Optimization of Enzymatic Activities in Malting of Oat
Malting is usually carried out on intact barley seed,
while hull is still attached to it. In this study, oat grain with and
without hull was subjected to controlled germination to optimize its
enzymes activity, in such a way that lipase has the lowest and α-
amylase and proteinase the highest activities. Since pH has a great
impact on the activity of the enzymes, the pH of germination media
was set up to 3 to 8. In dehulled oats, lipase and α-amylase had the
lowest and highest activities in pHs 3 and 6, respectively whereas the
highest proteinase activity was evidenced at pH 7 and 4 in the oats
with and without hull respectively. While measurements indicated
that the effect of hull on the enzyme activities particularly in lipase
and amylase at each level of the pH are significantly different, the
best results were obtained in those samples in which their hull had
been removed. However, since the similar lipase activity in
germinated dehulled oat were recorded at the pHs 4 and 5, therefore
it was concluded that pH 5 in dehulled oat seed may provide the
optimum enzyme activity for all the enzymes.
[1] G. Mazza, Functional Food: Biochemical & Processing Aspect,
Pennsylvania: Technomic Press, 1998, pp. 1-37
[2] P. Lehtinen, and S. Laakso, "Role of lipid reactions in quality of oat
products, " Agric. Food Sci., vol. 13, no. 1-2, pp. 88-99, 2004.
[3] D. M. Peterson, "Malting oats: Effects on chemical composition of
hull-less and hulled genotypes," Cereal Chem., vol. 75, no. 2, pp.
230-234, 1998.
[4] A. Dalby, and C. Y. Tsai, "Lysine and tryptophan increasing during
germination of cereal grains," Cereal Chem., vol. 53, no. 2, pp. 222-
226, 1976.
[5] M. Larson, and A. S. Sandberg, "Phytate reduction in oats during
malting," J. Food Sci., vol. 57, no. 4, pp. 994-997, 1992.
[6] AACC International, Approved Methods of the American Association
of Cereal Chemist, St. Paul, MN: American Association of Cereal
Chemists, 2000.
[7] C. Y. Ma, "Preparation, composition and functional properties of oat
protein isolated," Can. Inst. Food Sci. Technol. J., vol. 16, no. 3, pp.
[8] B. Sullivan, and H. M. Allison, "Lipase of wheat," J. Amer. Chem.
Soc., vol. 55, no. 1, pp. 320-324, 1933.
[9] A. Bonet, P. A. Caballero, M. Gomes, and C. M. Rossell, "Microbial
transglutaminase as a tool to restore the functionality of gluten from
insect-damage wheat," Cereal Chem., vol. 82, no. 4, pp. 425-430,
2005.
[10] P. M. Nielsen, D. Peterson, and C. Dambman, "Improved method for
determining food protein degree of hydrolysis," J .Food Sci., vol. 66,
no. 5, pp. 642-646, 2001.
[11] AOAC International, Official Methods of Analysis of AOAC
International, 17nd ed., Gaithersburg, MD: Association of Analytical
Communities, 2002.
[12] K. H. Liukkonen, A. Montfoort, and S. V. Laakso, "Water-Induced
lipid changes in oat processing," J. Agric. Food Chem., vol. 40, no. 1,
pp. 126-130, 1992.
[13] D. M. Peterson, "Lipase activity and lipid metabolism during oat
malting," Cereal Chem., vol. 76, no. 1, pp. 159-163, 1999.
[14] B. Ekstrand, I. Gangby, and G. Akesson, "Lipase activity in oats:
Distribution, pH dependence and heat inactivation," Cereal Chem.,
vol. 69, no. 4, pp. 379-381, 1992.
[15] K. H. Liukkonen, K. Johnson, and S. V. Laakso, "Alkaline sensitivity
of lipase activity in oat flour: Factor Contributing to inhibition," J.
Cereal Sci., vol. 21, no. 1, pp. 79-85, 1995.
[16] A. W. McGregor, and J. Daussant, "Evolution of ╬▒ - amylase
component during initial stages of barley germination with and
without prior steeping," Cereal Chem., vol. 56, no. 6, pp. 541-545,
1979.
