메뉴 건너뛰기




Volumn 90, Issue 5, 2010, Pages 729-734

Stability of hydroperoxide lyase activity from Amaranthus tricolor (Amaranthus mangostanus L.) leaves: Influence of selected additives

Author keywords

Additives; Amaranthus tricolor; Hydroperoxide lyase; Stabilisation

Indexed keywords

CYTOCHROME P450; FLAVORING AGENT; GLYCEROL; GLYCINE; HYDROPEROXIDE LYASE; LYASE; SUCROSE; TREHALOSE; VEGETABLE PROTEIN;

EID: 77649290930     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.3874     Document Type: Article
Times cited : (10)

References (37)
  • 2
    • 0035800894 scopus 로고    scopus 로고
    • Fatty acid hydroperoxide lyase: A plant cytochrome P450 enzyme involved in wound healing and pest resistance
    • Noordermeer MA, Veldink GA and Vliegenthart J-FG, Fatty acid hydroperoxide lyase: a plant cytochrome P450 enzyme involved in wound healing and pest resistance. ChemBioChem 2:494-504 (2001).
    • (2001) Chembiochem , vol.2 , pp. 494-504
    • Noordermeer, M.A.1    Veldink, G.A.2    Vliegenthart, J.-F.G.3
  • 3
    • 0343193114 scopus 로고    scopus 로고
    • Cytochrome P450-dependent metabolism of oxylipins in tomato cloning and expression of allene oxide synthase and fatty acid hydroperoxide lyase
    • Howe GA, Lee GI, Itoh A, Li L and DeRocher AD, Cytochrome P450-dependent metabolism of oxylipins in tomato cloning and expression of allene oxide synthase and fatty acid hydroperoxide lyase. Plant Physiol 123:711-724 (2000).
    • (2000) Plant Physiol , vol.123 , pp. 711-724
    • Howe, G.A.1    Lee, G.I.2    Itoh, A.3    Li, L.4    Derocher, A.D.5
  • 4
    • 0142229557 scopus 로고    scopus 로고
    • Characterization of a hydroperoxide lyase gene and effect of C6-volatiles on expression of genes of the oxylipin metabolism in citrus
    • Gomi K, Yamasaki Y, Yamamoto H and Akimitsu K, Characterization of a hydroperoxide lyase gene and effect of C6-volatiles on expression of genes of the oxylipin metabolism in citrus. J Plant Physiol 160:1219-1231 (2003).
    • (2003) J Plant Physiol , vol.160 , pp. 1219-1231
    • Gomi, K.1    Yamasaki, Y.2    Yamamoto, H.3    Akimitsu, K.4
  • 5
    • 4043071354 scopus 로고    scopus 로고
    • Recombinant lipoxygenases and oxylipin metabolism in relation to food quality
    • Casey R and Hughes RK, Recombinant lipoxygenases and oxylipin metabolism in relation to food quality. Food Biotechnol 18:135-170 (2004).
    • (2004) Food Biotechnol , vol.18 , pp. 135-170
    • Casey, R.1    Hughes, R.K.2
  • 6
    • 0033857476 scopus 로고    scopus 로고
    • Purification of hydroperoxide lyase from pea seeds
    • Hornostaj AR and Robinson DS, Purification of hydroperoxide lyase from pea seeds. Food Chem 71:241-247 (2000).
    • (2000) Food Chem , vol.71 , pp. 241-247
    • Hornostaj, A.R.1    Robinson, D.S.2
  • 7
    • 0037181301 scopus 로고    scopus 로고
    • Purification of hydroperoxide lyase from green bell pepper (Capsicum annuum L.) fruits for the generation of C6-aldehydes in vitro
    • Husson F and Belin JM, Purification of hydroperoxide lyase from green bell pepper (Capsicum annuum L.) fruits for the generation of C6-aldehydes in vitro. J Agric Food Chem 50:1991-1995 (2002).
    • (2002) J Agric Food Chem , vol.50 , pp. 1991-1995
    • Husson, F.1    Belin, J.M.2
  • 8
    • 0037125103 scopus 로고    scopus 로고
    • Development of a biocatalytic process for the production of C6-aldehydes from vegetable oils by soybean lipoxygenase and recombinant hydroperoxide lyase
