Probiotic Potential and Functional Properties of Lactobacillus Reuteri, Lactobacillus Rhamnosus and Lactobacillus Helveticus: A Comparative Study

This study was conducted to evaluate and comparethe probiotic propertiesofLactobacillus helveticusNK1, Lactobacillus rhamnosusF and Lactobacillus reuteriLR1lactobacilli strains.Changes in pH, cell growth, proteolytic activity, antioxidantactivity, and angiotensin-converting enzyme(ACE)inhibitoryactivity were monitored during fermentation ofreconstituted skim milk (RSM) by pure cultures of lactobacilli.Among the tested strains, L. helveticusNK1 showed the highest proteolytic, ACE inhibitoryand antioxidantactivitiesduring milk fermentation,followed by L. rhamnosus F and L. reuteriLR1.The promising capability of all of the lactobacilli strains to release bioactivepeptides from the milk proteins was demonstrated. Keywords: Lactobacillus, probiotic, milk fermentation, bioactive peptides

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Development of Antioxidant and Antihypertensive Properties during Growth of Lactobacillus helveticus, Lactobacillus rhamnosus and Lactobacillus reuteri on Cow’s Milk: Fermentation and Peptidomics Study

Foods ◽

10.3390/foods10010017 ◽

2020 ◽

Vol 10 (1) ◽

pp. 17

Author(s):

Anna V. Begunova ◽

Olga S. Savinova ◽

Olga A. Glazunova ◽

Konstantin V. Moiseenko ◽

Irina V. Rozhkova ◽

...

Keyword(s):

Proteolytic Activity ◽

Lactobacillus Reuteri ◽

Lactobacillus Rhamnosus ◽

Milk Proteins ◽

Ace Inhibition ◽

Fermented Milk ◽

Research Area ◽

Lactobacillus Helveticus ◽

Milk Fermentation ◽

C Terminus

Bioactive peptides derived from milk proteins are an active research area. Exhibiting numerous positive physiological effects on digestive, cardiovascular, immune and nervous systems, these peptides thought to be one of the most promising ingredients for functional food. Generally, these peptides are inactive within the parent proteins and can be liberated during milk fermentation by the specific proteolytic systems of various Lactobacillus spp. Here we present the study of milk fermentation by Lactobacillus helveticus NK1, Lactobacillus rhamnosus F and Lactobacillus reuteri LR1 strains. It was demonstrated that the antioxidant activity of the milk fermented by these strains concomitantly increased with the strains’ proteolytic activity. For the angiotensin I-converting enzyme (ACE) inhibitory activity, the same tendency was not observed. Although the proteolytic activity of L. helveticus NK1 was two times higher than that of L. rhamnosus F, the milk fermented by these strains showed comparable ACE inhibition. The analysis of the peptide profiles of the fermented milk samples allowed us to hypothesize that some previously unreported peptides can be produced by L. rhamnosus F. In addition, it was demonstrated that these potential ACE-inhibiting peptides originated from the C-terminus of αS2-casein.

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Chromatographic Characterization and In Vitro Bioactivity Evaluation of Lactobacillus helveticus Hydrolysates upon Fermentation of Different Substrates

Applied Sciences ◽

10.3390/app11020811 ◽

2021 ◽

Vol 11 (2) ◽

pp. 811

Author(s):

Federica Ianni ◽

Alessandra Anna Altomare ◽

Beniamino T. Cenci-Goga ◽

Francesca Blasi ◽

Luca Grispoldi ◽

...