[17] E. Kneen, "A comparative study of the development of amylases in
germinating cereals," Cereal Chem., vol. 21, pp. 304-313, 1944.
[18] E. Bertoft, C. Andtfolk, and S. E. Kulp, "Effects of pH, temperature
and calcium ions on barley malt ╬▒-amylase isoenzymes," J. Inst.
Brew., vol. 90, no. 5, pp. 298-302, 1984.
[19] P. Meredith, "Inactivation of cereal ╬▒-amylase by brief acidifications:
The pasting strength of wheat flour," Cereal Chem., vol. 47, no. 9, pp.
492-500, 1970.
[20] T. Beta, L. W. Rooney, L. T. Marovatsanga, and R. N. Taylor,
"Effects of chemical treatments on polyphenols and malt quality in
sorghum," J. Cereal Sci., vol. 31, no. 3, pp. 295-302, 2000.
[21] R. Tkachuk, and J. E. Kruger, "Wheat ╬▒- amylase II. Physical
characterization," Cereal Chem., vol. 51, no.4, pp. 508-529, 1974.
[22] N. Zhang, and B. L. Jones, "Characterization of germinated barley
endoproteolytic enzymes by tow-dimensional gel electrophoresis," J.
Cereal Sci., vol. 21, no. 2, pp. 145-153, 1995.
[23] M. Mikola, and B. L. Jones, "Electrophoretic and `in solution`
analyses of endoproteinases extracted from germinated oats," J.
Cereal Sci., vol. 31, no. 1, pp. 145-153, 1998.
[24] M. Mikola, and B. L. Jones, "Characterization of oat endoproteinases
that hydrolyze oat globulins," Cereal Chem., vol. 77, no. 4, pp. 572-
575, 2000.
[25] M. Mikola, and B. L. Jones, "Characterization of oat endoproteinases
that hydrolyze oat avenins," Cereal Chem., vol. 78, no. 1, pp. 55-58,
2001.
[26] N. L. Kent, and A. D. Evers, Technology of Cereals: An Introduction
for Students of Food Science and Agriculture, 4nd ed., Oxford:
Pergamon Press, 1994.
[27] C. Klose, B. D. Schehl, and E. K. Arendt, "Fundamental study on
protein change taking place during malting of oats," J. Cereal Sci.,
vol. 49, no.1 , pp. 83-91, 2009.
[28] A. M. Osman, "The advantages of using natural substrate based on
methods in assessing: The role of synergistic and competitive
interaction of barley malt starch degradation enzymes," J. Inst. Brew.,
vol. 108, no. 2, pp. 204-214, 2002.
[29] S. Kreisz, "Malting, "in Handbook of Brewing: Process, Technology
and Markets, H. M. Eblinger, Ed. Weinheim, Germany: Wiley-VCH
Verlag, 2009, pp. 147-164.
[30] Y. Pomeranz, and H. L. Shands, "Giberlic acid in malting of oats," J.
Food Sci., vol. 39, no. 5, pp. 950-951, 1974.
[31] M. J. Edney, J. K. Eglinton, H. M. Collins, A. R. Barr, W. G. Legge,
and B. G. Rossnagel, "Importance of endosperm modification for malt
wort fermentability," J. Inst. Brew., vol. 113, no. 2, pp. 228-238, 2007.
[32] J. Davidson, "Total and free amylase content of dormant cereals and
related seeds," J. Agric. Res., vol. 70, no. 6, pp. 175-200, 1945.
[33] R. T. Roberts, P. J. Keeney, and T. Wainwright, "The effects of lipids
and related materials on beer foam," J. Inst. Brew., vol. 84, pp. 9-12,
1978.
[34] D. Briggs, C. A. Boulton, P. A. Brookes, and R. Stevens, Brewing:
Science and Practice, Cambridge: Woodhead Publishing, 2004, pp. 1-
18.
