메뉴 건너뛰기




Volumn 133, Issue 4, 2012, Pages 1312-1319

Purification, structural characterization, and technological properties of an aspartyl proteinase from submerged cultures of Mucor mucedo DSM 809

Author keywords

Acid protease; Aspartyl proteinase; Characterization; Milk clotting enzymes; Mucor mucedo; Properties; Purification

Indexed keywords

ACID PROTEASE; ASPARTYL PROTEINASE; MILK-CLOTTING ENZYME; MUCOR MUCEDO; PROPERTIES;

EID: 84859801538     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2012.01.075     Document Type: Article
Times cited : (30)

References (29)
  • 1
    • 0025033985 scopus 로고
    • Effects of glycosylation on the secretion and enzyme activity of Mucor rennin, an aspartic proteinase of Mucor pusillus produced by recombinant yeast
    • Aikawa, J., Yamashita, T., Nishiyama, M., Horinouchi, S., & Beppu, T. (1990). Effects of glycosylation on the secretion and enzyme activity of Mucor rennin, an aspartic proteinase of Mucor pusillus produced by recombinant yeast. Journal of Biological Chemistry, 265, 13955-13959.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 13955-13959
    • Aikawa, J.1    Yamashita, T.2    Nishiyama, M.3    Horinouchi, S.4    Beppu, T.5
  • 2
    • 0001442231 scopus 로고
    • Milk clotting enzyme from Mucor pusillus
    • G. E. Perlman & L. Lorand (Eds.), New York: Academic Press
    • Arima, K., Yu, J., & Iwaski, S. (1970). Milk clotting enzyme from Mucor pusillus. In G. E. Perlman & L. Lorand (Eds.), Methods in enzymology (Vol. 19, pp. 446-459). New York: Academic Press.
    • (1970) Methods in Enzymology , vol.19 , pp. 446-459
    • Arima, K.1    Yu, J.2    Iwaski, S.3
  • 3
    • 0346058040 scopus 로고    scopus 로고
    • Characterization of acidic proteolytic enzymes from Monterey sardine (Sardinops sagax caerulea) viscera
    • DOI 10.1016/j.foodchem.2003.07.008
    • Castillo-Yanez, F. J., Pacheco-Aguilar, R., Garcia-Carreno, F. L., & Navarrete-Del Toro, M. A. (2004). Characterization of acidic proteolytic enzymes from Monterey sardine (Sardinops sagax caerulea) viscera. Food Chemistry, 85, 343-350. (Pubitemid 38067249)
    • (2004) Food Chemistry , vol.85 , Issue.3 , pp. 343-350
    • Castillo-Yanez, F.J.1    Pacheco-Aguilar, R.2    Garcia-Carreno, F.L.3    Navarrete-Del, T.M.D.L.A.4
  • 4
    • 84892302772 scopus 로고    scopus 로고
    • Aspartic proteases in cheese making
    • J. Polaina & A. P. Maccabe (Eds.), Netherlands: Springer
    • Claverie-Martin, F., & Vega-Hernandez, M. C. (2007). Aspartic proteases in cheese making. In J. Polaina & A. P. Maccabe (Eds.), Industrial enzymes (pp. 207-219). Netherlands: Springer.
    • (2007) Industrial Enzymes , pp. 207-219
    • Claverie-Martin, F.1    Vega-Hernandez, M.C.2
  • 5
    • 0030199970 scopus 로고    scopus 로고
    • The upper limits of enzyme thermal stability
    • Daniel, R. M. (1996). The upper limits of enzyme thermal stability. Enzyme and Microbial Technology, 19, 74-79.
    • (1996) Enzyme and Microbial Technology , vol.19 , pp. 74-79
    • Daniel, R.M.1
  • 6
    • 38349120529 scopus 로고    scopus 로고
    • An unusual thermostable aspartic protease from the latex of Ficus racemosa (L.)
    • Devaraj, K. B., Gowda, L. R., & Prakash, V. (2008). An unusual thermostable aspartic protease from the latex of Ficus racemosa (L.). Phytochemistry, 69, 647-655.
    • (2008) Phytochemistry , vol.69 , pp. 647-655
    • Devaraj, K.B.1    Gowda, L.R.2    Prakash, V.3
  • 8
    • 76349099156 scopus 로고    scopus 로고
    • Purification and characterization of hatching enzyme from brine shrimp Artemia salina
    • Fan, T., Wang, J., Yuan, W., Zhong, Q., Shi, Y., & Cong, R. (2010). Purification and characterization of hatching enzyme from brine shrimp Artemia salina. Acta Biochimica et Biophysica Sinica, 42, 165-171.
    • (2010) Acta Biochimica et Biophysica Sinica , vol.42 , pp. 165-171
    • Fan, T.1    Wang, J.2    Yuan, W.3    Zhong, Q.4    Shi, Y.5    Cong, R.6
  • 9
    • 77956154033 scopus 로고    scopus 로고
    • Characterization and cheese-making properties of rennet-like enzyme produced by a local Algerian isolate of Aspergillus niger
    • Fazouane-Naimi, F., Mechakra, A., Abdellaoui, R., Nouani, A., Daga, S. M., Alzouma, A. M., et al. (2010). Characterization and cheese-making properties of rennet-like enzyme produced by a local Algerian isolate of Aspergillus niger. Food Biotechnology, 24, 258-269.
    • (2010) Food Biotechnology , vol.24 , pp. 258-269
    • Fazouane-Naimi, F.1    Mechakra, A.2    Abdellaoui, R.3    Nouani, A.4    Daga, S.M.5    Alzouma, A.M.6