    • Noordermeer MA, van der Goot W, van Kooij AJ, Veldsink JW, Veldink GA and Vliegenthart JF, Development of a biocatalytic process for the production of C6-aldehydes from vegetable oils by soybean lipoxygenase and recombinant hydroperoxide lyase. J Agric Food Chem 50:4270-4274 (2002).
    • (2002) J Agric Food Chem , vol.50 , pp. 4270-4274
    • Noordermeer, M.A.1    van der Goot, W.2    van Kooij, A.J.3    Veldsink, J.W.4    Veldink, G.A.5    Vliegenthart, J.F.6
  • 9
    • 24644512929 scopus 로고    scopus 로고
    • A simple and efficient system for green note compound biogenesis by use of certain lipoxygenase and hydroperoxide lyase sources
    • Fukushige H and Hidebrand D-F, A simple and efficient system for green note compound biogenesis by use of certain lipoxygenase and hydroperoxide lyase sources. J Agric Food Chem 53:6877-6882 (2005).
    • (2005) J Agric Food Chem , vol.53 , pp. 6877-6882
    • Fukushige, H.1    Hidebrand, D.-F.2
  • 11
    • 0025741241 scopus 로고
    • Recent investigations into the lipoxygenase pathway of plants
    • Gardner HW, Recent investigations into the lipoxygenase pathway of plants. BiochimBiophys Acta 1084:221-239 (1991).
    • (1991) Biochimbiophys Acta , vol.1084 , pp. 221-239
    • Gardner, H.W.1
  • 12
    • 0027145402 scopus 로고
    • Biogeneration of green odor in green leaves
    • Hatanaka A, Biogeneration of green odor in green leaves. Phytochemistry 34:1201-1218 (1993).
    • (1993) Phytochemistry , vol.34 , pp. 1201-1218
    • Hatanaka, A.1
  • 13
    • 32644486049 scopus 로고    scopus 로고
    • Components of C6-aldehyde-induced resistance in Arabidopsis thaliana against a necrotrophic fungal pathogen
    • Kishimoto K, Matsui K, Ozawa R and Takabayashi J, Components of C6-aldehyde-induced resistance in Arabidopsis thaliana against a necrotrophic fungal pathogen. Botrytis Cinerea Plant Sci 170:715-723 (2006).
    • (2006) Botrytis Cinerea Plant Sci , vol.170 , pp. 715-723
    • Kishimoto, K.1    Matsui, K.2    Ozawa, R.3    Takabayashi, J.4
  • 14
    • 0033521729 scopus 로고    scopus 로고
    • The purification and characterization of fatty acid hydroperoxide lyase in sunflower
    • Itoh A and Vick BA, The purification and characterization of fatty acid hydroperoxide lyase in sunflower. Biochim Biophys Acta 1436:531-540 (1999).
    • (1999) Biochim Biophys Acta , vol.1436 , pp. 531-540
    • Itoh, A.1    Vick, B.A.2
  • 17
    • 0028838470 scopus 로고
    • Trehalose and sucrose protect both membranes and protein in intact bacteria during drying
    • Leslie SB, Israel E, Lighthart B, Crowe JH and Crowe JH, Trehalose and sucrose protect both membranes and protein in intact bacteria during drying. Appl Environ Microbiol 61:3592-3597 (1995).
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3592-3597
    • Leslie, S.B.1    Israel, E.2    Lighthart, B.3    Crowe, J.H.4    Crowe, J.H.5
  • 18
    • 0029020745 scopus 로고
    • Increseased stabilizing effects of amphiphilic excipients on freeze-drying of lactate dehydrogenase (LDH) by dispersion into sugar matrices
    • Izutsu K, Yoshioka S and Kojima S, Increseased stabilizing effects of amphiphilic excipients on freeze-drying of lactate dehydrogenase (LDH) by dispersion into sugar matrices. Pharm Res 12:838-843 (1995).
    • (1995) Pharm Res , vol.12 , pp. 838-843
    • Izutsu, K.1    Yoshioka, S.2    Kojima, S.3
