메뉴 건너뛰기




Volumn 56, Issue 3, 2010, Pages 332-342

Determining the safety of enzymes used in animal feed

Author keywords

Animal feed enzymes; Contaminants; Decision tree; Enzymes; Evaluation; Feed additives; Non toxigenic; Production strain; Safe strain lineage; Safety; Specifications

Indexed keywords

ALPHA GALACTOSIDASE; AMYLASE; BETA AMYLASE; BETA FRUCTOFURANOSIDASE; BETA GLUCAN HYDROLASE; BETA GLUCOSIDASE; BETA MANNOSIDASE; BROMELAIN; CATALASE; CELLULASE; ENZYME; FICIN; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLUCOSE OXIDASE; HEMICELLULOSE; KERATINASE; LACTASE; PAPAIN; PEPSIN A; PHYTASE; POLYGALACTURONASE; PROTEINASE; PULLULANASE; TRIACYLGLYCEROL LIPASE; TRYPSIN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 77249154528     PISSN: 02732300     EISSN: 10960295     Source Type: Journal    
DOI: 10.1016/j.yrtph.2009.10.005     Document Type: Article
Times cited : (74)

References (96)
  • 1
    • 77249152372 scopus 로고    scopus 로고
    • AAFCO Official
    • Association of American Feed Control Officials, Publication
    • Association of American Feed Control Officials, 2008. AAFCO Official Publication.
    • (2008)
  • 2
    • 2342468050 scopus 로고    scopus 로고
    • Toxicological studies on lactose oxidase from Microdochium nivale expressed in Fusarium venenatum
    • Ahmad S.K., et al. Toxicological studies on lactose oxidase from Microdochium nivale expressed in Fusarium venenatum. Regul. Toxicol. Pharmacol. 39 (2004) 256-270
    • (2004) Regul. Toxicol. Pharmacol. , vol.39 , pp. 256-270
    • Ahmad, S.K.1
  • 4
    • 77249165728 scopus 로고    scopus 로고
    • Ash, J.A. et al., 2000. The fate of genetically modified protein from Roundup Ready® soybeans in the laying hen. Poult. Sci. (Suppl. 1), 26. Palais de Congrès, Montreal Canada, August 18-21, 2000.
    • Ash, J.A. et al., 2000. The fate of genetically modified protein from Roundup Ready® soybeans in the laying hen. Poult. Sci. (Suppl. 1), 26. Palais de Congrès, Montreal Canada, August 18-21, 2000.
  • 5
    • 0042706451 scopus 로고    scopus 로고
    • The fate of genetically modified protein from Roundup Ready soybeans in laying hens
    • Ash J., Novak C.L., and Scheideler S.E. The fate of genetically modified protein from Roundup Ready soybeans in laying hens. J. Appl. Poult. Res. 12 (2003) 242-245
    • (2003) J. Appl. Poult. Res. , vol.12 , pp. 242-245
    • Ash, J.1    Novak, C.L.2    Scheideler, S.E.3
  • 6
    • 3242703062 scopus 로고    scopus 로고
    • Safety evaluation of an alpha-cyclodextrin glycosyltransferase preparation
    • Bär A., et al. Safety evaluation of an alpha-cyclodextrin glycosyltransferase preparation. Regul. Toxicol. Pharmacol. 39 (2004) S47-S56
    • (2004) Regul. Toxicol. Pharmacol. , vol.39
    • Bär, A.1
  • 7
    • 0026500194 scopus 로고
    • On the safety of Aspergillus oryzae
    • Barbesgaard P., et al. On the safety of Aspergillus oryzae. Appl. Microbiol. Biotechnol. 36 (1992) 569-572
    • (1992) Appl. Microbiol. Biotechnol. , vol.36 , pp. 569-572
    • Barbesgaard, P.1
  • 8
    • 21344433589 scopus 로고
    • Fibrolytic enzymes increase fiber digestibility and growth rate of steers fed dry forages
    • Beauchemin K.A., et al. Fibrolytic enzymes increase fiber digestibility and growth rate of steers fed dry forages. Can. J. Anim. Sci. 75 (1995) 641-644
    • (1995) Can. J. Anim. Sci. , vol.75 , pp. 641-644
    • Beauchemin, K.A.1
  • 9
    • 0031372163 scopus 로고    scopus 로고
    • Effects of fibrolytic enzymes in corn or barley diets on performance and carcass characteristics of feedlot cattle
    • Beauchemin K.A., et al. Effects of fibrolytic enzymes in corn or barley diets on performance and carcass characteristics of feedlot cattle. Can. J. Anim. Sci. 77 (1997) 645-653
    • (1997) Can. J. Anim. Sci. , vol.77 , pp. 645-653
    • Beauchemin, K.A.1
  • 10
    • 0030351537 scopus 로고    scopus 로고
    • The effect of enzymes on digestion
    • Bedford M.R. The effect of enzymes on digestion. J. Appl. Poult. Res. 5 (1996) 370-378
    • (1996) J. Appl. Poult. Res. , vol.5 , pp. 370-378
    • Bedford, M.R.1
  • 11
    • 0033883943 scopus 로고    scopus 로고
    • Exogenous enzymes in monogastric nutrition-their current value and future benefits
