scholarly journals Proline iminopeptidase PepI overexpressingLactobacillus caseias an adjunct starter in Edam cheese

Bioengineered ◽  
2013 ◽  
Vol 4 (6) ◽  
pp. 408-412 ◽  
Author(s):  
Sahar Navidghasemizad ◽  
Timo M Takala ◽  
Tapani Alatossava ◽  
Per EJ Saris
Keyword(s):  
Proline Iminopeptidase

scholarly journals Preparation of Antioxidant Enzymatic Hydrolysates from Honeybee-Collected Pollen Using Plant Enzymes

2010 ◽  
Vol 2010 ◽  
pp. 1-5 ◽  
Author(s):  
Margarita D. Marinova ◽  
Bozhidar P. Tchorbanov
Keyword(s):  
Radical Scavenging ◽  
Total Phenolic ◽  
Degree Of Hydrolysis ◽  
Enzymatic Hydrolysates ◽  
Phenolic Contents ◽  
Scavenging Capacity ◽  
Plant Enzymes ◽  
Hydrolysis Of ◽  
Proline Iminopeptidase ◽  
Dietary Food

Enzymatic hydrolysates of honeybee-collected pollen were prepared using food-grade proteinase and aminopeptidases entirely of plant origin. Bromelain from pineapple stem was applied (8 mAU/g substrate) in the first hydrolysis stage. Aminopeptidase (0.05 U/g substrate) and proline iminopeptidase (0.03 U/g substrate) from cabbage leaves (Brassica oleracea var. capitata), and aminopeptidase (0.2 U/g substrate) from chick-pea cotyledons (Cicer arietinum L.) were involved in the additional hydrolysis of the peptide mixtures. The degree of hydrolysis (DH), total phenolic contents, and protein contents of these hydrolysates were as follows: DH (about 20–28%), total phenolics (15.3–27.2 μg/mg sample powder), and proteins (162.7–242.8 μg/mg sample powder), respectively. The hydrolysates possessed high antiradical scavenging activity determined with DPPH (42–46% inhibition). The prepared hydrolysates of bee-collected flower pollen may be regarded as effective natural and functional dietary food supplements due to their remarkable content of polyphenol substances and significant radical-scavenging capacity with special regard to their nutritional-physiological implications.

Purification and Properties of a Proline Iminopeptidase from Apricot Seeds

1982 ◽  
Vol 92 (2) ◽  
pp. 413-421 ◽  
Author(s):  
Kazuto NINOMIYA ◽  
Keiko KAWATANI ◽  
Shuji TANAKA ◽  
Shuji KAWATA ◽  
Satoru MAKISUMI
Keyword(s):  
Purification And Properties ◽  
Proline Iminopeptidase

Use of PCR-Based Methods for Rapid Differentiation of Lactobacillus delbrueckii subsp.bulgaricus and L. delbrueckii subsp.lactis

1999 ◽  
Vol 65 (10) ◽  
pp. 4351-4356 ◽  
Author(s):  
Sandra Torriani ◽  
Giacomo Zapparoli ◽  
Franco Dellaglio
Keyword(s):  
Numerical Analysis ◽  
Dairy Products ◽  
Lactobacillus Delbrueckii ◽  
Randomly Amplified Polymorphic Dna ◽  
Specific Pcr ◽  
Single Colony ◽  
Rapd Pcr ◽  
Reliable Differentiation ◽  
Dna Pcr ◽  
Proline Iminopeptidase

ABSTRACT Two PCR-based methods, specific PCR and randomly amplified polymorphic DNA PCR (RAPD-PCR), were used for rapid and reliable differentiation of Lactobacillus delbrueckii subsp.bulgaricus and L. delbrueckii subsp.lactis. PCR with a single combination of primers which targeted the proline iminopeptidase (pepIP) gene ofL. delbrueckii subsp. bulgaricus allowed amplification of genomic fragments specific for the two subspecies when either DNA from a single colony or cells extracted from dairy products were used. A numerical analysis of the RAPD-PCR patterns obtained with primer M13 gave results that were consistent with the results of specific PCR for all strains except L. delbrueckii subsp.delbrueckii LMG 6412T, which clustered withL. delbrueckii subsp. lactis strains. In addition, RAPD-PCR performed with primer 1254 provided highly polymorphic profiles and thus was superior for distinguishing individual L. delbrueckii strains.

