Determination of the influence of the pH of hydrolysis on enzyme selectivity of Bacillus licheniformis protease towards whey protein isolate

International Dairy Journal

Volumn 44, Issue , 2015, Pages 44-53

  Butré, Claire I ^a   Sforza, Stefano ^a,b   Wierenga, Peter A ^a   Gruppen, Harry ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b UNIVERSITY OF PARMA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; ENZYMES; HYDROLYSIS; PROTEINS;

BACILLUS LICHENIFORMIS; BETA-LACTOGLOBULIN; CLEAVAGE SITES; DEGREE OF HYDROLYSIS; ENZYME SPECIFICITY; PEPTIDE RELEASE; PROTEIN HYDROLYSIS; WHEY PROTEIN ISOLATE;

ENZYMATIC HYDROLYSIS;

BACILLUS LICHENIFORMIS;

EID: 84922352620     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2014.12.007     Document Type: Article

References (18)

1. Adler-Nissen J. Enzymic hydrolysis of food proteins 1986, Elsevier Applied Science Publishers, London, UK.
2. Akpinar O., Penner M.H. Peptidase activity assays using protein substrates. Current protocols in food analytical chemistry 2001, John Wiley & Sons, Corvallis, OR, USA. R.E. Wrolstad (Ed.).
3. Boye J.I., Alli I., Ismail A.A. Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of α-lactalbumin. Journal of Agricultural and Food Chemistry 1997, 45:1116-1125.
4. Breddam K., Meldal M. Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. European Journal of Biochemistry 1992, 206:103-107.
5. Butré C.I., Sforza S., Gruppen H., Wierenga P.A. Introducing enzyme selectivity: a quantitative parameter to describe enzymatic protein hydrolysis. Analytical and Bioanalytical Chemistry 2014, 406:5827-5841.
6. Butré C.I., Sforza S., Gruppen H., Wierenga P.A. Determination of the influence of substrate concentration on the enzyme selectivity using whey protein isolate and Bacillus Licheniformis protease. Journal of Agricultural and Food Chemistry 2014, 62:10230-10239.
7. Butré C.I., Wierenga P.A., Gruppen H. Effects of ionic strength on the enzymatic hydrolysis of diluted and concentrated whey protein isolate. Journal of Agricultural and Food Chemistry 2012, 60:5644-5651.
8. Camacho F., González-Tello P., Guadix E.M. Influence of enzymes, pH and temperature on the kinetics of whey protein hydrolysis. Food Science and Technology International 1998, 4:79-84.
9. Cheison S.C., Leeb E., Toro-Sierra J., Kulozik U. Influence of hydrolysis temperature and pH on the selective hydrolysis of whey proteins by trypsin and potential recovery of native alpha-lactalbumin. International Dairy Journal 2011, 21:166-171.
10. Dubois V., Nedjar-Arroume N., Guillochon D. Influence of pH on the appearance of active peptides in the course of peptic hydrolysis of bovine haemoglobin. Preparative Biochemistry and Biotechnology 2005, 35:85-102.
11. Haug I.J., Skar H.M., Vegarud G.E., Langsrud T., Draget K.I. Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry. Food Hydrocolloids 2009, 23:2287-2293.
12. Huang X.L., Catignani G.L., Swaisgood H.E. Relative structural stabilities of β-lactoglobulins A and B as determined by proteolytic susceptibility and differential scanning calorimetry. Journal of Agricultural and Food Chemistry 1994, 42:1276-1280.
13. Kosters H.A., Wierenga P.A., De Vries R., Gruppen H. Characteristics and effects of specific peptides on heat-induced aggregation of β-lactoglobulin. Biomacromolecules 2011, 12:2159-2170.
14. Kuipers B.J.H., Gruppen H. Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis. Journal of Agricultural and Food Chemistry 2007, 55:5445-5451.
15. Madsen J.S., Qvist K.B. Hydrolysis of milk protein by a Bacillus licheniformis protease specific for acidic amino acid residues. Journal of Food Science 1997, 62:579-582.
16. Mil'gotina E.I., Voyushina T.L., Chestukhina G.G. Glutamyl endopeptidases: structure, function, and practical application. Russian Journal of Bioorganic Chemistry 2003, 29:511-522.
17. Svendsen I., Breddam K. Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis. European Journal of Biochemistry 1992, 204:165-171.
18. Vorob'ev M.M., Dalgalarrondo M., Chobert J.M., Haertlé T. Kinetics of β-casein hydrolysis by wild-type and engineered trypsin. Biopolymers 2000, 54:355-364.