    • Bedford M.R. Exogenous enzymes in monogastric nutrition-their current value and future benefits. Anim. Feed Sci. Technol. 86 (2000) 1-13
    • (2000) Anim. Feed Sci. Technol. , vol.86 , pp. 1-13
    • Bedford, M.R.1
  • 12
    • 43049123356 scopus 로고    scopus 로고
    • Advances in laboratory evolution of enzymes
    • Bershtein S., and Tawfik D.S. Advances in laboratory evolution of enzymes. Curr. Opin. Chem. Biol. 12 (2008) 151-158
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 151-158
    • Bershtein, S.1    Tawfik, D.S.2
  • 13
    • 33750727729 scopus 로고    scopus 로고
    • Investigation on possible allergenicity of 19 different commercial enzymes used in the food industry
    • Bindslev-Jensen C., et al. Investigation on possible allergenicity of 19 different commercial enzymes used in the food industry. Food Chem. Toxicol. 44 (2006) 1909-1915
    • (2006) Food Chem. Toxicol. , vol.44 , pp. 1909-1915
    • Bindslev-Jensen, C.1
  • 14
    • 1642385081 scopus 로고    scopus 로고
    • Production of toxic metabolites in Aspergillus niger, Aspergillus oryzae, and Trichoderma reesei: justification of mycotoxin testing in food grade enzyme preparations derived from the three fungi
    • Blumenthal C.Z. Production of toxic metabolites in Aspergillus niger, Aspergillus oryzae, and Trichoderma reesei: justification of mycotoxin testing in food grade enzyme preparations derived from the three fungi. Regul. Toxicol. Pharmacol. 39 (2004) 214-228
    • (2004) Regul. Toxicol. Pharmacol. , vol.39 , pp. 214-228
    • Blumenthal, C.Z.1
  • 16
    • 0036228861 scopus 로고    scopus 로고
    • Toxicological studies on Polyporus pinsitus laccase expressed by Aspergillus oryzae intended in food
    • Brinch D.S., and Pedersen P.B. Toxicological studies on Polyporus pinsitus laccase expressed by Aspergillus oryzae intended in food. Food Addit. Contam. 19 (2002) 323-334
    • (2002) Food Addit. Contam. , vol.19 , pp. 323-334
    • Brinch, D.S.1    Pedersen, P.B.2
  • 17
    • 0036595791 scopus 로고    scopus 로고
    • Toxicological studies on laccase from Myceliophtora thermophilia expressed in Aspergillus oryzae
    • Brinch D.S., and Pedersen P.B. Toxicological studies on laccase from Myceliophtora thermophilia expressed in Aspergillus oryzae. Regul. Toxicol. Pharmacol. 35 (2002) 296-307
    • (2002) Regul. Toxicol. Pharmacol. , vol.35 , pp. 296-307
    • Brinch, D.S.1    Pedersen, P.B.2
  • 18
    • 0042450891 scopus 로고
    • The effect of damaged starch, amylolytic enzymes and proteolytic enzymes on the utilization of cereals by chickens
    • Burnett G.S. The effect of damaged starch, amylolytic enzymes and proteolytic enzymes on the utilization of cereals by chickens. Br. Poult. Sci. 3 (1962) 89-103
    • (1962) Br. Poult. Sci. , vol.3 , pp. 89-103
    • Burnett, G.S.1
  • 19
    • 0042432086 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes: an update
    • Cherry J.R., and Fidantsef A.L. Directed evolution of industrial enzymes: an update. Curr. Opin. Biotechnol. 14 (2003) 438-443
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 438-443
    • Cherry, J.R.1    Fidantsef, A.L.2
  • 20
    • 0037392461 scopus 로고    scopus 로고
    • Safety evaluation of a phytase, expressed in Schizosaccharomyces pombe, intended for use in animal feeds
    • Ciofalo V.N., et al. Safety evaluation of a phytase, expressed in Schizosaccharomyces pombe, intended for use in animal feeds. Regul. Toxicol. Pharmacol. 37 (2003) 286-292
    • (2003) Regul. Toxicol. Pharmacol. , vol.37 , pp. 286-292
    • Ciofalo, V.N.1
  • 21
    • 33646506607 scopus 로고    scopus 로고
    • Safety evaluation of a lipase enzyme preparation, expressed in Pichia pastoris, intended for use in the degumming of edible vegetable oil
    • Ciofalo V., et al. Safety evaluation of a lipase enzyme preparation, expressed in Pichia pastoris, intended for use in the degumming of edible vegetable oil. Regul. Toxicol. Pharmacol. 45 (2006) 1-8
    • (2006) Regul. Toxicol. Pharmacol. , vol.45 , pp. 1-8
    • Ciofalo, V.1
  • 22
    • 77249140140 scopus 로고    scopus 로고
    • Codex Alimentarius Commission, 2004. International Code of Practice on Good Animal Feeding (CAC/RCP 54-2004).
    • Codex Alimentarius Commission, 2004. International Code of Practice on Good Animal Feeding (CAC/RCP 54-2004).