[1] G. Mazza, Functional Food: Biochemical & Processing Aspect,
Pennsylvania: Technomic Press, 1998, pp. 1-37
[2] P. Lehtinen, and S. Laakso, "Role of lipid reactions in quality of oat
products, " Agric. Food Sci., vol. 13, no. 1-2, pp. 88-99, 2004.
[3] D. M. Peterson, "Malting oats: Effects on chemical composition of
hull-less and hulled genotypes," Cereal Chem., vol. 75, no. 2, pp.
230-234, 1998.
[4] A. Dalby, and C. Y. Tsai, "Lysine and tryptophan increasing during
germination of cereal grains," Cereal Chem., vol. 53, no. 2, pp. 222-
226, 1976.
[5] M. Larson, and A. S. Sandberg, "Phytate reduction in oats during
malting," J. Food Sci., vol. 57, no. 4, pp. 994-997, 1992.
[6] AACC International, Approved Methods of the American Association
of Cereal Chemist, St. Paul, MN: American Association of Cereal
Chemists, 2000.
[7] C. Y. Ma, "Preparation, composition and functional properties of oat
protein isolated," Can. Inst. Food Sci. Technol. J., vol. 16, no. 3, pp.
[8] B. Sullivan, and H. M. Allison, "Lipase of wheat," J. Amer. Chem.
Soc., vol. 55, no. 1, pp. 320-324, 1933.
[9] A. Bonet, P. A. Caballero, M. Gomes, and C. M. Rossell, "Microbial
transglutaminase as a tool to restore the functionality of gluten from
insect-damage wheat," Cereal Chem., vol. 82, no. 4, pp. 425-430,
2005.
[10] P. M. Nielsen, D. Peterson, and C. Dambman, "Improved method for
determining food protein degree of hydrolysis," J .Food Sci., vol. 66,
no. 5, pp. 642-646, 2001.
[11] AOAC International, Official Methods of Analysis of AOAC
International, 17nd ed., Gaithersburg, MD: Association of Analytical
Communities, 2002.
[12] K. H. Liukkonen, A. Montfoort, and S. V. Laakso, "Water-Induced
lipid changes in oat processing," J. Agric. Food Chem., vol. 40, no. 1,
pp. 126-130, 1992.
[13] D. M. Peterson, "Lipase activity and lipid metabolism during oat
malting," Cereal Chem., vol. 76, no. 1, pp. 159-163, 1999.
[14] B. Ekstrand, I. Gangby, and G. Akesson, "Lipase activity in oats:
Distribution, pH dependence and heat inactivation," Cereal Chem.,
vol. 69, no. 4, pp. 379-381, 1992.
[15] K. H. Liukkonen, K. Johnson, and S. V. Laakso, "Alkaline sensitivity
of lipase activity in oat flour: Factor Contributing to inhibition," J.
Cereal Sci., vol. 21, no. 1, pp. 79-85, 1995.
[16] A. W. McGregor, and J. Daussant, "Evolution of ╬▒ - amylase
component during initial stages of barley germination with and
without prior steeping," Cereal Chem., vol. 56, no. 6, pp. 541-545,
1979.
[17] E. Kneen, "A comparative study of the development of amylases in
germinating cereals," Cereal Chem., vol. 21, pp. 304-313, 1944.
[18] E. Bertoft, C. Andtfolk, and S. E. Kulp, "Effects of pH, temperature
and calcium ions on barley malt ╬▒-amylase isoenzymes," J. Inst.
Brew., vol. 90, no. 5, pp. 298-302, 1984.
[19] P. Meredith, "Inactivation of cereal ╬▒-amylase by brief acidifications:
The pasting strength of wheat flour," Cereal Chem., vol. 47, no. 9, pp.
492-500, 1970.
[20] T. Beta, L. W. Rooney, L. T. Marovatsanga, and R. N. Taylor,
"Effects of chemical treatments on polyphenols and malt quality in
sorghum," J. Cereal Sci., vol. 31, no. 3, pp. 295-302, 2000.
[21] R. Tkachuk, and J. E. Kruger, "Wheat ╬▒- amylase II. Physical
characterization," Cereal Chem., vol. 51, no.4, pp. 508-529, 1974.
