A pyruvated mannose-specific xanthan lyase involved in xanthan degradation by Paenibacillus alginolyticus XL-1
Article Abstract:
The xanthan-degrading bacteria Paenibacillus alginolyticus XL-1, isolated from soil, degrades approximately 28% of the xanthan molecule and appears to leave the backbone intact. Several xanthan-degrading enzymes were excreted during growth on xanthan, including xanthan lyase. Xanthan lyase production was induced by xanthan and inhibited by glucose and low-molecular-weight enzymatic degradation products from xanthan. A xanthan lyase with a molecular mass of 85 kDa and a pI of 7.9 was purified and characterized. The enzyme is specific for pyruvated mannosyl side chain residues.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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Screening for microorganisms producing D-malate from maleate
Article Abstract:
An investigation was conducted to isolate microorganisms capable of synthesizing D-malate from maleate on a commercial scale. More than 300 microorganisms were screened, resulting in the detection of 128 strains with putative maleate hydratase activities. Characterization of a single strain, identified as Pseudomonas pseudoalcaligenes NCIMB 9867 showed that it was not able to transport maleate. However, permeabilized cells were able to form D-malate at an enantiomeric purity of more than 99.97%.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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Aerobic vinyl chloride metabolism in Mycobacterium aurum L1
Article Abstract:
Mycobacterium aurum L1 is the sole bacterial strain that utilizes vinyl chloride aerobically as a source of carbon and energy. Enzyme assays were used to investigate the mechanism behind this utilization. Results show that an alkene monooxygenase isinvolved in the initial step of vinyl chloride metabolism. This enzyme convertsvinyl chloride into epoxide chlorooxirane. Further steps in the metabolism werenot identified due to the instability of this monooxygenase.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
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