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Volumn 242, Issue 7, 2016, Pages 1005-1012

Batch-to-batch variation and storage stability of the commercial peptidase preparation Flavourzyme in respect of key enzyme activities and its influence on process reproducibility

Author keywords

Aspergillus oryzae peptidases; Batch to batch variation; Commercial enzyme preparation; Flavourzyme; Process reproducibility; Protein hydrolysis

Indexed keywords

ASPERGILLUS; ENZYMES; HYDROLYSIS; INDUSTRIAL RESEARCH; PROTEINS;

EID: 84949498878     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-015-2606-8     Document Type: Article
Times cited : (27)

References (26)
  • 1
    • 84901266680 scopus 로고    scopus 로고
    • Performance of enzymatic wheat gluten hydrolysis in batch and continuous processes using Flavourzyme
    • COI: 1:CAS:528:DC%2BC2cXmt1Gmur0%3D
    • Berends P, Appel D, Eisele T et al (2014) Performance of enzymatic wheat gluten hydrolysis in batch and continuous processes using Flavourzyme. Food Sci Technol 58:534–540
    • (2014) Food Sci Technol , vol.58 , pp. 534-540
    • Berends, P.1    Appel, D.2    Eisele, T.3
  • 2
    • 84929143043 scopus 로고    scopus 로고
    • Continuous long-term hydrolysis of wheat gluten using a principally food-grade enzyme membrane reactor system
    • COI: 1:CAS:528:DC%2BC2MXlsFels7o%3D
    • Merz M, Eisele T, Claaßen W, Appel D, Rabe S, Stressler T, Fischer L (2015) Continuous long-term hydrolysis of wheat gluten using a principally food-grade enzyme membrane reactor system. Biochem Eng J 99:114–123
    • (2015) Biochem Eng J , vol.99 , pp. 114-123
    • Merz, M.1    Eisele, T.2    Claaßen, W.3    Appel, D.4    Rabe, S.5    Stressler, T.6    Fischer, L.7
  • 3
    • 0001070322 scopus 로고    scopus 로고
    • Comparison of the aroma characteristics of acid-hydrolyzed and enzyme-hydrolyzed vegetable proteins produced from soy
    • COI: 1:CAS:528:DyaK1cXnt1Cks7w%3D
    • Aaslyng MD, Elmore JS, Mottram DS (1998) Comparison of the aroma characteristics of acid-hydrolyzed and enzyme-hydrolyzed vegetable proteins produced from soy. J Agric Food Chem 46:5225–5231
    • (1998) J Agric Food Chem , vol.46 , pp. 5225-5231
    • Aaslyng, M.D.1    Elmore, J.S.2    Mottram, D.S.3
  • 4
    • 0032765362 scopus 로고    scopus 로고
    • Production of seafood flavor from red hake (Urophycis chuss) by enzymatic Hydrolysis
    • COI: 1:CAS:528:DyaK1MXjtVSmsrg%3D
    • Imm JY, Lee CM (1999) Production of seafood flavor from red hake (Urophycis chuss) by enzymatic Hydrolysis. J Agric Food Chem 47:2360–2366
    • (1999) J Agric Food Chem , vol.47 , pp. 2360-2366
    • Imm, J.Y.1    Lee, C.M.2
  • 5
    • 43649091361 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme-inhibitory peptides from commercial wet- and dry-milled corn germ
    • COI: 1:CAS:528:DC%2BD1cXjsFGjurk%3D
    • Parris N, Moreau RA, Johnston DB et al (2008) Angiotensin I converting enzyme-inhibitory peptides from commercial wet- and dry-milled corn germ. J Agric Food Chem 56:2620–2623
    • (2008) J Agric Food Chem , vol.56 , pp. 2620-2623
    • Parris, N.1    Moreau, R.A.2    Johnston, D.B.3
  • 6
    • 84894698710 scopus 로고    scopus 로고
    • Optimization of the enzymatic hydrolysis of lupin (Lupinus) proteins for producing ACE-inhibitory peptides
    • COI: 1:CAS:528:DC%2BC2cXhsFeqtb0%3D
    • Boschin G, Scigliuolo GM, Resta D, Arnoldi A (2014) Optimization of the enzymatic hydrolysis of lupin (Lupinus) proteins for producing ACE-inhibitory peptides. J Agric Food Chem 62:1846–1851
    • (2014) J Agric Food Chem , vol.62 , pp. 1846-1851
    • Boschin, G.1    Scigliuolo, G.M.2    Resta, D.3    Arnoldi, A.4
  • 7
    • 67649170643 scopus 로고    scopus 로고
    • Preparation and antioxidative properties of a rapeseed (Brassica napus) protein hydrolysate and three peptide fractions
    • COI: 1:CAS:528:DC%2BD1MXls1Gks7o%3D