  • 23
    • 2342586720 scopus 로고    scopus 로고
    • Screening of exogenous enzymes for ruminant diets: relationship between biochemical characteristics and in vitro ruminal degradation
    • Colombatto D., et al. Screening of exogenous enzymes for ruminant diets: relationship between biochemical characteristics and in vitro ruminal degradation. J Anim. Sci. 81 (2003) 2628-2638
    • (2003) J Anim. Sci. , vol.81 , pp. 2628-2638
    • Colombatto, D.1
  • 24
    • 0037399660 scopus 로고    scopus 로고
    • Safety evaluation of a hexose oxidase in Hansenula polymorpha
    • Cook M.W., and Thygesen H.V. Safety evaluation of a hexose oxidase in Hansenula polymorpha. Food Chem. Toxicol. 41 (2003) 523-529
    • (2003) Food Chem. Toxicol. , vol.41 , pp. 523-529
    • Cook, M.W.1    Thygesen, H.V.2
  • 25
    • 33745863690 scopus 로고    scopus 로고
    • Association of Manufacturers and Formulators of Enzyme Products (AMFEP), Brussels, Belgium
    • Dauvrin T., et al. Consumer Allergy Risk from Enzyme Residues in Food (1998), Association of Manufacturers and Formulators of Enzyme Products (AMFEP), Brussels, Belgium
    • (1998) Consumer Allergy Risk from Enzyme Residues in Food
    • Dauvrin, T.1
  • 26
    • 0025940355 scopus 로고
    • On the safety of Bacillus subtilis and B. amyloliquefaciens: a review
    • de Boer A.S., and Diderichsen B. On the safety of Bacillus subtilis and B. amyloliquefaciens: a review. Appl. Microbiol. Biotechnol. 36 (1991) 1-4
    • (1991) Appl. Microbiol. Biotechnol. , vol.36 , pp. 1-4
    • de Boer, A.S.1    Diderichsen, B.2
  • 27
    • 0028091411 scopus 로고
    • On the industrial uses of Bacillus licheniformis: a review
    • de Boer A.S., et al. On the industrial uses of Bacillus licheniformis: a review. Appl. Microbiol. Biotechnol. 40 (1994) 595-598
    • (1994) Appl. Microbiol. Biotechnol. , vol.40 , pp. 595-598
    • de Boer, A.S.1
  • 28
    • 0037298581 scopus 로고    scopus 로고
    • Safety evaluation of a glucanase preparation intended for use in food including a subchronic study in rats and mutagenicity studies
    • Elvig S.G., and Pedersen P.B. Safety evaluation of a glucanase preparation intended for use in food including a subchronic study in rats and mutagenicity studies. Regul. Toxicol. Pharmacol. 37 (2003) 11-19
    • (2003) Regul. Toxicol. Pharmacol. , vol.37 , pp. 11-19
    • Elvig, S.G.1    Pedersen, P.B.2
  • 29
    • 77249165208 scopus 로고    scopus 로고
    • FAO (Food and Agricultural Organization), 1981. FAO Food and Nutrition Paper: 25th Session of the Joint FAO/WHO Expert Committee on Food Additives. Appendix A, FAO/WHO, Geneva, Switzerland, pp. 317-318.
    • FAO (Food and Agricultural Organization), 1981. FAO Food and Nutrition Paper: 25th Session of the Joint FAO/WHO Expert Committee on Food Additives. Appendix A, FAO/WHO, Geneva, Switzerland, pp. 317-318.
  • 31
    • 77249130900 scopus 로고    scopus 로고
    • FCC Food Chemicals Codex, Rockville, Maryland
    • FCC (Food Chemicals Codex), 2008. US Pharmacopeia, Rockville, Maryland.
    • (2008) US Pharmacopeia
  • 32
    • 0035005482 scopus 로고    scopus 로고
    • Safety evaluation of lipase produced from Candida rugosa: summary of toxicological data
    • Flood M.T., and Kondo M. Safety evaluation of lipase produced from Candida rugosa: summary of toxicological data. Regul. Toxicol. Pharmacol. 33 (2001) 157-164
    • (2001) Regul. Toxicol. Pharmacol. , vol.33 , pp. 157-164
    • Flood, M.T.1    Kondo, M.2
  • 33
    • 0037394196 scopus 로고    scopus 로고
    • Safety evaluation of lipase produced from Rhizopus oryzae: summary of toxicological data
    • Flood M.T., and Kondo M. Safety evaluation of lipase produced from Rhizopus oryzae: summary of toxicological data. Regul. Toxicol. Pharmacol. 37 (2003) 293-304
    • (2003) Regul. Toxicol. Pharmacol. , vol.37 , pp. 293-304
    • Flood, M.T.1    Kondo, M.2
  • 35
    • 0041737266 scopus 로고
    • Influence of enzyme supplementation and water treatment on the nutritional value of different grains for poults
    • Fry R.E., et al. Influence of enzyme supplementation and water treatment on the nutritional value of different grains for poults. Poult. Sci. 37 (1958) 372-375
    • (1958) Poult. Sci. , vol.37 , pp. 372-375
    • Fry, R.E.1
  • 36
    • 1842525539 scopus 로고    scopus 로고
    • Enhancing the thermal tolerance and gastric performance of a microbial phytase for use as a phosphate-mobilizing monogastric-feed supplement
    • Garrett J.B., et al. Enhancing the thermal tolerance and gastric performance of a microbial phytase for use as a phosphate-mobilizing monogastric-feed supplement. Appl. Environ. Microbiol. 70 (2004) 3041-3046
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3041-3046
    • Garrett, J.B.1
  • 37
    • 77249112892 scopus 로고    scopus 로고
    • GRAS Notice No. 00022, 1999. Alpha-amylase derived from Bacillus licheniformis carrying a gene encoding a modified alpha-amylase derived from Bacillus lichenformis and Bacillus amyloliquefaciens. Available from .