Keyword(s):

Liquid Chromatography ◽

Proteolytic Activity ◽

Bioactive Peptides ◽

Biological Activities ◽

Skim Milk ◽

Brain Heart Infusion ◽

Starter Cultures ◽

Lactobacillus Helveticus ◽

Food Sources

Among various food sources, milk proteins remain the major vector for functional peptides endowed with several biological activities. Particularly, the proteolytic activity of lactic acid bacteria during milk fermentation has been one of the most followed strategies to produce bioactive peptides. In the present study, the exploration of the activity of several starter cultures, at different fermentation times, was firstly investigated by reversed phase-high performance liquid chromatography. Among the tested strains, Lactobacillus helveticus showed a higher proteolytic activity and it was submitted to further investigations by changing the fermentation substrate (skim milk, brain heart infusion, peptone water) as well as the extraction strategy (trichloroacetic acid vs. glass beads). The chromatographic analyses and the in vitro antioxidant and antihypertensive assays highlighted considerable differences for L. helveticus hydrolysates from different substrates, while a negligible impact by the two extraction protocols emerged. Furthermore, nano-high pressure liquid chromatography coupled with a high resolution mass spectrometry analyzer allowed the preliminary discrimination of fractions from fermented skim milk, likely responsible for the found activity. The obtained results suggest the possibility of varying the fermentation parameters in order to maximize the functional effects of the bioactive peptides.

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Angiotensin I-converting enzyme inhibitory peptides in skim milk fermented with Lactobacillus helveticus 130B4 from camel milk in Inner Mongolia, China

Journal of the Science of Food and Agriculture ◽

10.1002/jsfa.3394 ◽

2008 ◽

Vol 88 (15) ◽

pp. 2688-2692 ◽

Cited By ~ 48

Author(s):

Shuang quan ◽

Harutoshi Tsuda ◽

Taku Miyamoto

Keyword(s):

Inner Mongolia ◽

Skim Milk ◽

Lactobacillus Helveticus ◽

Camel Milk ◽

Converting Enzyme ◽

Angiotensin I ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme

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Draft Genome Sequence of Lactobacillus helveticus Strain Lh 12 Isolated from Natural Whey Starter

Genome Announcements ◽

10.1128/genomea.00139-18 ◽

2018 ◽

Vol 6 (10) ◽

Author(s):

Gaia Bertani ◽

Daniela Bassi ◽

Monica Gatti ◽

Pier Sandro Cocconcelli ◽

Erasmo Neviani

Keyword(s):

Lactic Acid ◽

Genome Sequence ◽

Bioactive Peptides ◽

Draft Genome ◽

Milk Proteins ◽

Lactobacillus Helveticus ◽

Draft Genome Sequence ◽

Content Type ◽

Grana Padano ◽

Grana Padano Cheese

ABSTRACT Lactobacillus helveticus is a lactic acid bacterium widely used in cheese-making and for the production of bioactive peptides from milk proteins. Here, we describe the draft genome sequence and annotation of L. helveticus strain Lh 12 isolated from natural whey starter used in the production of Grana Padano cheese.

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Hydrolysis of Milk Proteins by Microbial Enzymes

Journal of Food Protection ◽

10.4315/0362-028x-43.9.709 ◽

1980 ◽

Vol 43 (9) ◽

pp. 709-712 ◽

Cited By ~ 28

Author(s):

A. GEBRE-EGZIABHER ◽

E. S. HUMBERT ◽

G. BLANKENAGEL

Keyword(s):

Room Temperature ◽

Polyacrylamide Gel Electrophoresis ◽

Whey Proteins ◽

Skim Milk ◽

Milk Proteins ◽

Raw Milk ◽

Incubation Periods ◽

Pure Cultures ◽

Sterilized Milk ◽

Hydrolysis Of

Raw skim milk was incubated at 7 C for 15 days after inoculation with six psychrotrophic bacterial cultures previously isolated from raw milk. Effects of the microbial activities on proteins of milk were evaluated by polyacrylamide gel electrophoresis. Results showed that all psychrotrophs hydrolyzed milk proteins. The K- and β-caseins were most susceptible to proteolysis while the a-casein was less affected. Most of the isolates required extended incubation periods for hydrolysis of the whey proteins. Commercially sterilized milk samples inoculated with pure cultures developed bitterness after 4 days of storage at 7 C when the psychrotrophic count was 2.5 × 106/ml. The addition of 9.8 enzyme units to UHT milk caused a bitter flavor within 28 days at 7 C and in less than 3 days at room temperature. The presence of only 2 units resulted in bitterness in less than 7 days at room temperature.

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