  • 19
    • 34347385387 scopus 로고    scopus 로고
    • Sugar-mediated lyoprotection of purified human CYP3A4 and CYP2D6
    • Chefson A, Zhao J and Auclair K, Sugar-mediated lyoprotection of purified human CYP3A4 and CYP2D6. J Biotechnol 130:436-440 (2007).
    • (2007) J Biotechnol , vol.130 , pp. 436-440
    • Chefson, A.1    Zhao, J.2    Auclair, K.3
  • 20
    • 0029141193 scopus 로고
    • Purification and properties of fatty acid hydroperoxide lyase from green bell pepper fruits
    • Shibata Y, Matsui K, Kajiwara T and Hatanaka A, Purification and properties of fatty acid hydroperoxide lyase from green bell pepper fruits. Plant Physiol 36:147-156 (1995).
    • (1995) Plant Physiol , vol.36 , pp. 147-156
    • Shibata, Y.1    Matsui, K.2    Kajiwara, T.3    Hatanaka, A.4
  • 21
    • 0032919455 scopus 로고    scopus 로고
    • Purification of hydroperoxide lyase from cucumbers
    • Hornostaj AR and Robinson DS, Purification of hydroperoxide lyase from cucumbers. Food Chem 66:173-180 (1999).
    • (1999) Food Chem , vol.66 , pp. 173-180
    • Hornostaj, A.R.1    Robinson, D.S.2
  • 22
    • 39149136852 scopus 로고    scopus 로고
    • Stabilization of an enzymatic extract from Penicillium camemberti containing lipoxygenase and hydroperoxide lyase activities
    • Hall CE, Karboune S, Florence H and Selim K, Stabilization of an enzymatic extract from Penicillium camemberti containing lipoxygenase and hydroperoxide lyase activities. Process Biochem (Oxford, UK) 43:258-264 (2008).
    • (2008) Process Biochem (oxford, Uk) , vol.43 , pp. 258-264
    • Hall, C.E.1    Karboune, S.2    Florence, H.3    Selim, K.4
  • 23
    • 0025734174 scopus 로고
    • A spectrophotometric assay for hydroperoxide lyase
    • Vick BA, A spectrophotometric assay for hydroperoxide lyase. Lipids 26:315-320 (1991).
    • (1991) Lipids , vol.26 , pp. 315-320
    • Vick, B.A.1
  • 24
    • 0344177952 scopus 로고    scopus 로고
    • Lipoxygenase and hydroperoxide lyase activities in ripening strawberry fruits
    • Pérez AG, Sanz C, Olías R and Olías JM, Lipoxygenase and hydroperoxide lyase activities in ripening strawberry fruits, J Agric Food Chem 47:249-253 (1999).
    • (1999) J Agric Food Chem , vol.47 , pp. 249-253
    • Pérez, A.G.1    Sanz, C.2    Olías, R.3    Olías, J.M.4
  • 26
    • 0034398516 scopus 로고    scopus 로고
    • Green color degradation of blanched broccoli (BrassicaOleracea) due to acid andmicrobial growth
    • Gunawan MA and Barringer HA, Green color degradation of blanched broccoli (BrassicaOleracea) due to acid andmicrobial growth. J Food Process Preserve 24:253-263 (2007).
    • (2007) J Food Process Preserve , vol.24 , pp. 253-263
    • Gunawan, M.A.1    Barringer, H.A.2
  • 28
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • Wang W, Lyophilization and development of solid protein pharmaceuticals. Int J Pharm 203:1-60 (2000).
    • (2000) Int J Pharm , vol.203 , pp. 1-60
    • Wang, W.1
  • 29
    • 2942685201 scopus 로고    scopus 로고
    • Investigation of the stabilization of freeze-dried lysozyme and the physical properties of the formulations
    • Liao YH, Browna MB and Martina GP, Investigation of the stabilization of freeze-dried lysozyme and the physical properties of the formulations. Eur J Pharm Biopharm 58:15-24 (2004).
    • (2004) Eur J Pharm Biopharm , vol.58 , pp. 15-24
    • Liao, Y.H.1    Browna, M.B.2    Martina, G.P.3
  • 30