    • GRAS Notice No. 00022, 1999. Alpha-amylase derived from Bacillus licheniformis carrying a gene encoding a modified alpha-amylase derived from Bacillus lichenformis and Bacillus amyloliquefaciens. Available from .
  • 38
    • 77249137379 scopus 로고    scopus 로고
    • GRAS Notice No. 00024, 1999. Alpha-amylase derived from Bacillus licheniformis carrying a gene encoding alpha-amylase from Bacillus stearothermophilus. Available from .
    • GRAS Notice No. 00024, 1999. Alpha-amylase derived from Bacillus licheniformis carrying a gene encoding alpha-amylase from Bacillus stearothermophilus. Available from .
  • 39
    • 77249178374 scopus 로고    scopus 로고
    • GRAS Notice No. 00079, 2001. Alpha-amylase derived from Bacillus licheniformis carrying a gene encoding a modified alpha-amylase from Bacillus licheniformis. Available from .
    • GRAS Notice No. 00079, 2001. Alpha-amylase derived from Bacillus licheniformis carrying a gene encoding a modified alpha-amylase from Bacillus licheniformis. Available from .
  • 40
    • 77249173952 scopus 로고    scopus 로고
    • GRAS Notice No. 00103, 2002. Lipase enzyme preparation from Aspergillus oryzae carrying a gene constructed from a modified Thermomyces lanuginosus lipase gene and a portion of the Fusarium oxysporum lipase gene. Available from .
    • GRAS Notice No. 00103, 2002. Lipase enzyme preparation from Aspergillus oryzae carrying a gene constructed from a modified Thermomyces lanuginosus lipase gene and a portion of the Fusarium oxysporum lipase gene. Available from .
  • 41
    • 77249173441 scopus 로고    scopus 로고
    • Alpha-amylase enzyme preparation from Pseudomonas fluorescens Biovar I expressing a gene encoding a hybrid alpha-amylase derived from three microorganisms within the order Thermococcales. Available from
    • GRAS Notice No. 00126, 2003. Alpha-amylase enzyme preparation from Pseudomonas fluorescens Biovar I expressing a gene encoding a hybrid alpha-amylase derived from three microorganisms within the order Thermococcales. Available from .
    • (2003) GRAS Notice No. 00126
  • 42
    • 77249148512 scopus 로고    scopus 로고
    • GRAS Notice No. 00265, 2008. Glycerophospholipid cholesterol acyltransferase (GCAT) enzyme preparation produced by Bacillus licheniformis expressing the gene encoding GCAT enzyme from Aeromonas salmonicida subsp. Salmonicida (pending review).
    • GRAS Notice No. 00265, 2008. Glycerophospholipid cholesterol acyltransferase (GCAT) enzyme preparation produced by Bacillus licheniformis expressing the gene encoding GCAT enzyme from Aeromonas salmonicida subsp. Salmonicida (pending review).
  • 43
    • 77249085795 scopus 로고    scopus 로고
    • GRAS Notice No. 00277, 2009. G4-amylase enzyme preparation from Bacillus licheniformis expressing the gene encoding a modified maltotetraohydrolase enzyme from Pseudomonas saccharophila (pending review).
    • GRAS Notice No. 00277, 2009. G4-amylase enzyme preparation from Bacillus licheniformis expressing the gene encoding a modified maltotetraohydrolase enzyme from Pseudomonas saccharophila (pending review).
  • 44
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: molecular approaches and industrial applications
    • Gupta R., Beg Q.K., and Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Appl. Microbiol. Biotechnol. 59 (2002) 15-32
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.K.2    Lorenz, P.3
  • 45
    • 0036132752 scopus 로고    scopus 로고
    • Safety evaluation of a xylanase expressed in Bacillus subtilis
    • Harbak L., and Thygesen H.V. Safety evaluation of a xylanase expressed in Bacillus subtilis. Food Chem. Toxicol. 40 (2002) 1-8
    • (2002) Food Chem. Toxicol. , vol.40 , pp. 1-8
    • Harbak, L.1    Thygesen, H.V.2
  • 46
    • 0037912651 scopus 로고
    • Enzyme supplements to poultry feeds
    • Hastings W.H. Enzyme supplements to poultry feeds. Poult. Sci. 25 (1946) 584-586
    • (1946) Poult. Sci. , vol.25 , pp. 584-586
    • Hastings, W.H.1
  • 47
    • 0003185272 scopus 로고
    • Safety Evaluation of foods and food ingredients derived from microorganisms in biotechnologies and food: Assuring the safety of foods produced by genetic modification
    • IFBC International Food Biotechnology Council
    • IFBC (International Food Biotechnology Council), 1990. Safety Evaluation of foods and food ingredients derived from microorganisms in biotechnologies and food: Assuring the safety of foods produced by genetic modification. Regul. Toxicol. Pharmacol. 12, S1-S196.
