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  • 1
    Electronic Resource
    Electronic Resource
    Hydrolysis of β-casein (193-209) Fragment by Whole Cells and Fractions of Lactobacillus casei and Lactococcus lactis (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 64 (1999), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Whole cells and fractions of Lactococcus lactis subsp. lactis IFPL 359 and Lactobacillus casei subsp. casei IFPL731 were studied. Hydrolysis products were separated by reversed-phase, high-performance liquid chromatography (RPHPLC). Under conditions, pH 5.2 and 3% NaCl, L. casei IFPL 731 was more active in hydrolysis of the b-casein (f193-209) peptide than was L. lactis IFPL 359. This hydrolyzing activity was attributed for L. casei IFPL 731 by the cell-wall proteinase. Hydrolysis of the peptide by the intracellular extract of L. casei IFPL731 was mainly located in the fraction that contained endopeptidase and Pep N aminopeptidase activities. Results may help provide approaches and treatments to control bitterness in cheese products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1999.tb15936.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Process for Low-fat Cheese from Ultrafiltered Milk (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 63 (1998), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Our objective was to optimize the process for making low-fat cheeses using liquid pre-cheeses obtained by ultrafiltration (UF). The study was conducted to examine the effects of using different proportions of cow, sheep, and goat milk in different compositions on the characteristics of cheeses, and to determine the effect of heating of the retentate on texture. Using ultrafiltered semi-skim milk (total protein content of retentate of 13–14%), cheeses with acceptable quality and reduced fat content were produced. Heating of the retentate produced by UF at 68–72°C, 20 s, improved cheese texture.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1998.tb15808.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The aminopeptidase C (PepC) from Lactobacillus helveticus CNRZ32. A comparative study of PepC from lactic acid bacteria (2000)
    Springer
    European food research and technology 212 (2000), S. 89-94 
    Details
    ISSN: 1438-2385
    Keywords: Key words Aminopeptidase C ; Lactobacillus helveticus CNRZ32 ; Lactic acid bacteria ; Enzymatic specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The aminopeptidase C (PepC) of Lactobacillus helveticus CNRZ32 was purified by anion exchange chromatography from cell free extracts of an E. coli DH5α clone overexpressing the Lactobacillus aminopeptidase. PepC was found to have a tetrameric structure in its native form with subunits of 50 kDa each, a pH optimum of 6.5 and maximum activity at 45  °C. Sulfhydryl-blocking reagents inhibited the enzyme activity whereas reducing or metal chelating reagents had an activating effect on the PepC activity. The PepC hydrolyzed a wide range of p-nitroaniline derivatives, dipeptides and several tripeptides which contained basic amino acids (Arg, Lys), Pro residues, or cheese flavour precursor amino acids (Met, Leu, Phe) at the N-terminal position. The substrate specificity and residual activity of PepC from several lactic acid bacteria, including the PepC described above, were compared at conditions of pH and NaCl present in cheese.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002170000203
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  • 4
    Electronic Resource
    Electronic Resource
    Lactococcin A overexpression in a Lactococcus lactis subsp. lactis transformant containing a Tn5 insertion in the lcnD gene (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 413-418 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Lactococcin A production in lactococci has recently been linked to a signal-sequence-independent secretory system consisting of a four-gene cluster. Lactococcus lactis subsp. lactis LLM23L-A1 has been obtained after Tn5 mutagenesis of pLLM23, a plasmid containing the gene cluster responsible for lactococcin A production. In contrast to other Tn5-generated mutants, strain LLM23L-A1 exhibited a 12-fold increase in lactococcin A production. Overproduction of lactococcin A was not linked to an increased pLLM23 copy number. Restriction-enzyme analysis indicated the site of Tn5 insertion to be at the 3′ end of lcnD and upstream of the lcnA structural gene. From DNA sequencing, the Tn5 insertion was located −79 bp upstream of the transcription start site of the lcnA and lciA genes, eliminating eight amino acids from the C-terminal end of lactococcin D. Northern blots revealed overproduction of a 500-base transcript in strain LLM23L-A1, which corresponded to that predicted from the positions of the lactococcin A operon transcriptional start site and the termination structures. This result suggests that the overproduction of lactococcin A in strain LLM23L-A1 is at the transcriptional level and provides further impetus for elucidating the complete regulatory mechanism for lactococcin A expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169937