    • Xue Z, Yu W, Liu Z, Wu M, Kou X, Wang J (2009) Preparation and antioxidative properties of a rapeseed (Brassica napus) protein hydrolysate and three peptide fractions. J Agric Food Chem 57:5287–5293
    • (2009) J Agric Food Chem , vol.57 , pp. 5287-5293
    • Xue, Z.1    Yu, W.2    Liu, Z.3    Wu, M.4    Kou, X.5    Wang, J.6
  • 8
    • 35549005384 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of brewers’ spent grain proteins and technofunctional properties of the resulting hydrolysates
    • COI: 1:CAS:528:DC%2BD2sXhtV2hsbzL
    • Celus I, Brijs K, Delcour JA (2007) Enzymatic hydrolysis of brewers’ spent grain proteins and technofunctional properties of the resulting hydrolysates. J Agric Food Chem 55:8703–8710
    • (2007) J Agric Food Chem , vol.55 , pp. 8703-8710
    • Celus, I.1    Brijs, K.2    Delcour, J.A.3
  • 9
    • 58149359080 scopus 로고    scopus 로고
    • Radical scavenging and reducing ability of tilapia (Oreochromis niloticus) protein hydrolysates
    • COI: 1:CAS:528:DC%2BD1cXhtF2ju7fN
    • Raghavan S, Kristinsson HG, Leeuwenburgh C (2008) Radical scavenging and reducing ability of tilapia (Oreochromis niloticus) protein hydrolysates. J Agric Food Chem 56:10359–10367
    • (2008) J Agric Food Chem , vol.56 , pp. 10359-10367
    • Raghavan, S.1    Kristinsson, H.G.2    Leeuwenburgh, C.3
  • 10
    • 84935027210 scopus 로고    scopus 로고
    • Flavourzyme, an enzyme preparation with industrial relevance—automated nine-step purification and partial characterization of eight enzymes
    • COI: 1:CAS:528:DC%2BC2MXoslKku7w%3D
    • Merz M, Eisele T, Berends P, Appel D, Rabe S, Blank I, Stressler T, Fischer L (2015) Flavourzyme, an enzyme preparation with industrial relevance—automated nine-step purification and partial characterization of eight enzymes. J Agric Food Chem 63:5682–5693
    • (2015) J Agric Food Chem , vol.63 , pp. 5682-5693
    • Merz, M.1    Eisele, T.2    Berends, P.3    Appel, D.4    Rabe, S.5    Blank, I.6    Stressler, T.7    Fischer, L.8
  • 11
    • 84944323466 scopus 로고    scopus 로고
    • Wheat gluten hydrolysis using isolated Flavourzyme peptidases: product inhibition and determination of synergistic effects using response surface methodology
    • COI: 1:CAS:528:DC%2BC2MXhs1CqtLbL
    • Merz M, Ewert J, Baur C, Appel D, Blank I, Stressler T, Fischer L (2015) Wheat gluten hydrolysis using isolated Flavourzyme peptidases: product inhibition and determination of synergistic effects using response surface methodology. J Mol Catal B Enzym 122:218–226
    • (2015) J Mol Catal B Enzym , vol.122 , pp. 218-226
    • Merz, M.1    Ewert, J.2    Baur, C.3    Appel, D.4    Blank, I.5    Stressler, T.6    Fischer, L.7
  • 12
    • 84973327806 scopus 로고    scopus 로고
    • Accessed 26 May 2015
    • Novozymes (2012) Product data sheet—Flavourzyme 1000L. https://www.ulprospector.com/en/na/Food/Detail/4497/331869/Flavourzyme-1000-L. Accessed 26 May 2015
    • (2012) Product data sheet—Flavourzyme 1000L
  • 13
    • 0034085404 scopus 로고    scopus 로고
    • Growth of filamentous fungi in submerged culture: problems and possible solutions
    • COI: 1:CAS:528:DC%2BD3cXivFWqtro%3D
    • Gibbs PA, Seviour RJ, Schmid F (2000) Growth of filamentous fungi in submerged culture: problems and possible solutions. Crit Rev Biotechnol 20:17–48
    • (2000) Crit Rev Biotechnol , vol.20 , pp. 17-48
    • Gibbs, P.A.1    Seviour, R.J.2    Schmid, F.3
  • 15
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • COI: 1:CAS:528:DyaE1MXlvFWnsbw%3D
    • Adler-Nissen J (1979) Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J Agric Food Chem 27:1256–1262
    • (1979) J Agric Food Chem , vol.27 , pp. 1256-1262
    • Adler-Nissen, J.1
  • 16
    • 84973361505 scopus 로고    scopus 로고
    • Milk and dairy products. In: Belitz HD, Grosch W, Schieberle P (eds) Food chemistry. Springer, Heidelberg
