Studies on the production of lipase from recombinant Staphylococcus carnosus

Falk, Martina; Sanders, Ernst A.; Deckwer, Wolf‐Dieter

doi:10.1007/bf00180627

Cited by 9 publications

(4 citation statements)

References 12 publications

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“…This effect of agitation was absent when skim-milk was the inducer. A similar effect of agitation on lipase production was demonstrated by Falk et al (1991), who attributed it to a decrease in the enzyme activity. In contrast, agitation or an increase in oxygenation increased lipase production by A. lipolyticum (Khan et al 1967) and P. fragi (Lawrence 1967).…”

Section: Resultsmentioning

confidence: 57%

“…This was also true for the production of two periplasmic phosphatases. Optimal production of lipase by cells cultivated at a growth temperature lower than the optimal growth temperature has been demonstrated in other bacteria such as P. fragi (8°C versus 20 ° C) (Andersson 1980) Staphylococcus carnosus (Falk et al 1991), and Achromobacter lipolyticum (21°C versus 30 ° C) (Khan et al 1967). …”

Section: Introductionmentioning

confidence: 99%

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Temperature regulation of lipase secretion by Pseudomonas fluorescens strain MFO

Merieau¹,

Gügi²,

Guespin‐Michel

et al. 1993

Appl Microbiol Biotechnol

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The psychrotrophic bacterium Pseudomonas fluorescens is a milk contaminant known to secrete a lipase that is a nuisance for the dairy industry but may have a biotechnological interest. Strain MF0 secretes this enzyme upon induction under various conditions. Regardless of the inducer and growth temperature, a single enzyme is produced. However, optimal production occurs when the culture is grown at 17.5 ° C. Other exported proteins (an extracellular protease and two periplasmic phosphatases) have previously been shown to display exactly the same optimal temperature of production. In contrast, constitutive cell-bound esterase and cytochrome oxidase are produced at a roughly constant rate regardless of the growth temperature. The relevance of these results are discussed in terms of multifunctional regulation and interest for the dairy industry.

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Section: Resultsmentioning

confidence: 57%

Section: Introductionmentioning

confidence: 99%

Temperature regulation of lipase secretion by Pseudomonas fluorescens strain MFO

Merieau¹,

Gügi²,

Guespin‐Michel

et al. 1993

Appl Microbiol Biotechnol

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“…Generally, the pH of a culture medium affects both the morphological and physiological characteristics of an organism [36] and [37] observed maximum lipase at a pH 8. "Microorganisms vary in their oxygen requirements.…”

Section: Discussionmentioning

confidence: 99%

Protease Production by Submerged Fermentation in Shake Flasks Using Bacillus sp. Isolated from the Soil

Okpalla

Onyekuru²,

Duru³

et al. 2022

MRJI

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Proteases are one of the most industrially important enzymes, which account for about 60% of total enzyme market. Protease production by submerged fermentation in shake flasks using Bacillus sp. isolated from the soil was studied. Soil samples were collected from different locations within Chukwuemeka Odumegwu Ojukwu University, Uli, Anambra state. The soil samples were serially diluted and inoculated on sterilized skim milk agar plates. The plates were incubated at 30oC for 72 h. A clear zone around the colonies gave an indication of protease-producing bacteria isolates. The selected protease producers were subsequently used for shake flask fermentation in 50 ml sterile medium. Optimization study was conducted to determine the effect of carbon sources, nitrogen sources, trace elements, agitation rates and pH. Twenty one bacteria isolates were found to be active protease producers and isolates RS-5 and OS-9 had the highest zone of clearance of 13.5 and 12.1 mm respectively. The result of submerged production of protease by the bacteria isolates revealed that the isolates RS-5 and OS-9 accumulated maximum protease yield of 3.23 and 2.71 U/ml respectively. The isolates were Gram positive and endospore formers, and were identified as Bacillus sp. RS-5 and OS-9.The addition of Starch and maltose stimulated optimum protease production of 3.47 and 2.77 U/ml by Bacillus sp. RS-5 and OS-9 respectively. Beef extract enhanced maximum enzyme yield of 3.35 and 2.90 U/ml for Bacillus sp. RS-5 and OS-9 respectively. Maximum protease yield of 3.28 U/ml for Bacillus sp. RS-5 and 2.85 U/ml for Bacillus sp. OS-9 was obtained by the supplementation of 0.4 g/l of FeS04 respectively. The maximum protease yield was observed at agitation rate of 200 rpm for Bacillus sp. RS-5 and 170 rpm for Bacillus sp. OS-9. At pH8, protease accumulation was highest for Bacillus sp. RS-5 and OS-9. The study revealed that the soil harbours some protease-producing bacteria strains and protease production can be greatly enhanced through optimization of process parameters.