    • (1990) Regul. Toxicol. Pharmacol , vol.12
  • 49
    • 77249138895 scopus 로고    scopus 로고
    • IUBMB (International Union of Biochemistry and Molecular Biology), 1992. Enzyme Nomenclature: Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes. Academic Press, San Diego, California. Suppl. 1-5 in Eur. J. Biochem. (1994), 223, 1-5; Eur. J. Biochem. (1995) 232, 1-6; Eur. J. Biochem. (1996) 237, 1-5; Eur. J. Biochem. (1997) 250, 1-6; and Eur. J. Biochem. (1999) 264, 610-650; respectively). See also: http://www.chem.qmul.ac.uk/iubmb/enzyme/.
    • IUBMB (International Union of Biochemistry and Molecular Biology), 1992. Enzyme Nomenclature: Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes. Academic Press, San Diego, California. Suppl. 1-5 in Eur. J. Biochem. (1994), 223, 1-5; Eur. J. Biochem. (1995) 232, 1-6; Eur. J. Biochem. (1996) 237, 1-5; Eur. J. Biochem. (1997) 250, 1-6; and Eur. J. Biochem. (1999) 264, 610-650; respectively). See also: http://www.chem.qmul.ac.uk/iubmb/enzyme/.
  • 50
    • 77249129932 scopus 로고    scopus 로고
    • JECFA (Joint FAO/WHO Expert Committee on Food Additives), 2001. Report of the 57th Meeting, Rome, Italy.
    • JECFA (Joint FAO/WHO Expert Committee on Food Additives), 2001. Report of the 57th Meeting, Rome, Italy.
  • 51
    • 77249112394 scopus 로고    scopus 로고
    • Safety evaluations: α-amylase from Bacillus licheniformis containing a genetically engineered α-amylase gene from B. licheniformis. In: Joint FAP/WHO Expert Committee on Food Additives (2003: Rome, Italy) Evaluation of Certain Food Additives and Contaminants: Sixty-First Report of the Joint FAP/WHO Expert Commitee on Food Additives
    • JECFA
    • JECFA, 2004. Safety evaluations: α-amylase from Bacillus licheniformis containing a genetically engineered α-amylase gene from B. licheniformis. In: Joint FAP/WHO Expert Committee on Food Additives (2003: Rome, Italy) Evaluation of Certain Food Additives and Contaminants: Sixty-First Report of the Joint FAP/WHO Expert Commitee on Food Additives. WHO Technical Report Series, vol. 922, pp. 9-11.
    • (2004) WHO Technical Report Series , vol.922 , pp. 9-11
  • 52
    • 77249085317 scopus 로고    scopus 로고
    • Safety evaluations: Xylanases from Bacillus subtilis expressed in B. subtilis. In: Joint FAP/WHO Expert Committee on Food Additives (2004: Geneva, Switzerland) Evaluation of Certain Food Additives: Sixty-Third Report of the Joint FAO/WHO Expert Committee on Food Additives
    • JECFA
    • JECFA, 2005. Safety evaluations: Xylanases from Bacillus subtilis expressed in B. subtilis. In: Joint FAP/WHO Expert Committee on Food Additives (2004: Geneva, Switzerland) Evaluation of Certain Food Additives: Sixty-Third Report of the Joint FAO/WHO Expert Committee on Food Additives. WHO Technical Report Series, vol. 928, pp. 42-45.