    • 0037403152 scopus 로고    scopus 로고
    • Thermal inactivation of lipoxygenase and hydroperoxytrienoic acid lyase in tomatoes
    • Anthon GE and Barrett DM, Thermal inactivation of lipoxygenase and hydroperoxytrienoic acid lyase in tomatoes. Food Chem 81: 275-279 (2003).
    • (2003) Food Chem , vol.81 , pp. 275-279
    • Anthon, G.E.1    Barrett, D.M.2
  • 31
    • 33749326559 scopus 로고    scopus 로고
    • Jolie R, Loey VAandHendrick M, Thermalandhighpressure stability of tomato lipoxygenase and hydroperoxide lyase
    • Rodrigo D, Jolie R, Loey VAandHendrick M, Thermalandhighpressure stability of tomato lipoxygenase and hydroperoxide lyase. J Food Eng 79:423-429 (2007).
    • (2007) J Food Eng , vol.79 , pp. 423-429
    • Rodrigo, D.1
  • 32
    • 34547801845 scopus 로고    scopus 로고
    • Thermal stability of lipoxygenase and hydroperoxide lyase from olive fruit and repercussion on olive oil aroma biosynthesis
    • Luaces P, Sanz C and Pérez AG, Thermal stability of lipoxygenase and hydroperoxide lyase from olive fruit and repercussion on olive oil aroma biosynthesis. J Agric Food Chem 55:6309-6313 (2007).
    • (2007) J Agric Food Chem , vol.55 , pp. 6309-6313
    • Luaces, P.1    Sanz, C.2    Pérez, A.G.3
  • 33
    • 0000174052 scopus 로고
    • Lipoxygenase inactivation bymanothermosonication: Effects of sonication on physicalparameters, pH, KCl, sugars, glycerol, and enzyme concentration
    • Lopez P and Burgos J, Lipoxygenase inactivation bymanothermosonication: effects of sonication on physicalparameters, pH, KCl, sugars, glycerol, and enzyme concentration. JAgric FoodChem 43:620-625 (1995).
    • (1995) Jagric Foodchem , vol.43 , pp. 620-625
    • Lopez, P.1    Burgos, J.2
  • 34
    • 0032441482 scopus 로고    scopus 로고
    • Stabilization against thermal inactivation promoted by sugars on enzyme structure and function: Why is trehalose more effective than other sugars?
    • Sola-Penna M and Meyer-Fernandes JR, Stabilization against thermal inactivation promoted by sugars on enzyme structure and function: Why is trehalose more effective than other sugars? Arch Biochem Biophys 360:10-14 (1998).
    • (1998) Arch Biochem Biophys , vol.360 , pp. 10-14
    • Sola-Penna, M.1    Meyer-Fernandes, J.R.2
  • 35
    • 0001491692 scopus 로고    scopus 로고
    • Effect of thermal protectants on the stability of bovine milk immunoglobulin G
    • Chen CC and Chang HM, Effect of thermal protectants on the stability of bovine milk immunoglobulin G. J Agric Food Chem 46:3570-3576 (1998).
    • (1998) J Agric Food Chem , vol.46 , pp. 3570-3576
    • Chen, C.C.1    Chang, H.M.2
  • 36
    • 0033028681 scopus 로고    scopus 로고
    • Kinetics of thermal inactivation of pea seed lipoxygenases and the effect of additives on their thermostability
    • Busto MD, Apenten RK, Robinson DS, Wu Z, Casey R and Hughes RK, Kinetics of thermal inactivation of pea seed lipoxygenases and the effect of additives on their thermostability. Food Chem 65:323-329 (1999).
    • (1999) Food Chem , vol.65 , pp. 323-329
    • Busto, M.D.1    Apenten, R.K.2    Robinson, D.S.3    Wu, Z.4    Casey, R.5    Hughes, R.K.6
  • 37
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding and preferential hydration
    • Timasheff SN, Protein hydration, thermodynamic binding and preferential hydration. Biochemistry 41:13473-13482 (2002).
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.