Differentiation of Serratia Marcescens and Serratia Liquefaciens by Tests for Lipase and Phospholipase Production

Legakis, N. J.; Nicolas, K. J.; Xilinas, M; Papavassiliou, J.

doi:10.1099/00222615-11-3-225

Cited by 6 publications

(4 citation statements)

References 17 publications

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“…S. liquefaciens S33 DB‐1 showed an extracellular alkaline lipase activity in lipolytic olive oil with similar molecular size to the one in this study and an optimal pH range of 7–9 at temperatures below 45 °C . Although S. marcescens is usually associated with lipase production, it has also been seen in S. liquefaciens . This extracellular enzyme activity also could cause negative nutritional benefits by hydrolyzing long chain fatty acids…”

Section: Discussionsupporting

confidence: 62%

Purification and characterization of the thermostable protease produced by Serratia grimesii isolated from channel catfish

et al. 2018

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BACKGROUND: Microbial spoilage of fishery products accounts for significant financial losses, yearly on a global scale. Psychrotrophic spoilage bacteria often secrete extracellular enzymes to break down surrounding fish tissue, rendering the product unsuitable for human consumption. For a better understanding of bacterial spoilage due to enzymatic digestion of fish products, proteases in Serratia grimesii isolated from North American catfish fillets (Ictalurus punctatus) were investigated. RESULTS: Mass spectrometric evidence demonstrated that S. grimesii secretes two distinct extracellular proteases and one lipase.Protease secretion displayed broad thermostability in the 30-90 ∘ C range. The major protease-secretion (O-1) was most active under alkaline conditions and utilized manganese as a co-factor. Organic solvents significantly disrupted the efficacy of S. grimesii extracellular enzymes and, in a series of bactericidal detergents, protease activity was highest when treated with Triton X-100. Ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF) significantly inhibited the enzyme activity, while protease was moderately stable under freeze-thaw and refrigerated storage. CONCLUSION: The influence of fish spoilage-related enzymes, depending on various factors, is discussed in this paper. This study will provide new insight into enzymatic spoilage and its control, which can be exploited to enhance food safety and the shelf-life of fishery products worldwide.

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Section: Discussionsupporting

confidence: 62%

Purification and characterization of the thermostable protease produced by Serratia grimesii isolated from channel catfish

et al. 2018

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“…Until now, there have been few reports on lipases from S. liquefaciens. In 1978, one test on the lipase and phospholipase revealed that S. liquefaciens exhibited strong lipase, but only a minor phospholipase activity [9]. Yu et al isolated a strain with the highest lipolytic activity, S. liquefaciens S33 DB-1, from 150 oil-contacted soil samples [10].…”

Section: Introductionmentioning

confidence: 99%

Isolation of a Novel Lipase Gene from Serratia liquefaciens S33 DB-1, Functional Expression in Pichia pastoris and its Properties

Yao

Zhang

et al. 2007

Mol Biotechnol

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Utilization of RNA interference (RNAi) for knockdown of gene expression has become a standard tool for the study of gene function. Short hairpin RNAs (shRNAs) expressed from RNA polymerase III promoters are widely used to achieve stable knockdown of gene expression by RNAi. We have constructed a retroviralbased shRNA expression vector, pSiRPG, as a tool for shRNA-based functional genomic studies. This vector is based on a widely used shRNA expression system and was modified to harbor an enhanced green fluorescent protein (EGFP) and a puromycin selection marker. The functionality of the elements in the pSiRPG vector was validated. The H1(TetO2) promoter in the vector facilitates doxycycline-inducible shRNA expression, which was demonstrated in cells expressing the Tet repressor (TetR). However, we also demonstrated limited efficiency of the inhibition of shRNA expression in an uninduced TetR-expressing cell line. This observation strongly indicates that the H1(TetO2) promoter, which is used in a wide range of vectors, is not optimal for tightly regulated shRNA expression. Stable repression of the NDRG1 protein level was observed when introducing pSiRPG constructs expressing shRNAs targeting NDRG1 into two mammary epithelial cell lines by retroviral delivery. This vector should therefore facilitate functional studies in breast cell lines that are hard to transfect with conventional plasmid-based methods.

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“…To date, there have been no prior reports of suppurative thrombophlebitis or endocarditis caused by S. liquefaciens in the world's literature. This organism is differentiated from S. marcescens by its relatively weak phospholipase activity [17] and the lack of fermentation of l ‐arabinose by the latter [1]. Antimicrobial susceptibility is also somewhat different, with S. liquefaciens being more resistant to aztreonam, ceftazidime and amikacin than S. marcescens [18].…”

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confidence: 99%

The world's first case of Serratia liquefaciens intravascular catheter-related suppurative thrombophlebitis and native valve endocarditis

Mossad

2000

Clinical Microbiology and Infection

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Differentiation of Serratia Marcescens and Serratia Liquefaciens by Tests for Lipase and Phospholipase Production

Cited by 6 publications

References 17 publications

Purification and characterization of the thermostable protease produced by Serratia grimesii isolated from channel catfish

Purification and characterization of the thermostable protease produced by Serratia grimesii isolated from channel catfish

Isolation of a Novel Lipase Gene from Serratia liquefaciens S33 DB-1, Functional Expression in Pichia pastoris and its Properties

The world's first case of Serratia liquefaciens intravascular catheter-related suppurative thrombophlebitis and native valve endocarditis

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