    • (2005) WHO Technical Report Series , vol.928 , pp. 42-45
  • 53
    • 0006929436 scopus 로고
    • Improvement in the nutritional value of barley for chicks by enzyme supplementation
    • Jensen L.S., et al. Improvement in the nutritional value of barley for chicks by enzyme supplementation. Poult. Sci. 36 (1957) 919-921
    • (1957) Poult. Sci. , vol.36 , pp. 919-921
    • Jensen, L.S.1
  • 54
    • 33750006508 scopus 로고    scopus 로고
    • Directed evolution: an approach to engineer enzymes
    • Kaur J., and Sharma R. Directed evolution: an approach to engineer enzymes. Crit. Rev. Biotechnol. 26 (2006) 165-199
    • (2006) Crit. Rev. Biotechnol. , vol.26 , pp. 165-199
    • Kaur, J.1    Sharma, R.2
  • 55
    • 42149088826 scopus 로고    scopus 로고
    • Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR
    • Kim M.S., and Lei X.G. Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR. Appl. Microbiol. Biotechnol. 79 (2008) 69-75
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , pp. 69-75
    • Kim, M.S.1    Lei, X.G.2
  • 56
    • 33745159981 scopus 로고    scopus 로고
    • Shifting the pH profile of Aspergillus niger PhyA phytase to match the stomach pH enhances its effectiveness an animal feed additive
    • Kim T., et al. Shifting the pH profile of Aspergillus niger PhyA phytase to match the stomach pH enhances its effectiveness an animal feed additive. Appl. Environ. Microbiol. 72 (2006) 4397-4403
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4397-4403
    • Kim, T.1
  • 57
    • 46549087211 scopus 로고    scopus 로고
    • Assembly of mutations for improving thermostability of Escherichia coli AppA2 phytase
    • Kim M.S., et al. Assembly of mutations for improving thermostability of Escherichia coli AppA2 phytase. Appl. Microbiol. Biotechnol. 79 (2008) 751-758
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , pp. 751-758
    • Kim, M.S.1
  • 58
    • 23244461394 scopus 로고    scopus 로고
    • Effect of grain source and exogenous phytase on phosphorus digestibility in dairy cows
    • Kincaid R.L., et al. Effect of grain source and exogenous phytase on phosphorus digestibility in dairy cows. J. Dairy Sci. 88 (2005) 2893-2902
    • (2005) J. Dairy Sci. , vol.88 , pp. 2893-2902
    • Kincaid, R.L.1
  • 61
    • 34848867309 scopus 로고    scopus 로고
    • Manure nutrient excretion by lactating cows fed exogenous phytase and cellulase
    • Knowlton K.F., et al. Manure nutrient excretion by lactating cows fed exogenous phytase and cellulase. J. Dairy Sci. 90 (2007) 4356-4360
    • (2007) J. Dairy Sci. , vol.90 , pp. 4356-4360
    • Knowlton, K.F.1
  • 62
    • 0035081373 scopus 로고    scopus 로고
    • Safety evaluation of phosphodiesterase produced from Penicillium citrinum: summary of toxicological data
    • Kondo M., et al. Safety evaluation of phosphodiesterase produced from Penicillium citrinum: summary of toxicological data. Regul. Toxicol. Pharmacol. 33 (2001) 2-11
    • (2001) Regul. Toxicol. Pharmacol. , vol.33 , pp. 2-11
    • Kondo, M.1
  • 63
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalysts
    • Kuchner O., and Arnold F.H. Directed evolution of enzyme catalysts. Trends Biotechnol. 15 (1997) 523-530
    • (1997) Trends Biotechnol. , vol.15 , pp. 523-530
    • Kuchner, O.1    Arnold, F.H.2
  • 64
    • 0037298656 scopus 로고    scopus 로고
    • Safety evaluation of an alpha-amylase enzyme preparation derived from the archaeal order Thermococcales as expressed in Pseudomonas fluorescens biovar I
    • Landry T.D., et al. Safety evaluation of an alpha-amylase enzyme preparation derived from the archaeal order Thermococcales as expressed in Pseudomonas fluorescens biovar I. Regul. Toxicol. Pharmacol. 37 (2003) 149-168
    • (2003) Regul. Toxicol. Pharmacol. , vol.37 , pp. 149-168
    • Landry, T.D.1
  • 66
    • 0033963277 scopus 로고    scopus 로고
    • From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase
    • Lehman M., et al. From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. Protein Eng. 13 (2000) 49-57
    • (2000) Protein Eng. , vol.13 , pp. 49-57
    • Lehman, M.1
  • 67
    • 0028924379 scopus 로고
    • Nucleotide sequence and expression of kerA, the gene encoding a keratinolytic protease of Bacillus licheniformis PWD-1
    • Lin X., et al. Nucleotide sequence and expression of kerA, the gene encoding a keratinolytic protease of Bacillus licheniformis PWD-1. Appl. Environ. Microbiol. 61 (1995) 1469-1474
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1469-1474
    • Lin, X.1
  • 68
    • 14644392810 scopus 로고    scopus 로고
    • Degradation of Cry1Ab protein from genetically modified maize in the bovine gastrointestinal tract
    • Lutz B., et al. Degradation of Cry1Ab protein from genetically modified maize in the bovine gastrointestinal tract. J. Agric. Food Chem. 53 (2005) 1453-1456
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 1453-1456
    • Lutz, B.1
  • 69
    • 0242588278 scopus 로고
    • Growth of chicks and turkey poults fed western barley and corn grain-based rations: effects of autoclaving on supplemental enzyme requirement and asymmetry of antibiotic response between grains
    • Moran Jr. E.T., and McGinnis J. Growth of chicks and turkey poults fed western barley and corn grain-based rations: effects of autoclaving on supplemental enzyme requirement and asymmetry of antibiotic response between grains. Poult. Sci. 47 (1968) 152-158
    • (1968) Poult. Sci. , vol.47 , pp. 152-158
    • Moran Jr., E.T.1    McGinnis, J.2
  • 70
    • 0014356144 scopus 로고
    • Effect of phytate on the calcium requirement of chicks
    • Nelson T.S., et al. Effect of phytate on the calcium requirement of chicks. Poult. Sci. 47 (1968) 1985-1989
    • (1968) Poult. Sci. , vol.47 , pp. 1985-1989
    • Nelson, T.S.1
  • 71
    • 0014353867 scopus 로고
    • The availability of phytate phosphorus in soybean meal before and after treatment with a mold phytase
    • Nelson T.S., et al. The availability of phytate phosphorus in soybean meal before and after treatment with a mold phytase. Poult. Sci. 47 (1968) 1842-1848
    • (1968) Poult. Sci. , vol.47 , pp. 1842-1848
    • Nelson, T.S.1
  • 72
    • 0028113146 scopus 로고
    • On the safety of Trichoderma reesei
    • Nevalainen H., et al. On the safety of Trichoderma reesei. J. Biotechnol. 37 (1994) 193-200
    • (1994) J. Biotechnol. , vol.37 , pp. 193-200
    • Nevalainen, H.1
  • 73
    • 0034731354 scopus 로고    scopus 로고
    • Protein engineering of bacterial α-amylases
    • Nielsen J.E., and Borchert T.V. Protein engineering of bacterial α-amylases. Biochim. Biophys. Acta. 1543 (2000) 253-274
    • (2000) Biochim. Biophys. Acta. , vol.1543 , pp. 253-274
    • Nielsen, J.E.1    Borchert, T.V.2
  • 74
    • 0003745722 scopus 로고
    • OECD, Paris, France. Available from:, accessed: 27.10.08
    • OECD, 1992. Safety Considerations for Biotechnology. OECD, Paris, France. Available from: (accessed: 27.10.08.).
