Production of WGHs and AFPHs using Protease Combinations at High and Ambient Pressure
Wheat gluten hydrolyzates (WGHs) and anchovy fine
powder hydrolyzates (AFPHs) were produced at 300 MPa using
combinations of Flavourzyme 500MG (F), Alcalase 2.4L (A),
Marugoto E (M) and Protamex (P), and then were compared to those
produced at ambient pressure concerning the contents of soluble solid
(SS), soluble nitrogen and electrophoretic profiles. The contents of SS
in the WGHs and AFPHs increased up to 87.2% according to the
increase in enzyme number both at high and ambient pressure. Based
on SS content, the optimum enzyme combinations for one-, two-,
three- and four-enzyme hydrolysis were determined as F, FA, FAM
and FAMP, respectively. Similar trends were found for the contents of
total soluble nitrogen (TSN) and TCA-soluble nitrogen (TCASN). The
contents of SS, TSN and TCASN in the hydrolyzates together with
electrophoretic mobility maps indicates that the high-pressure
treatment of this study accelerated protein hydrolysis compared to
ambient-pressure treatment.
[1] Balny, C. (2006). What lies in the future of high-pressure bioscience?
Biochim. Biophys. Acta 1764:632-639.
[2] Heremans, K. and Smeller, L. (1998). Protein structure and dynamics at
high pressure. Biochim. Biophys. Acta 1386:353-370.
[3] Vila Real, H.J., Alfaia, A.J., Calado, A.R.T., and Ribeiro, M.H.L. (2007).
High pressure temperature effects on enzymatic activity: Naringin
bioconversion. Food Chem. 102:565-570.
[4] Katsaros, G.I., Katapodis, P., and Taoukis, P.S. (2009). High hydrostatic
pressure inactivation kinetics of the plant proteases ficin and papain. J.
Food Eng. 91:42-48.
[5] Borda, D., Indrawati, Smout, C., Van Loey, A., and Hendrickx, M.
(2004). High pressure thermal inactivation of a plasmin system. J. Dairy
Sci. 87:2351-2358.
[6] Kim, N., Maeng, J.-S., and Kim, C.-T. (2013). Effects of medium high
pressure treatments on protease activity. Food Sci. Biotechnol.
22:289-294.
[7] Curl, L. and Jansen, E.F. (1950). The effect of high pressure on pepsin and
chymotrypsinogen. J. Biol. Chem. 185:716-723.
[8] Yaldagard, M., Mortazavi, S.A., and Tabatabaie, F. (2008). The
principles of ultra high pressure technology and its application in food
processing/preservation: A review of microbiological and quality aspects.
Afr. J. Biotechnol. 7:2739-2767.
[9] El Enshasy, H., Abuoul-Enein, A., Helmy, S., and El Azaly, Y. (2008).
Optimization of the industrial production of alkaline protease by Bacillus
licheniformis in different production scales. Aust. J. Basic Appl. Sci.
2:583-589.
[10] Kumar, C.G. and Takagi, H. (1999). Microbial alkaline proteases: from a
bioindustrial viewpoint. Biotechnol. Adv. 17:561-594.
[11] Dayanandan, A., Kanagaraj, J., Sounderraj, L., Govindaraju, R., and
Rajkumar, G.S. (2003). Application of an alkaline protease in leather
processing: an ecofriendly approach. J. Clean. Prod.11:533-536
[12] Gusek, T.W. and Kinsella, J.E. (1987). Purification and characterization
of the heat-stable serine proteinase from Thermomonospora fusca YX.
Biochem. J. 246:511-517.
[13] Sugiura, M., Suzuki, M., Ishikawa, M., and Sasaki, M. (1976).
Pharmaceutical studies on aminopeptidase from Aspergillus japonica. I.
Chem. Pharm. Bull. 24:2286-2293.
[1] Balny, C. (2006). What lies in the future of high-pressure bioscience?
Biochim. Biophys. Acta 1764:632-639.
[2] Heremans, K. and Smeller, L. (1998). Protein structure and dynamics at
high pressure. Biochim. Biophys. Acta 1386:353-370.