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  • 5
    Electronic Resource
    Electronic Resource
    Lactococcin A overexpression in a Lactococcus lactis subsp. lactis transformant containing a Tn5 insertion in the lcnD gene (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 413-418 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Lactococcin A production in lactococci has recently been linked to a signal-sequence-independent secretory system consisting of a four-gene cluster. Lactococcus lactis subsp. lactis LLM23L-A1 has been obtained after Tn5 mutagenesis of pLLM23, a plasmid containing the gene cluster responsible for lactococcin A production. In contrast to other Tn5-generated mutants, strain LLM23L-A1 exhibited a 12-fold increase in lactococcin A production. Overproduction of lactococcin A was not linked to an increased pLLM23 copy number. Restriction-enzyme analysis indicated the site of Tn5 insertion to be at the 3′ end of lcnD and upstream of the lcnA structural gene. From DNA sequencing, the Tn5 insertion was located −79 bp upstream of the transcription start site of the lcnA and lciA genes, eliminating eight amino acids from the C-terminal end of lactococcin D. Northern blots revealed overproduction of a 500-base transcript in strain LLM23L-A1, which corresponded to that predicted from the positions of the lactococcin A operon transcriptional start site and the termination structures. This result suggests that the overproduction of lactococcin A in strain LLM23L-A1 is at the transcriptional level and provides further impetus for elucidating the complete regulatory mechanism for lactococcin A expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050575
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  • 6
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    Unknown
    Inactivation of the panE Gene in Lactococcus lactis Enhances Formation of Cheese Aroma Compounds [Food Microbiology] (2013)
    The American Society for Microbiology (ASM)
    Details
    Publication Date: 2013-05-07
    Description: Hydroxyacid dehydrogenases limit the conversion of α-keto acids into aroma compounds. Here we report that inactivation of the panE gene, encoding the α-hydroxyacid dehydrogenase activity in Lactococcus lactis , enhanced the formation of 3-methylbutanal and 3-methylbutanol. L. lactis IFPL953 panE was an efficient strain producing volatile compounds related to cheese aroma.
    Print ISSN: 0099-2240
    Electronic ISSN: 1098-5336
    Topics: Biology
    Published by The American Society for Microbiology (ASM)
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  • 7
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    Identification of two novel mutations in FAM136A and DTNA genes in autosomal-dominant familial Meniere's disease (2015)
    Oxford University Press
    Details
    Publication Date: 2015-01-25
    Description: Meniere's disease (MD) is a chronic disorder of the inner ear defined by sensorineural hearing loss, tinnitus and episodic vertigo, and familial MD is observed in 5–15% of sporadic cases. Although its pathophysiology is largely unknown, studies in human temporal bones have found an accumulation of endolymph in the scala media of the cochlea. By whole-exome sequencing, we have identified two novel heterozygous single-nucleotide variants in FAM136A and DTNA genes, both in a Spanish family with three affected cases in consecutive generations, highly suggestive of autosomal-dominant inheritance. The nonsense mutation in the FAM136A gene leads to a stop codon that disrupts the FAM136A protein product. Sequencing revealed two mRNA transcripts of FAM136A in lymphoblasts from patients, which were confirmed by immunoblotting. Carriers of the FAM136A mutation showed a significant decrease in the expression level of both transcripts in lymphoblastoid cell lines. The missense mutation in the DTNA gene produces a novel splice site which skips exon 21 and leads to a shorter alternative transcript. We also demonstrated that FAM136A and DTNA proteins are expressed in the neurosensorial epithelium of the crista ampullaris of the rat by immunohistochemistry. While FAM136A encodes a mitochondrial protein with unknown function, DTNA encodes a cytoskeleton-interacting membrane protein involved in the formation and stability of synapses with a crucial role in the permeability of the blood–brain barrier. Neither of these genes has been described in patients with hearing loss, FAM136A and DTNA being candidate gene for familiar MD.
    Print ISSN: 0964-6906
    Electronic ISSN: 1460-2083
    Topics: Biology , Medicine
    Published by Oxford University Press
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