    • (1992) Safety Considerations for Biotechnology
  • 75
    • 33747029276 scopus 로고    scopus 로고
    • Food-processing enzymes from recombinant microorganisms - a review
    • Olempska-Beer Z.S., et al. Food-processing enzymes from recombinant microorganisms - a review. Regul. Toxicol. Pharmacol. 45 (2006) 144-158
    • (2006) Regul. Toxicol. Pharmacol. , vol.45 , pp. 144-158
    • Olempska-Beer, Z.S.1
  • 76
    • 2542622107 scopus 로고    scopus 로고
    • Nutritional significance of phytic acid and phytase
    • Pallauf J., and Rimbach G. Nutritional significance of phytic acid and phytase. Arch. Tierernahr. 50 (1997) 301-319
    • (1997) Arch. Tierernahr. , vol.50 , pp. 301-319
    • Pallauf, J.1    Rimbach, G.2
  • 77
    • 0001459597 scopus 로고
    • Determining the safety of enzymes used in food processing
    • Pariza M.W., and Foster E.M. Determining the safety of enzymes used in food processing. J. Food Prot. 46 (1983) 453-468
    • (1983) J. Food Prot. , vol.46 , pp. 453-468
    • Pariza, M.W.1    Foster, E.M.2
  • 78
    • 0035016537 scopus 로고    scopus 로고
    • Evaluating the safety of microbial enzyme preparations used in food processing: update for a new century
    • Pariza M.W., and Johnson E.A. Evaluating the safety of microbial enzyme preparations used in food processing: update for a new century. Regul. Toxicol. Pharmacol. 33 (2001) 173-186
    • (2001) Regul. Toxicol. Pharmacol. , vol.33 , pp. 173-186
    • Pariza, M.W.1    Johnson, E.A.2
  • 79
    • 84971916737 scopus 로고
    • Enzyme supplementation of low or high crude protein concentration diets for broiler chickens
    • Pettersson D., et al. Enzyme supplementation of low or high crude protein concentration diets for broiler chickens. Anim. Prod. 51 (1990) 399-404
    • (1990) Anim. Prod. , vol.51 , pp. 399-404
    • Pettersson, D.1
  • 80
    • 8744284616 scopus 로고    scopus 로고
    • Allergy assessment of foods or ingredients derived from biotechnology, gene-modified organisms, or novel foods
    • Poulsen L.K. Allergy assessment of foods or ingredients derived from biotechnology, gene-modified organisms, or novel foods. Mol. Nutr. Food Res. 48 (2004) 413-423
    • (2004) Mol. Nutr. Food Res. , vol.48 , pp. 413-423
    • Poulsen, L.K.1
  • 81
    • 0001468013 scopus 로고
    • Covalent adducts of DNA and the nonprotein chromophore of neocarzinostatin contain a modified deoxyribose
    • Povrik L.F., and Goldberg I.H. Covalent adducts of DNA and the nonprotein chromophore of neocarzinostatin contain a modified deoxyribose. Proc. Natl. Acad. Sci. USA 79 (1982) 369-373
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 369-373
    • Povrik, L.F.1    Goldberg, I.H.2
  • 82
    • 0037135614 scopus 로고    scopus 로고
    • A novel, high performance enzyme for starch liquefaction: discovery and optimization of a low ph, thermostable α-amylase
    • Richardson T.H., et al. A novel, high performance enzyme for starch liquefaction: discovery and optimization of a low ph, thermostable α-amylase. J. Biol. Chem. 277 (2002) 26501-26507
    • (2002) J. Biol. Chem. , vol.277 , pp. 26501-26507
    • Richardson, T.H.1
  • 83
    • 0034307020 scopus 로고    scopus 로고
    • Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris
    • Rodriguez E., et al. Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris. Arch. Biochem. Biophys. 382 (2000) 105-112
    • (2000) Arch. Biochem. Biophys. , vol.382 , pp. 105-112
    • Rodriguez, E.1
  • 84
    • 77249102735 scopus 로고    scopus 로고
    • Scientific Committee for Food (SCF), 1992. Guidelines for the Presentation of Data on Food Enzymes, 27th Series, Ref. No. EUR14181 EN, pp. 13-22.