  • 12
    • 0002874342 scopus 로고    scopus 로고
    • B. A. Law (Ed.), Sheffield: Academic Press
    • Harboe, M., & Budtz, P. (1999). In B. A. Law (Ed.), Technology of cheesemaking (pp. 33-65). Sheffield: Academic Press.
    • (1999) Technology of Cheesemaking , pp. 33-65
    • Harboe, M.1    Budtz, P.2
  • 14
    • 84859806409 scopus 로고    scopus 로고
    • June
    • K2d software: http://www.embl.de/~andrade/k2d (June, 2011).
    • (2011) K2d Software
  • 15
    • 38849160976 scopus 로고    scopus 로고
    • Purification of extracellular acid protease and analysis of fermentation metabolites by Synergistes sp. utilizing proteinaceous solid waste from tanneries
    • DOI 10.1016/j.biortech.2007.05.001, PII S0960852407004154
    • Kumar, G. A., Nagesh, N., Prabhakar, T. G., & Sekaran, G. (2008). Purification of extracellular acid protease and analysis of fermentation metabolites by Synergistes sp. utilizing proteinaceous solid waste from tanneries. Bioresourse Technology, 99, 2364-2372. (Pubitemid 351208498)
    • (2008) Bioresource Technology , vol.99 , Issue.7 , pp. 2364-2372
    • Kumar, A.G.1    Nagesh, N.2    Prabhakar, T.G.3    Sekaran, G.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0019322201 scopus 로고
    • Kinetic studies on the action of Mucor pusillus, Mucor miehei acid protease and chymosins A and B on a synthetic chromophoric hexapeptide
    • Martin, P., Raymond, M. N., Bricas, E., & Ribadeau Dumas, B. (1980). Kinetic studies on the action of Mucor pusillus, Mucor miehei acid protease and chymosins A and B on a synthetic chromophoric hexapeptide. Biochimica Biophysica Acta, 612, 410-420.
    • (1980) Biochimica Biophysica Acta , vol.612 , pp. 410-420
    • Martin, P.1    Raymond, M.N.2    Bricas, E.3    Ribadeau Dumas, B.4
  • 18
    • 84859797467 scopus 로고    scopus 로고
    • June
    • NCBI protein database: http://www.ncbi.nlm.nih.gov/ (June, 2011).
    • (2011) NCBI Protein Database
  • 20
    • 0016188918 scopus 로고
    • Structural and functional determinants of Mucor miehei protease. IV. Nitration and spectrophotometric titration of tyrosine residues
    • Rickert, W. S., & McBridge-Warren, P. A. (1974). Structural and functional determinants of Mucor miehei protease. IV. Nitration and spectrophotometric titration of tyrosine residues. Biochimica et Biophysica Acta, 371, 368-378.
    • (1974) Biochimica et Biophysica Acta , vol.371 , pp. 368-378
    • Rickert, W.S.1    McBridge-Warren, P.A.2
  • 23
    • 0034870511 scopus 로고    scopus 로고
    • Advances in the study of proteolysis during cheese ripening
    • DOI 10.1016/S0958-6946(01)00062-0, PII S0958694601000620
    • Sousa, M. J., Ardo, Y., & McSweeney, P. L. H. (2001). Advances in the study of proteolysis during cheese ripening. International Dairy Journal, 11, 327-345. (Pubitemid 32752173)
    • (2001) International Dairy Journal , vol.11 , Issue.4-7 , pp. 327-345
    • Sousa, M.J.1    Ardo, Y.2    McSweeney, P.L.H.3
  • 24
    • 84859806410 scopus 로고
    • Differential thermal inactivation analysis of calf rennets
    • Turk, R. S., Watkins, A. S., & Blair, G. T. (1990). Differential thermal inactivation analysis of calf rennets. Journal of Dairy Science, 73, 2000-2006.
    • (1990) Journal of Dairy Science , vol.73 , pp. 2000-2006
    • Turk, R.S.1    Watkins, A.S.2    Blair, G.T.3
  • 25
  • 27
    • 0010627348 scopus 로고
    • The use of principal component analysis to study the relationship between physical/chemical properties and milk-clotting to proteolytic activity ratio of some aspartyl proteinases
    • Yada, R. Y., & Nakai, S. (1986). The use of principal component analysis to study the relationship between physical/chemical properties and milk-clotting to proteolytic activity ratio of some aspartyl proteinases. Journal of Agricultural and Food Chemistry, 34, 675-679.
    • (1986) Journal of Agricultural and Food Chemistry , vol.34 , pp. 675-679
    • Yada, R.Y.1    Nakai, S.2
  • 28
    • 77958006953 scopus 로고    scopus 로고
    • Production of extracellular aspartic protease in submerged fermentation with Mucor mucedo DSM 809
    • Yegin, S., Fernandez-Lahore, M., Guvenc, U., & Goksungur, Y. (2010). Production of extracellular aspartic protease in submerged fermentation with Mucor mucedo DSM 809. African Journal of Biotechnology, 9, 6380-6386.
    • (2010) African Journal of Biotechnology , vol.9 , pp. 6380-6386
    • Yegin, S.1    Fernandez-Lahore, M.2    Guvenc, U.3    Goksungur, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.