Hydrolysis of milk-derived bioactive peptides by cell-associated extracellular peptidases of Streptococcus thermophilus

2013 ◽  
Vol 97 (22) ◽  
pp. 9787-9799 ◽  
Author(s):  
Zeeshan Hafeez ◽  
Céline Cakir-Kiefer ◽  
Jean-Michel Girardet ◽  
Julien Jardin ◽  
Clarisse Perrin ◽  
...  
2012 ◽  
Vol 60 (2) ◽  
pp. 554-565 ◽  
Author(s):  
Laurent Miclo ◽  
Émeline Roux ◽  
Magali Genay ◽  
Émilie Brusseaux ◽  
Chantal Poirson ◽  
...  

2020 ◽  
Vol 109 ◽  
pp. 106095 ◽  
Author(s):  
Natalia Estévez ◽  
Pablo Fuciños ◽  
Clara Fuciños ◽  
Paula Jauregi ◽  
Clara A. Tovar ◽  
...  

Processes ◽  
2021 ◽  
Vol 9 (9) ◽  
pp. 1626
Author(s):  
Giselle Franca-Oliveira ◽  
Tiziana Fornari ◽  
Blanca Hernández-Ledesma

In addition to their nutritional and physiological role, proteins are recognized as the major compounds responsible for the rheological properties of food products and their stability during manufacture and storage. Furthermore, proteins have been shown to be source of bioactive peptides able to exert beneficial effects on human health. In recent years, scholarly interest has focused on the incorporation of high-quality proteins into the diet. This fact, together with the new trends of consumers directed to avoid the intake of animal proteins, has boosted the search for novel and sustainable protein sources and the development of suitable, cost-affordable, and environmentally friendly technologies to extract high concentrations of valuable proteins incorporated into food products and supplements. In this review, current data on emergent and promising methodologies applied for the extraction of proteins from natural sources are summarized. Moreover, the advantages and disadvantages of these novel methods, compared with conventional methods, are detailed. Additionally, this work describes the combination of these technologies with the enzymatic hydrolysis of extracted proteins as a powerful strategy for releasing bioactive peptides.


2008 ◽  
Vol 26 (3) ◽  
pp. 339-345 ◽  
Author(s):  
Suman Dhanda ◽  
Jasbir Singh ◽  
Hari Singh

1993 ◽  
Vol 2 (5) ◽  
pp. 395-401
Author(s):  
Zhennai Yang ◽  
Eero Pahkala ◽  
Tuomo Tupasela

To study lactose hydrolysis by β-galactosidase, this enzyme was produced from Streptococcus thermophilus strain 11F and partially purified by acetone and ammonium sulphate fractionation, and ion exchange chromatography on a Q Sepharose FF column. Lactose hydrolysis by the enzyme was affected by lactose concentrations, sugars and milk proteins. The maximum extent of lactose hydrolysis in buffer was obtained with a 15% lactose concentration. Addition of 2% of lactose, glucose, galactose or sucrose in milk inhibited the enzymatic hydrolysis. The enzyme was activated by bovine serum albumin and a combination of αs-casein and β-casein. Of the casein fractions, the principal fraction, αs-casein, was less effective than β-casein and κ-casein. The fibre entrapped enzyme had a temperature optimum of 57°C, and a pH optimum from 7.5 to at least 9.0 with O-nitrophenyl-β-D-galactopyranoside as substrate. By recycling with whey and skim milk through a jacketed glass column (1.6 cm x 30 cm) loaded with fibre-entrapped enzyme at 55°C, a lactose hydrolysis of 49.5% and 47.9% was achieved in 11 h and 7 h respectively.


Sign in / Sign up

Export Citation Format

Share Document