    • Scientific Committee for Food (SCF), 1992. Guidelines for the Presentation of Data on Food Enzymes, 27th Series, Ref. No. EUR14181 EN, pp. 13-22.
  • 85
    • 35548976223 scopus 로고    scopus 로고
    • Studies on the non-pathogenicity of Chryseobacterium proteolyticum and on the safety of the enzyme: protein-glutaminase
    • Scheuplein R.J., et al. Studies on the non-pathogenicity of Chryseobacterium proteolyticum and on the safety of the enzyme: protein-glutaminase. Regul. Toxicol. Pharmacol. 49 (2007) 79-89
    • (2007) Regul. Toxicol. Pharmacol. , vol.49 , pp. 79-89
    • Scheuplein, R.J.1
  • 86
    • 0036039911 scopus 로고    scopus 로고
    • On the safety of Aspergillus niger - a review
    • Schuster E., et al. On the safety of Aspergillus niger - a review. Appl. Microbiol. Biotechnol. 59 (2002) 426-435
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 426-435
    • Schuster, E.1
  • 87
    • 36949009858 scopus 로고    scopus 로고
    • Developments in directed evolution for improving enzyme functions
    • Sen S., et al. Developments in directed evolution for improving enzyme functions. Appl. Biochem. Biotechnol. 143 (2007) 212-222
    • (2007) Appl. Biochem. Biotechnol. , vol.143 , pp. 212-222
    • Sen, S.1
  • 88
    • 0033179308 scopus 로고    scopus 로고
    • Protein engineering of alpha-amylase for low pH performance
    • Shaw A., et al. Protein engineering of alpha-amylase for low pH performance. Curr. Opin. Biotechnol. 10 (1999) 349-352
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 349-352
    • Shaw, A.1
  • 89
    • 1942469983 scopus 로고    scopus 로고
    • Safety evaluation of phosphodiesterase derived from Leptographium procerum
    • Steensma A., et al. Safety evaluation of phosphodiesterase derived from Leptographium procerum. Food Chem. Toxicol. 42 (2004) 935-944
    • (2004) Food Chem. Toxicol. , vol.42 , pp. 935-944
    • Steensma, A.1
  • 90
    • 0036204592 scopus 로고    scopus 로고
    • Engineering of phytase for improved activity at low pH
    • Tomschy A., et al. Engineering of phytase for improved activity at low pH. Appl. Environ. Microbiol. 68 (2002) 1907-1913
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1907-1913
    • Tomschy, A.1
  • 92
    • 0038159924 scopus 로고    scopus 로고
    • On the safety of a new generation of DSM Aspergillus niger enzyme production strains
    • van Dijck P.W.M., Selton G.C.M., and Hempenius R.A. On the safety of a new generation of DSM Aspergillus niger enzyme production strains. Regul. Toxicol. Pharmacol. 38 (2003) 27-35
    • (2003) Regul. Toxicol. Pharmacol. , vol.38 , pp. 27-35
    • van Dijck, P.W.M.1    Selton, G.C.M.2    Hempenius, R.A.3
  • 93
    • 0026931216 scopus 로고
    • Peptide absorption: a review of current concepts and future perspectives
    • Webb Jr. K.E., et al. Peptide absorption: a review of current concepts and future perspectives. J. Anim. Sci. 70 (1992) 3248-3257
    • (1992) J. Anim. Sci. , vol.70 , pp. 3248-3257
    • Webb Jr., K.E.1
  • 94
    • 0009236188 scopus 로고    scopus 로고
    • Grower-finisher growth performance and carcass characteristics including attempts to detect transgenic plant DNA and protein in muscle from pigs fed genetically modified "Bt" corn
    • Weber T.E., and Richert B.T. Grower-finisher growth performance and carcass characteristics including attempts to detect transgenic plant DNA and protein in muscle from pigs fed genetically modified "Bt" corn. J. Anim. Sci. 79 Suppl. 2 (2001) 67
    • (2001) J. Anim. Sci. , vol.79 , Issue.SUPPL. 2 , pp. 67
    • Weber, T.E.1    Richert, B.T.2
  • 95
    • 33748760632 scopus 로고    scopus 로고
    • In situ studies on the time-dependent degradation of recombinant corn DNA and protein in the bovine rumen
    • Wiedemann S., et al. In situ studies on the time-dependent degradation of recombinant corn DNA and protein in the bovine rumen. J. Anim. Sci. 84 (2006) 135-144
    • (2006) J. Anim. Sci. , vol.84 , pp. 135-144
    • Wiedemann, S.1
  • 96
    • 0032976125 scopus 로고    scopus 로고
    • Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance
    • Wyss M., et al. Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance. Appl. Environ. Microbiol. 65 (1999) 359-366
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 359-366
    • Wyss, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.