 and 3937. These genes were previously isolated from genomic libraries or by in vivo cloning as R' factors promoted by the pULB113 plasmid.
Reverchon, Sylvie, Van Gijsegem, Frédérique, Rouve, M., Kotoujansky, Alain, Robert-Baudouy, Janine   +4 more
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