Effect of a Heat-Resistant Microbial Lipase on Flavor of Ultra-High-Temperature Sterilized Milk

Andersson, Ronnie; Danielsson, G.; Hedlund, C.B.; Svensson, S.G.

doi:10.3168/jds.s0022-0302(81)82581-7

Cited by 33 publications

(23 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Many cases of milk spoilage have reportedly been attributed to the thermostable lipase produced by P. fluorescens SIK W1 (3,4). In a previous study, the P. fluorescens SIK W1 thermostable lipase/protease operon containing prtA, inh, tliD, tliE, tliF, and tliA was cloned and sequenced (2).…”

Section: Resultsmentioning

confidence: 99%

Lipase and Protease Double-Deletion Mutant of Pseudomonas fluorescens Suitable for Extracellular Protein Production

Son

Moon

et al. 2012

Appl Environ Microbiol

View full text Add to dashboard Cite

bPseudomonas fluorescens, a widespread Gram-negative bacterium, is an ideal protein manufacturing factory (PMF) because of its safety, robust growth, and high protein production. P. fluorescens possesses a type I secretion system (T1SS), which mediates secretion of a thermostable lipase (TliA) and a protease (PrtA) through its ATP-binding cassette (ABC) transporter. Recombinant proteins in P. fluorescens are attached to the C-terminal signal region of TliA for transport as fusion proteins to the extracellular medium. However, intrinsic TliA from the P. fluorescens genome interferes with detection of the recombinant protein and the secreted recombinant protein is hydrolyzed, due to intrinsic PrtA, resulting in decreased efficiency of the PMF. In this research, the lipase and protease genes of P. fluorescens SIK W1 were deleted using the targeted gene knockout method. Deletion mutant P. fluorescens ⌬tliA ⌬prtA secreted fusion proteins without TliA or protein degradation. Using wild-type P. fluorescens as an expression host, degradation of the recombinant protein varied depending on the type of culture media and aeration; however, degradation did not occur with the P. fluorescens ⌬tliA ⌬prtA double mutant irrespective of growth conditions. By homologous expression of tliA and the ABC transporter in a plasmid, TliA secreted from P. fluorescens ⌬prtA and P. fluorescens ⌬tliA ⌬prtA cells was found to be intact, whereas that secreted from the wild-type P. fluorescens and P. fluorescens ⌬tliA cells was found to be hydrolyzed. Our results demonstrate that the P. fluorescens ⌬tliA ⌬prtA deletion mutant is a promising T1SS-mediated PMF that enhances production and detection of recombinant proteins in extracellular media.

show abstract

Section: Resultsmentioning

confidence: 99%

Lipase and Protease Double-Deletion Mutant of Pseudomonas fluorescens Suitable for Extracellular Protein Production

Son

Moon

et al. 2012

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…However, bacterial lipases are much more heat-resistant. Several reports have indicated that some bacterial lipases of Pseudomonas fluorescens have survived in milk during UHT processing (22,26,27). Recently, Choi and Jeon (20) presented some evidence of residual lipase activities in commercial UHT milks, as well as in their centrifugal fractions (12,000 χ g for 30 min at 4°C).…”

Section: Free Fatty Acids and Uht Milk Flavormentioning

confidence: 97%

“…Cause for Increase of Free Fatty Acids in UHT milk The increase of free fatty acids in UHT milk during storage is believed to be caused by heat-resistant lipase (27,22,23). This is either an indigenous milk lipase (milk lipoprotein lipase) or a bacterial lipase produced by psychrotrophic bacteria during cold storage of raw milk (24).…”

Section: Free Fatty Acids and Uht Milk Flavormentioning

confidence: 99%

Flavor Chemistry of Dairy Lipids

Jeon

1994

ACS Symposium Series

View full text Add to dashboard Cite

“…Lipid hydrolysis from residual levels of lipase remaining after heat treatment reduce the shelf life of milk. For example, ; Andersson and others () found that after 22 d at 8 °C, lipase activity can remain at 60% of the postpasteurization level. Many bacterial species, including Pseudomonas spp., produce proteases and lipases (Champagne and other ; Sorhaug and Stepaniak ) that alter the physicochemical, functional, and sensory properties of milk.…”

Section: Introductionmentioning

confidence: 99%

Monitoring Shelf Life of Pasteurized Whole Milk Under Refrigerated Storage Conditions: Predictive Models for Quality Loss

Ziyaina

Govindan

Rasco

et al. 2018

Journal of Food Science

View full text Add to dashboard Cite

show abstract

Effect of a Heat-Resistant Microbial Lipase on Flavor of Ultra-High-Temperature Sterilized Milk

Cited by 33 publications

References 9 publications

Lipase and Protease Double-Deletion Mutant of Pseudomonas fluorescens Suitable for Extracellular Protein Production

Lipase and Protease Double-Deletion Mutant of Pseudomonas fluorescens Suitable for Extracellular Protein Production

Flavor Chemistry of Dairy Lipids

Monitoring Shelf Life of Pasteurized Whole Milk Under Refrigerated Storage Conditions: Predictive Models for Quality Loss

Contact Info

Product

Resources

About