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“…Furthermore, the addition of anti foam agent stabilized the enzyme up to 97%. Falk et al [21] found that gassing with helium led to the same decrease in lipase activity from Staphylococcus carnosus as gassing with air.…”

Section: Treatmentmentioning

confidence: 95%

Regulation and Properties of A Fungal Lipase Showing Interfacial Inactivation by Gas Bubbles, or Droplets of Lipid or Fatty Acid

Stahmann

Böddecker

Sahm

1997

European Journal of Biochemistry

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Ashbya gossypii can grow on triacylglycerol as carbon source. A degradation rate of 0.05 gXg-' mycelial dry massxh-' was detected for soybean oil. Although this rate was within the sensitivity range of lipase assays no activity was detectable. On the other hand, extracellular lipase activity could be visualized by clearance halos round the growing mycelium when trioleoylglycerol was emulsified as the sole carbon source in agar plates. Variation of the culture conditions revealed that reduced shaking speed and decreased fat content in the medium led to detectable amounts of lipase in the supernatant of flask cultures. A maximal activity of 800 UX1-I was obtained after 32 h of cultivation in flasks containing 1 % yeast extract and incubated at 60 rpm. Because of its PI of 9.0, the enzyme could be purified in a single step by preparative isoelectric focusing. It appeared as a homogeneous protein in analytical isoelectric focusing and SDS/PAGE (Mr 35 000). The lipase was inactivated within minutes in stirred gadwater, trioleoylglycerol/water or oleic acidwater mixtures. These effects suggested an interface inactivation. This idea was supported by a stability modulation observed with the surfactant PluronicR F-68. Inactivation by oleic acid led to an aggregation of the lipase shown by gel filtration. Growth experiments performed under lipase-stabilizing conditions revealed a negative influence of glucose, glycerol or oleic acid on detectable lipase activity, probably due to a regulation of lipase formation. Inactivation and regulation thus explained the lack of detectable lipase activity in cultures of A. gossypii growing on triacylglycerol.Keywords: lipase; enzyme stability ; interface ; fungi ; Ashbya gossypii.Lipases are widely distributed among animals, plants and microorganisms [ l , 21. All the enzymes studied so far have in common that they are water-soluble but only maximally active when adsorbed to the interface between water and their waterinsoluble substrate. This property, also relevant for other interfacial enzymes [3], is known as interfacial activation [4]. It can be interpreted in two ways: firstly as an activation of the substrate and secondly as a change in the enzyme's conformation [5]. The major aspect of this paper is a strong effect of the interface on a lipase resulting in complete loss of its enzymatic activity. The enzyme in question is an extracellular lipase formed by the filamentous fungus Ashbya gossypii.The hemiascomycete A. gossypii (Ashby & Nowell) Guilliermond (1 928) is an important overproducer of vitamin B,. Since 1968 it has been used in technical processes on an industrial scale [6]. As a carbon source, carbohydrates are suitable but plant oils are even better 171. An unsolved problem in the metabolism of the fungus was its first step, namely the degradation of the triacylglycerol. Up to now, it has not been possible to detect an extracellular lipase in cultures degrading fat. Its existence could only be concluded from growth experiments with pure trioleoylglycerol and the subseq...

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Studies on the production of lipase from recombinant Staphylococcus carnosus

Cited by 9 publications

References 12 publications

Temperature regulation of lipase secretion by Pseudomonas fluorescens strain MFO

Temperature regulation of lipase secretion by Pseudomonas fluorescens strain MFO

Protease Production by Submerged Fermentation in Shake Flasks Using Bacillus sp. Isolated from the Soil

Regulation and Properties of A Fungal Lipase Showing Interfacial Inactivation by Gas Bubbles, or Droplets of Lipid or Fatty Acid

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