Effect of membrane perturbing treatments on the membrane-bound peptidases ofStreptococcus cremorisHP

1979 ◽  
Vol 46 (3) ◽  
pp. 473-484 ◽  
Author(s):  
Fred A. Exterkate
Keyword(s):  
Intact Cells ◽  
Irreversible Inhibition ◽  
Alkaline Conditions ◽  
Membrane Bound ◽  
Functional Peptide ◽  
Solvent Molecules ◽  
And Storage ◽  
No Activation ◽  
Proline Iminopeptidase

SummaryThe effects of solubilization, treatment with organic solvents and storage under alkaline conditions on membrane-associated peptidases of intact cells ofStreptococcus cremorisHP were studied. Differences in the response of the peptidase activities towards these membrane perturbing treatments were observed. Pyrrolidonecarboxylylpeptidase (PCP) and an endopeptidase (P50) showed 50% irreversible inhibition at the same concentration of each solvent tested. An amino- and proline iminopeptidase activity and the endopeptidase P37were in this respect much more sensitive to the action of the solvents. Within a homologous series of n-alkanols irreversible inhibition of PCP showed a dependence on the hydrophobicity of the solvent molecules. Only P37activity was increased considerably upon solubilization of the enzyme. Similar levels of activation were found upon treatment of cells with 3% (v/v) n-butanol at 25 °C or storage at 30 °C at an alkaline pH. Optimal activity of P50during n-butanol treatment was at 25 °C using a concentration of 5% (v/v), but no activation was observed upon solubilization. The results are discussed in terms of enzyme–lipid interaction and accessibility of the enzymes in situ. It is concluded that the enzymes apparently occupy different positions within the membrane although they may together constitute a functional peptide-hydrolysing unit.

Tricorn protease (TRI) interacting factor 1 fromThermoplasma acidophilumis a proline iminopeptidase

FEBS Letters ◽  
1996 ◽  
Vol 398 (1) ◽  
pp. 101-105 ◽  
Author(s):  
Tomohiro Tamura ◽  
Noriko Tamura ◽  
Friedrich Lottspeich ◽  
Wolfgang Baumeister
Keyword(s):  
Proline Iminopeptidase

scholarly journals Purification and characterization of an extracellular proline iminopeptidase fromArthrobacter nicotianae9458

1999 ◽  
Vol 178 (1) ◽  
pp. 191-197 ◽  
Author(s):  
Emanuele Smacchi ◽  
Marco Gobbetti ◽  
Rosalba Lanciotti ◽  
Patrick F. Fox
Keyword(s):  
Purification And Characterization ◽  
Proline Iminopeptidase

scholarly journals Proline iminopeptidase from the outer cell envelope of the human oral spirochete Treponema denticola ATCC 35405.

1996 ◽  
Vol 64 (3) ◽  
pp. 702-708 ◽  
Author(s):  
K K Mäkinen ◽  
C Y Chen ◽  
P L Mäkinen
Keyword(s):  
Cell Envelope ◽  
Treponema Denticola ◽  
Outer Cell ◽  
Proline Iminopeptidase

Purification and characterization of proline iminopeptidase from Lyophyllum cinerascens

1989 ◽  
Vol 68 (3) ◽  
pp. 178-182 ◽  
Author(s):  
A.K.M. Abdus Sattar ◽  
Tadashi Yoshimoto ◽  
Daisuke Tsuru
Keyword(s):  
Purification And Characterization ◽  
Proline Iminopeptidase
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