[3] Vila Real, H.J., Alfaia, A.J., Calado, A.R.T., and Ribeiro, M.H.L. (2007).
High pressure temperature effects on enzymatic activity: Naringin
bioconversion. Food Chem. 102:565-570.
[4] Katsaros, G.I., Katapodis, P., and Taoukis, P.S. (2009). High hydrostatic
pressure inactivation kinetics of the plant proteases ficin and papain. J.
Food Eng. 91:42-48.
[5] Borda, D., Indrawati, Smout, C., Van Loey, A., and Hendrickx, M.
(2004). High pressure thermal inactivation of a plasmin system. J. Dairy
Sci. 87:2351-2358.
[6] Kim, N., Maeng, J.-S., and Kim, C.-T. (2013). Effects of medium high
pressure treatments on protease activity. Food Sci. Biotechnol.
22:289-294.
[7] Curl, L. and Jansen, E.F. (1950). The effect of high pressure on pepsin and
chymotrypsinogen. J. Biol. Chem. 185:716-723.
[8] Yaldagard, M., Mortazavi, S.A., and Tabatabaie, F. (2008). The
principles of ultra high pressure technology and its application in food
processing/preservation: A review of microbiological and quality aspects.
Afr. J. Biotechnol. 7:2739-2767.
[9] El Enshasy, H., Abuoul-Enein, A., Helmy, S., and El Azaly, Y. (2008).
Optimization of the industrial production of alkaline protease by Bacillus
licheniformis in different production scales. Aust. J. Basic Appl. Sci.
2:583-589.
[10] Kumar, C.G. and Takagi, H. (1999). Microbial alkaline proteases: from a
bioindustrial viewpoint. Biotechnol. Adv. 17:561-594.
[11] Dayanandan, A., Kanagaraj, J., Sounderraj, L., Govindaraju, R., and
Rajkumar, G.S. (2003). Application of an alkaline protease in leather
processing: an ecofriendly approach. J. Clean. Prod.11:533-536
[12] Gusek, T.W. and Kinsella, J.E. (1987). Purification and characterization
of the heat-stable serine proteinase from Thermomonospora fusca YX.
Biochem. J. 246:511-517.
[13] Sugiura, M., Suzuki, M., Ishikawa, M., and Sasaki, M. (1976).
Pharmaceutical studies on aminopeptidase from Aspergillus japonica. I.
Chem. Pharm. Bull. 24:2286-2293.
@article{"International Journal of Biological, Life and Agricultural Sciences:54073", author = "Namsoo Kim and So-Hee Son and Jin-Soo Maeng and Yong-Jin Cho and Chul-Jin Kim and Chong-Tai Kim", title = "Production of WGHs and AFPHs using Protease Combinations at High and Ambient Pressure", abstract = "Wheat gluten hydrolyzates (WGHs) and anchovy fine
powder hydrolyzates (AFPHs) were produced at 300 MPa using
combinations of Flavourzyme 500MG (F), Alcalase 2.4L (A),
Marugoto E (M) and Protamex (P), and then were compared to those
produced at ambient pressure concerning the contents of soluble solid
(SS), soluble nitrogen and electrophoretic profiles. The contents of SS
in the WGHs and AFPHs increased up to 87.2% according to the
increase in enzyme number both at high and ambient pressure. Based
on SS content, the optimum enzyme combinations for one-, two-,
three- and four-enzyme hydrolysis were determined as F, FA, FAM
and FAMP, respectively. Similar trends were found for the contents of
total soluble nitrogen (TSN) and TCA-soluble nitrogen (TCASN). The
contents of SS, TSN and TCASN in the hydrolyzates together with
electrophoretic mobility maps indicates that the high-pressure
treatment of this study accelerated protein hydrolysis compared to
ambient-pressure treatment.", keywords = "Production, Wheat gluten hydrolyzates, Anchovy
fine powder hydrolyzates, Protease combinations.", volume = "7", number = "4", pages = "265-3", }