Hydrolysing protein at home

[Guest guest]

http://www.ingentaconnect.com/content/bsc/jfbc/2007/00000031/00000005/art

00008

HYDROLYSIS OF MAJOR DAIRY PROTEINS BY LACTIC ACID BACTERIA FROM BULGARIAN

YOGURTS

Authors: TZVETKOVA, IRENA; DALGALARRONDO, MICHÈLE1; DANOVA, SVETLA2;

ILIEV, ILIA3; IVANOVA, ISKRA4; CHOBERT, JEAN-MARC; HAERTLÉ, THOMAS1

Source: Journal of Food Biochemistry, Volume 31, Number 5, October 2007 ,

pp. 680-702(23)

Abstract:

Twenty-one Lactobacillus strains isolated from three types of Balkan

homemade yogurts were grown on sodium caseinate, ß-casein or whey

proteins, and the proteolysis was followed by electrophoresis and

reversed-phase high-performance liquid chromatography. The best

conditions allowing obtaining proteolysis without casein precipitation

are 0.8% casein in 50-mM phosphate buffer. The strains tested showed a

relatively high proteolytic activity despite the limited conditions for

bacterial growth. Within 72 and 96?h of incubation, 80-90% of ß-casein

was consumed. They showed also a proteolytic activity toward

a-lactalbumin (ALA), being able to reduce its concentration between 5 and

55%, depending on the strains used. The capacity of the strains to

hydrolyze ß-lactoglobulin was lower as compared with hydrolysis of ALA.

Hydrolysis of casein by all strains produced peptides with an

antibacterial effect against Escherichia coli. Consequently, to obtain a

maximal hydrolysis of the dairy proteins seconded by appearance of

antimicrobial peptides, a combination of strains with different

beneficial properties to be used as starters was proposed. PRACTICAL

APPLICATIONS

Some of the 21 Lactobacillus strains isolated from three types of Balkan

homemade yogurts may be used to proteolyze milk proteins in order to

produce peptides with an antibacterial effect against Escherichia coli.

To obtain a maximal hydrolysis of the dairy proteins seconded by

appearance of antimicrobial peptides, a combination of strains with

different beneficial properties to be used as starters should be

determined. During fermentation process, milk proteins are acidified by

the production of lactic acid and are hydrolyzed by proteases and

peptidases from bacteria. This proteolysis is followed by a reduction of

the number of epitopes and consequently by a decrease in allergenicity of

hydrolyzed proteins. For these reasons, starters as Lactobacillus strains

with beneficial properties able to reduce the allergenicity of fermented

milk products are of great interest for the dairy industry.

Seems like fermenting for a long time, with varied strains, does the

trick.

desh

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[Guest guest]

Ah, but the trick is to make sure that you've got the right strains in

the microbial stew (and this is hard to verify in one's kitchen

without a fancy microbiology and genomics lab). The proteins in kefir

that bother me (casein, others?) definitely are broken down in a 36-48

hour fermentation period - there actually was another paper a year or

so ago that showed L. delbrueckii does a fine job all on its own

(reference escapes me). However, when the microbial stew shifts and

loses those casein-devouring critters, I can tell within a few minutes

of drinking the product. Hence, those who are seriously bothered by

milk proteins (casein most often) tend to (and should) avoid all forms

initially while they are healing their guts.

-jennifer

[Guest guest]

Also, that study I posted says that it took 72-96 hours of incubation to

remove 80-90% of the b-casein. That's way more culturing than even scd

yogurts get.

d

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