Generation of the antimicrobial peptide caseicin A from casein by hydrolysis with thermolysin enzymes

Guinane, Caitriona M.; Kent, Robert M.; Norberg, Sarah; O’Connor, Paula M.; Cotter, Paul D.; Hill, Colin; Fitzgerald, Gerald F.; Stanton, Catherine; Ross, R. Paul

doi:10.1016/j.idairyj.2015.04.001

Cited by 22 publications

(10 citation statements)

References 32 publications

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“…Potent AMPs have also been isolated from fish and fish products. Hydrolysis of Mackerel by-products yielded SIFIQRFTT which inhibited Listeria innocua and Escherichia coli [ 164 ]. When anchovy cooking waste water was treated with protamix, the AMP GLSRLFTALK was isolated.…”

Section: Food-derived Bioactive Peptides and Human Healthmentioning

confidence: 99%

Bioactive Peptides

Daliri

Lee

2017

Foods

423

254

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The increased consumer awareness of the health promoting effects of functional foods and nutraceuticals is the driving force of the functional food and nutraceutical market. Bioactive peptides are known for their high tissue affinity, specificity and efficiency in promoting health. For this reason, the search for food-derived bioactive peptides has increased exponentially. Over the years, many potential bioactive peptides from food have been documented; yet, obstacles such as the need to establish optimal conditions for industrial scale production and the absence of well-designed clinical trials to provide robust evidence for proving health claims continue to exist. Other important factors such as the possibility of allergenicity, cytotoxicity and the stability of the peptides during gastrointestinal digestion would need to be addressed. This review discusses our current knowledge on the health effects of food-derived bioactive peptides, their processing methods and challenges in their development.

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Section: Food-derived Bioactive Peptides and Human Healthmentioning

confidence: 99%

Bioactive Peptides

Daliri

Lee

2017

Foods

423

254

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“…They can also act as peptide and ester synthetases and can be used for peptide synthesis and the production of a precursor of the artificial sweetener aspartame [ 58 ], and have been used for the hydrolysis of plant cell walls in order to assist in aqueous extraction processes [ 59 ]. Proteases with similar characteristics and molecular weight also showed anti-biofilm activity against pathogenic bacteria such as Listeria monocytogenes , Escherichia coli , and Salmonella typhi [ 49 ] and are potential candidates for the production of bioactive peptides from casein [ 60 ]. Our initial promising results contribute towards the application of protease 32-F38 in industrial and analytical processes.…”

Section: Discussionmentioning

confidence: 99%

Production and Characterization of an Extracellular Acid Protease from Thermophilic Brevibacillus sp. OA30 Isolated from an Algerian Hot Spring

Gomri¹,

Rico-Díaz

Escuder-Rodríguez

et al. 2018

Microorganisms

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Proteases have numerous biotechnological applications and the bioprospection for newly-thermostable proteases from the great biodiversity of thermophilic microorganisms inhabiting hot environments, such as geothermal sources, aims to discover more effective enzymes for processes at higher temperatures. We report in this paper the production and the characterization of a purified acid protease from strain OA30, a moderate thermophilic bacterium isolated from an Algerian hot spring. Phenotypic and genotypic study of strain OA30 was followed by the production of the extracellular protease in a physiologically-optimized medium. Strain OA30 showed multiple extracellular proteolytic enzymes and protease 32-F38 was purified by chromatographic methods and its biochemical characteristics were studied. Strain OA30 was affiliated with Brevibacillus thermoruber species. Protease 32-F38 had an estimated molecular weight of 64.6 kDa and was optimally active at 50 °C. It showed a great thermostability after 240 min and its optimum pH was 6.0. Protease 32-F38 was highly stable in the presence of different detergents and solvents and was inhibited by metalloprotease inhibitors. The results of this work suggest that protease 32-F38 might have interesting biotechnological applications.

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“…This is in contrast to mono-gastric animals, for which it has been suggested that some form of prior processing may be required in order for animals (and humans) to utilise algal proteins more efficiently [164]. Cattle will preferentially drink water containing 20% suspended Spirulina, increasing their daily water intake by 24.8 g/kg [165].…”

Section: Ruminantsmentioning

confidence: 99%

Food Proteins and Bioactive Peptides

2018

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Generation of the antimicrobial peptide caseicin A from casein by hydrolysis with thermolysin enzymes

Cited by 22 publications

References 32 publications

Bioactive Peptides

Bioactive Peptides

Production and Characterization of an Extracellular Acid Protease from Thermophilic Brevibacillus sp. OA30 Isolated from an Algerian Hot Spring

Food Proteins and Bioactive Peptides

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