[22] N. Zhang, and B. L. Jones, "Characterization of germinated barley
endoproteolytic enzymes by tow-dimensional gel electrophoresis," J.
Cereal Sci., vol. 21, no. 2, pp. 145-153, 1995.
[23] M. Mikola, and B. L. Jones, "Electrophoretic and `in solution`
analyses of endoproteinases extracted from germinated oats," J.
Cereal Sci., vol. 31, no. 1, pp. 145-153, 1998.
[24] M. Mikola, and B. L. Jones, "Characterization of oat endoproteinases
that hydrolyze oat globulins," Cereal Chem., vol. 77, no. 4, pp. 572-
575, 2000.
[25] M. Mikola, and B. L. Jones, "Characterization of oat endoproteinases
that hydrolyze oat avenins," Cereal Chem., vol. 78, no. 1, pp. 55-58,
2001.
[26] N. L. Kent, and A. D. Evers, Technology of Cereals: An Introduction
for Students of Food Science and Agriculture, 4nd ed., Oxford:
Pergamon Press, 1994.
[27] C. Klose, B. D. Schehl, and E. K. Arendt, "Fundamental study on
protein change taking place during malting of oats," J. Cereal Sci.,
vol. 49, no.1 , pp. 83-91, 2009.
[28] A. M. Osman, "The advantages of using natural substrate based on
methods in assessing: The role of synergistic and competitive
interaction of barley malt starch degradation enzymes," J. Inst. Brew.,
vol. 108, no. 2, pp. 204-214, 2002.
[29] S. Kreisz, "Malting, "in Handbook of Brewing: Process, Technology
and Markets, H. M. Eblinger, Ed. Weinheim, Germany: Wiley-VCH
Verlag, 2009, pp. 147-164.
[30] Y. Pomeranz, and H. L. Shands, "Giberlic acid in malting of oats," J.
Food Sci., vol. 39, no. 5, pp. 950-951, 1974.
[31] M. J. Edney, J. K. Eglinton, H. M. Collins, A. R. Barr, W. G. Legge,
and B. G. Rossnagel, "Importance of endosperm modification for malt
wort fermentability," J. Inst. Brew., vol. 113, no. 2, pp. 228-238, 2007.
[32] J. Davidson, "Total and free amylase content of dormant cereals and
related seeds," J. Agric. Res., vol. 70, no. 6, pp. 175-200, 1945.
[33] R. T. Roberts, P. J. Keeney, and T. Wainwright, "The effects of lipids
and related materials on beer foam," J. Inst. Brew., vol. 84, pp. 9-12,
1978.
[34] D. Briggs, C. A. Boulton, P. A. Brookes, and R. Stevens, Brewing:
Science and Practice, Cambridge: Woodhead Publishing, 2004, pp. 1-
18.
@article{"International Journal of Biological, Life and Agricultural Sciences:56986", author = "E. Hosseini and M. Kadivar and M. Shahedi", title = "Optimization of Enzymatic Activities in Malting of Oat", abstract = "Malting is usually carried out on intact barley seed,
while hull is still attached to it. In this study, oat grain with and
without hull was subjected to controlled germination to optimize its
enzymes activity, in such a way that lipase has the lowest and α-
amylase and proteinase the highest activities. Since pH has a great
impact on the activity of the enzymes, the pH of germination media
was set up to 3 to 8. In dehulled oats, lipase and α-amylase had the
lowest and highest activities in pHs 3 and 6, respectively whereas the
highest proteinase activity was evidenced at pH 7 and 4 in the oats
with and without hull respectively. While measurements indicated
that the effect of hull on the enzyme activities particularly in lipase
and amylase at each level of the pH are significantly different, the
best results were obtained in those samples in which their hull had
been removed. However, since the similar lipase activity in
germinated dehulled oat were recorded at the pHs 4 and 5, therefore
it was concluded that pH 5 in dehulled oat seed may provide the
optimum enzyme activity for all the enzymes.", keywords = "Enzyme activity, malting, oat, optimization.", volume = "4", number = "7", pages = "463-6", }