    • Belitz HD, Grosch W, Schieberle P (2009) Milk and dairy products. In: Belitz HD, Grosch W, Schieberle P (eds) Food chemistry. Springer, Heidelberg, pp 498–545
    • (2009) pp 498–545
    • Belitz, H.D.1    Grosch, W.2    Schieberle, P.3
  • 17
    • 0028819302 scopus 로고
    • Azocasein assay for alkaline protease in complex fermentation broth
    • COI: 1:CAS:528:DyaK2MXnslyrs7Y%3D
    • Iversen SL, Jørgensen MH (1995) Azocasein assay for alkaline protease in complex fermentation broth. Biotechnol Tech 9:573–576
    • (1995) Biotechnol Tech , vol.9 , pp. 573-576
    • Iversen, S.L.1    Jørgensen, M.H.2
  • 18
    • 0001743127 scopus 로고
    • Control of storage protein metabolism in the cotyledons of germinating mung beans: role of endopeptidase
    • COI: 1:CAS:528:DyaE2MXksVShu7Y%3D
    • Chrispeels MJ, Boulter D (1975) Control of storage protein metabolism in the cotyledons of germinating mung beans: role of endopeptidase. Plant Physiol 55:1031–1037
    • (1975) Plant Physiol , vol.55 , pp. 1031-1037
    • Chrispeels, M.J.1    Boulter, D.2
  • 19
    • 84880488807 scopus 로고    scopus 로고
    • Characterization of the recombinant exopeptidases PepX and PepN from Lactobacillus helveticus ATCC 12046 important for food protein hydrolysis
    • COI: 1:CAS:528:DC%2BC3sXht1aju7jL
    • Stressler T, Eisele T, Schlayer M, Kutz-Wahl S, Fischer L (2013) Characterization of the recombinant exopeptidases PepX and PepN from Lactobacillus helveticus ATCC 12046 important for food protein hydrolysis. PLoS One 8:e70055
    • (2013) PLoS One , vol.8 , pp. e70055
    • Stressler, T.1    Eisele, T.2    Schlayer, M.3    Kutz-Wahl, S.4    Fischer, L.5
  • 20
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • COI: 1:CAS:528:DyaG38XivFegsw%3D%3D
    • Somogyi M (1952) Notes on sugar determination. J Biol Chem 195:19–23
    • (1952) J Biol Chem , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 21
    • 0000674033 scopus 로고
    • A photometric adaptation of the Somogyi method for the determination of glucose
    • COI: 1:CAS:528:DyaH2cXjtFenuw%3D%3D
    • Nelson N (1944) A photometric adaptation of the Somogyi method for the determination of glucose. J Biol Chem 153:375–379
    • (1944) J Biol Chem , vol.153 , pp. 375-379
    • Nelson, N.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • COI: 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (1970) Cleavage of structural 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
  • 23
    • 0034012213 scopus 로고    scopus 로고
    • Heating greatly speeds Coomassie blue staining and destaining
    • COI: 1:CAS:528:DC%2BD3cXhvVejs78%3D
    • Wong C, Sridhara S, Bardwell JC, Jakob U (2000) Heating greatly speeds Coomassie blue staining and destaining. Biotechniques 28:426–428
    • (2000) Biotechniques , vol.28 , pp. 426-428
    • Wong, C.1    Sridhara, S.2    Bardwell, J.C.3    Jakob, U.4
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • COI: 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0037008441 scopus 로고    scopus 로고
    • Determination of key enzyme activities in commercial peptidase and lipase preparations from microbial or animal sources
    • COI: 1:CAS:528:DC%2BD38Xlt12lur0%3D
    • Kilcawley K, Wilkinson M, Fox P (2002) Determination of key enzyme activities in commercial peptidase and lipase preparations from microbial or animal sources. Enzyme Microb Technol 31:310–320
    • (2002) Enzyme Microb Technol , vol.31 , pp. 310-320
    • Kilcawley, K.1    Wilkinson, M.2    Fox, P.3
  • 26
    • 0034097072 scopus 로고    scopus 로고
    • Characterization and functional properties of rice bran proteins modified by commercial exoproteases and endoproteases
    • COI: 1:CAS:528:DC%2BD3cXivFyhsrk%3D
    • Hamada JS (2000) Characterization and functional properties of rice bran proteins modified by commercial exoproteases and endoproteases. J Food Sci 65:305–310
    • (2000) J Food Sci , vol.65 , pp. 305-310
    • Hamada, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.