Production of Aminopeptidase from Skim Milk Whey Permeate Medium by Lactobacillus casei ssp. casei

Choi, Hyun Joo; Laleye, L.C.; Amantea, G.F.; Simard, R.E.

doi:10.3168/jds.s0022-0302(96)76446-9

Cited by 10 publications

(6 citation statements)

References 21 publications

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“…2). In this sense, L. acidophilus presented an increase of 0.50 log cycle CFU/mL in Gala apple juice, corroborating the results obtained by Choi et al [35], who verified an increase of 1 log cycle CFU/mL of L. casei in skimmed milk after 24-h fermentation at 30 o C. The authors also verified an increase of 0.8 log cycle CFU/mL of L. acidophilus in MRS broth.…”

Section: Cell Growth (L Casei and L Acidophilus)supporting

confidence: 89%

Development and sensory profile of a probiotic beverage from apple fermented with Lactobacillus casei

Ellendersen

Granato

Guergoletto

et al. 2012

Engineering in Life Sciences

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The objective of this study was the development and optimization of a probiotic apple beverage as well as the establishment of a sensory profile by using chemical, microbiological, and quantitative descriptive analysis (sensory profiling). For this purpose, both Lactobacillus casei and L. acidophilus were tested in two different media ‐ Fuji and Gala apple juices ‐ at different pH values. The optimal conditions to develop the apple probiotic beverage were obtained by response surface methodology. They were found to be 10 h of fermentation at 37oC in Gala apple juice. Sensorially, the clarified Gala apple juice was characterized by a caramel color, apple aroma, and an acidic apple taste. The fresh fermented probiotic apple beverage was characterized by a thick texture and sweet taste. The probiotic apple beverage stored for 28 days at 7oC presented a thick texture and acidic taste. Finally, when the fermented probiotic beverage was tested by potential consumers, it presented an acceptance index of 96%.

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Section: Cell Growth (L Casei and L Acidophilus)supporting

confidence: 89%

Development and sensory profile of a probiotic beverage from apple fermented with Lactobacillus casei

Ellendersen

Granato

Guergoletto

et al. 2012

Engineering in Life Sciences

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“…The absence of aminopeptidase activity in extracellular fraction allowed us to conclude that the studied enzyme is not or little exuded in the extracellular medium by our strains. Membrane and cytoplasm localisations were usually indicated for lactobacilli pepN (Eggimann and Bachmann, 1980;Atlan et al, 1989Atlan et al, , 1990Cholette and Mc Kellar, 1990;Tsakalidou et al, 1993;Choi et al, 1995;Macedo et al, 2003;Pan and Tanokura, 2004). These results are evident because such enzyme plays an important role in cellular nutrition by supplying requisites amino acids for cells growth.…”

Section: Discussionmentioning

confidence: 95%

Specific aminopeptidases of indigenous Lactobacillus brevis and Lactobacillus plantarum

Belkheir¹,

Roudj²,

Karam³

et al. 2012

Afr. J. Biotechnol.

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Lactic acid bacteria play an important role in milk coagulation and cheese ripening. To select strains showing interesting industrial features, two indigenous lactobacilli (Lactobacillus brevis and Lactobacillus plantarum) were studied for aminopeptidase activity. Cell and cells free extract were tested for leucyl aminopeptidase activity on the chromogenic leucyl-p-nitroanilide substrate. Intracellular and membrane enzymes were solubilized with glycine /lyzozyme treatment then purified by ammonium sulphate precipitation followed by Sephadex G100 and diethylaminoethyl (DEAE) ions exchange chromatography's separation. The molecular weight of denatured proteins was estimated on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE). Effects of several parameters, pH, temperature, some ions and inhibitors on purified enzyme activity were studied. Cellular aminopeptidase activity was higher for CHTD 27 strain than BH14 strain. No aminopeptidase activity was noted in the cell free extract. The results of chromatography sephadex G100 combined to those of electrophoresis allowed suggesting a dimer structure for the native enzyme. The Lb CHTD27 purified enzyme showed maximal activity at pH 6.6 and at 40°C. This enzyme was partially inhibited by ethylenediamine acetic acid (EDTA) and Cu 2+ ions but increased by Na 2+ and Co 2+ ions. The aminopeptidase extracted from Lb BH14 was inhibited by EDTA and phenylmethanesulfonylfluoride or phenylmethylsulfonyl fluoride (PMSF), its maximal activity was observed at pH 7.5 and 40°C. In addition to other characteristics as proteolysis and autolysis, in this paper we showed that both studied strains were also able to degrade peptide with specific peptidases which are important characters in cheese manufacturing.

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“…1 9 9 4; K l ei n e t a l. 19 9 4) . Aminopeptidases from lactic acid bacteria are of industrially important since they are widely used in food industry (Pan and Tanokura 2004;Choi et al 1996).…”

Section: Microbial Aminopeptidases-an Overviewmentioning

confidence: 99%

Therapeutic and biotechnological applications of substrate specific microbial aminopeptidases

Nandan

Nampoothiri

2020

Appl Microbiol Biotechnol

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Aminopeptidases (EC 3.4.11.) belongs to exoprotease family, which can catalyze the cleavage of peptide bond which connects the N-terminal amino acid to the penultimate residue in a protein. Aminopeptidases catalyze the process of removal of the Nterminal amino acids of target substrates by sequential cleavage of one amino acid residue at a time. Microbial aminopeptidase are of great acceptance as industrial enzymes with varying applications in food and pharma industry since these enzymes possess unique characteristics than aminopeptidases from other sources. This review describes the various applications of microbial aminopeptidases in different industrial sectors. These enzymes are widely used in food industry as a debittering agent as well as in the preparation of protein hydrolysates. In baking, brewing, and cheese making aminopeptidases are extensively used for removing the bitterness of peptides. The inhibitors of these enzymes are found great clinical applications against various diseases such as cancer, diabetes, and viral infections. Aminopeptidases are widely used for the synthesis of biopeptides and amino acids, and found to be efficient than chemical synthesis. These enzymes are capable of hydrolyzing organophosphate compounds, thus having biological as well as environmental significance. Key Points• Cleaves the amino-terminal amino acid residues from proteins and peptides.• Microbial aminopeptidase are of great acceptance as both therapeutic and industrial enzyme.• Review describes the potential applications of microbial aminopeptidases.

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Production of Aminopeptidase from Skim Milk Whey Permeate Medium by Lactobacillus casei ssp. casei

Cited by 10 publications

References 21 publications

Development and sensory profile of a probiotic beverage from apple fermented with Lactobacillus casei

Development and sensory profile of a probiotic beverage from apple fermented with Lactobacillus casei

Specific aminopeptidases of indigenous Lactobacillus brevis and Lactobacillus plantarum

Therapeutic and biotechnological applications of substrate specific microbial aminopeptidases

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