Advanced SearchSearch Tips
Usage of Enzyme Substrate to Protect the Activities of Cellulase, Protease and α-Amylase in Simulations of Monogastric Animal and Avian Sequential Total Tract Digestion
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Usage of Enzyme Substrate to Protect the Activities of Cellulase, Protease and α-Amylase in Simulations of Monogastric Animal and Avian Sequential Total Tract Digestion
Wang, H.T.; Hsu, J.T.;
  PDF(new window)
Cellulase from Aspergillus niger, (-amylase from Bacillus sp. and protease from Bacillus globigii were used as enzyme sources in this study to examine how their respective substrates protect them in two kinds of simulated gastrointestinal tract digesting processes. Avian total digest tract simulation test showed that filter paper, Avicel and cellulose resulted in 7.7, 6.4 and 7.4 times more activity than of unprotected cellulose, respectively. Protease with addition of casein, gelatin or soybean protein showed no significant protection response. Starch protected amylase to be 2.5 times activity of the unprotected one. Monogastric animal total tract digestion simulation test showed that filter paper, Avicel and cellulose resulted in 5.9, 9.0 and 8.8 times activity of unprotected cellulase, respectively. Casein, gelatin and soybean protein resulted in 1.2, 1.3 and 2.0 times activity of unprotected protease, respectively. Starch did not protect amylase activity in monogastric animal total tract simulation. Protection of mixed enzymes by substrates in two animal total tract simulation tests showed that filter paper in combination with soybean protein resulted in 1.5 times activity of unprotected cellulose, but all substrates tested showed no significant protection effect to protease. Soybean protein and starch added at the same time protected the amylase activity to be two times of the unprotected one. Test of non-purified substrate protection in two animal total digest tract simulation showed that cellulase activity increased as BSA (bovine serum albumin) concentration increased, with the highest activity to be 1.3 times of unprotected enzyme. However, BSA showed no significant protection effect to protease. Amylase activity increased to 1.5 times as BSA added more than 1.5% (w/v). Cellulase activity increased to 1.5 times as soybean hull was added higher than 1.5%. Amylase had a significant protection response only when soybean hull added up to 2%. Protease activity was not protected by soybean hull to any significant extent.
Enzyme Substrate;Activity Protection;Cellulase;Protease;Amylase;
 Cited by
Characterisation of a Novel White Laccase from the Deuteromycete Fungus Myrothecium verrucaria NF-05 and Its Decolourisation of Dyes, PLoS ONE, 2012, 7, 6, e38817  crossref(new windwow)
7, Bioscience, Biotechnology, and Biochemistry, 2012, 76, 1, 34  crossref(new windwow)
, Aquaculture Nutrition, 2016, 23, 2, 414  crossref(new windwow)
lipase B (CALB) on surface-modified rice husk ashes (RHA) via physical adsorption and cross-linking methods, Biocatalysis and Biotransformation, 2016, 34, 4, 172  crossref(new windwow)
Atallah, M. T. and T. A. Melnik. 1982. Effect of pectin structure on protein utilization by growing rats. J. Nutr. 112:2027-2032

Brock, F. M., C. W. Forsberg and J. C. Buchanan-Smith. 1982. Proteolytic activity of rumen microorganism and effects of proteinase inhibitors. Appl. Environ. Microbiol. 44:561-569

Broderick, G. and W. M. Craig. 1989. Metabolism of peptides and amino acids during in vitro protein degradation by mixed rumen organisms. J. Dairy Sci. 72:2540-2548 crossref(new window)

Fontes, C. M., J. Hall, B. H. Hirst, G. P. Hazlewood and H. J. Gilbert. 1995. The resistance of cellulases and xylanases to proteolytic inactivation. Appl. Microbiol. Biotechnol. 43:52-57 crossref(new window)

Gilkes, N. R., B. Henrissat, D. G. Kilburn, R. C. Miller, Jr. and R. A. Warren. 1991. Domains in microbial beta-1, 4-glycanases: Sequnce conservation, function, and enzyme families. Microbiol. Rev. 55:303-315

Ikedo, S., M. Shimoyamada and K. Watanabe. 1996. Interaction between bovine serum albumin and saponin as studied by heat stability and protease digestion. J. Agric. Food Chem. 44:792-795 crossref(new window)

Ishaaya, I. and Y. Birk. 1965. Soybean saponins. IV. The effect of proteins on the inhibitory activity of soybean saponin on certain enzymes. J. Food Sci. 30:118-126 crossref(new window)

Jin, W. P. 1996. Improvement of cellulase stability by the covalent modification of copolymer of polyalkylene derivative. Biotechnol. Tech. 10:457-462

Kim, Y. Y., B. G. Kim, J. Z. Tian, J. S. Lim, D. Y. Kil, H. Y. Jeon and Y. K. Chung. 2004. Influnces of enzymes complex supplementation on growth, ileal and apparent fecal digestibility and morphology of small intestine in pigs. Asian-Aust. J. Anim. Sci. 17:1729-1735 crossref(new window)

Liener, I. E. 1994. Implications of antinutritional components in soybean foods. Crit. Rev. Food Sci. Nutr. 34:31-67 crossref(new window)

Mangan, J. L. 1972. Quantitative studies on nitrogen metabolism in the bovine rumen. The rate of proteolysis of casein and ovalbumin and the release and metabolism of free amino acids. Br. J. Nutr. 27:261-283 crossref(new window)

McCleary, B. V. and H. Sheehan. 1987. Measurement of cereal $\alpha$-amylase: a new assay procedure. J. Cereal Sci. 6:237-251 crossref(new window)

Olsen, O. and K. K. Thomsen. 1991. Improvement of bacterial beta-glucanase thermostability by glycosylation. J. Gen. Microbiol. 137:579-585 crossref(new window)

Pettersson, D. and P. Aman. 1989. Enzyme supplementation of a poultry diet containing rye and wheat. Br. J. Nutr. 62:139-149 crossref(new window)

Price, K. R., I. T. Johnson and G. R. Fenwick. 1987. The chemistry and biological significance of saponins in foods and feedingstuffs. Crit. Rev. Food. Sci. Nutr. 26:27-135 crossref(new window)

Qiao, S., Y. Wu, C. Lai, L. Gong, W. Lu and D. Li. 2005. Properties of Aspergillar xylanase and the effects of xylanase supplementation in wheat-based diets on growth performance and the blood biochemical valus in broilers. Asian-Aust. J. Anim. Sci. 18:66-74 crossref(new window)

Wood, T. M. and M. Bhat. 1988. Methods for measuring cellulase activities. In (Ed. A. W. Willis and S. T. Kellogg). Methods in Enzymology, v. 160. Academic Press, pp. 87-143