1994
DOI: 10.1007/bf02814442
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Proteinase production by halophilic isolates from marine sediments

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Cited by 4 publications
(3 citation statements)
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“…This temperature range seems quite low for a thermophilic species (Ronimus et al 1997), but strains of B. licheniformis are known to have a large thermotolerance (Logan and De Vos, 2015). The presence of B. licheniformis in the Wadden Sea samples is perhaps more related to the presence of suspended marine sediment (Manachini and Fortina 1994) due to high spring wind speeds than to temperature. B. licheniformis did not produce false-positive results in the standard enterococci MEA-BEA method (Figure 5).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…This temperature range seems quite low for a thermophilic species (Ronimus et al 1997), but strains of B. licheniformis are known to have a large thermotolerance (Logan and De Vos, 2015). The presence of B. licheniformis in the Wadden Sea samples is perhaps more related to the presence of suspended marine sediment (Manachini and Fortina 1994) due to high spring wind speeds than to temperature. B. licheniformis did not produce false-positive results in the standard enterococci MEA-BEA method (Figure 5).…”
Section: Resultsmentioning
confidence: 99%
“…11 licheniformis were isolated from marine sediment off the Italian west coast and all were able to grow in seawater and in NaCl solutions up to 150 g/L (Manachini and Fortina 1994). In the Wadden Sea, the water temperature ranged from 6 to 12°C and the highest concentrations of B. licheniformis (ca 2,000/100 mL) were measured at <8 °C with lower concentrations at elevated temperatures (12-13°C) at the end of April.…”
Section: Resultsmentioning
confidence: 99%
“…The immobilization of glucoamylase is studied in detail with a view not only to its industrial application, which is very attractive, but also connected with its use as a model system when Comparing different modes of immobilization. Glucoamylase has been immobilized by adsorption [ [16,17,181 investigated the immobilization of glucoamylase by entrapping in gelatin or by covalent binding with glutaraldehyde and TiC14 on the surface of the gel particles. The authors reported divergences in the properties of the immobilized enzyme, more specifically in the formation of reversion products with a-1,6…”
Section: Introductionmentioning
confidence: 99%