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Volumn 14, Issue 2, 2013, Pages 3124-3139

Optimization of the preparation of fish protein anti-obesity hydrolysates using response surface methodology

Author keywords

amylase; Anti obesity; Fish protein; Kinetics; Porcine pancreas lipase; Response surface methodology (RSM)

Indexed keywords

AMYLASE; ANTIOBESITY AGENT; FISH PROTEIN HYDROLYSATE; NEUTRAL PROTEINASE; PAPAIN; PROTAMEX; PROTEIN HYDROLYSATE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 84875115310     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms14023124     Document Type: Article
Times cited : (37)

References (48)
  • 1
    • 0033964032 scopus 로고    scopus 로고
    • Dietary fat intake and regulation of energy balance: Implications for obesity
    • Hill, J.O.; Melanson, E.L.; Wyatt, H.T. Dietary fat intake and regulation of energy balance: Implications for obesity. J. Nutr. 2000, 130, 284S-288S.
    • (2000) J. Nutr , vol.130
    • Hill, J.O.1    Melanson, E.L.2    Wyatt, H.T.3
  • 2
    • 0036865734 scopus 로고    scopus 로고
    • Weight management: A comparison of existing dietary approaches in a work-site setting
    • Leslie, W.S.; Lean, M.E.J.; Baillie, H.M.; Hankey, C.R. Weight management: A comparison of existing dietary approaches in a work-site setting. Int. J. Obesity 2002, 26, 1469-1475.
    • (2002) Int. J. Obesity , vol.26 , pp. 1469-1475
    • Leslie, W.S.1    Lean, M.E.J.2    Baillie, H.M.3    Hankey, C.R.4
  • 3
    • 0033028164 scopus 로고    scopus 로고
    • New approaches in the pharmacological treatment of obesity
    • Leonhardt, M.; Hrupka, B.; Langhans, W. New approaches in the pharmacological treatment of obesity. Eur. J. Nutr. 1999, 38, 1-13.
    • (1999) Eur. J. Nutr. , vol.38 , pp. 1-13
    • Leonhardt, M.1    Hrupka, B.2    Langhans, W.3
  • 4
    • 0031556926 scopus 로고    scopus 로고
    • Covalent inhibition of digestive lipases: An in vitro study
    • Gargouri, Y.; Ransac, S.; Verger, R. Covalent inhibition of digestive lipases: An in vitro study. Biochim. Biophysica. Acta 1997, 1344, 6-37.
    • (1997) Biochim. Biophysica. Acta , vol.1344 , pp. 6-37
    • Gargouri, Y.1    Ransac, S.2    Verger, R.3
  • 5
    • 0032434821 scopus 로고    scopus 로고
    • Sibutramine: A review of its contribution to the management of obesity
    • McNeely, W.; Goa, K.L. Sibutramine: A review of its contribution to the management of obesity. Drugs 1998, 56, 1093-1124.
    • (1998) Drugs , vol.56 , pp. 1093-1124
    • McNeely, W.1    Goa, K.L.2
  • 6
    • 77956341108 scopus 로고    scopus 로고
    • Dieckol isolated from Ecklonia cava inhibits alpha-glucosidase and alpha-amylase in vitro and alleviates postprandial hyperglycemia in streptozotocin-induced diabetic mice
    • Lee, S.H.; Park, M.H.; Heo, S.J.; Kang, S.M.; Ko, S.C.; Han, J.S.; Jeon, Y.J. Dieckol isolated from Ecklonia cava inhibits alpha-glucosidase and alpha-amylase in vitro and alleviates postprandial hyperglycemia in streptozotocin-induced diabetic mice. Food Chem. Toxicol. 2010, 48, 2633-2637.
    • (2010) Food Chem. Toxicol. , vol.48 , pp. 2633-2637
    • Lee, S.H.1    Park, M.H.2    Heo, S.J.3    Kang, S.M.4    Ko, S.C.5    Han, J.S.6    Jeon, Y.J.7
  • 7
    • 77958476424 scopus 로고    scopus 로고
    • Inhibitory activities of cyanidin and its glycosides and synergistic effect with acarbose against intestinal α-glucosidase and pancreatic α-amylase
    • Akkarachiyasit, S.; Charoenlertkul, P.; Yibchok-Anun, S.; Adisakwattana, S. Inhibitory activities of cyanidin and its glycosides and synergistic effect with acarbose against intestinal α-glucosidase and pancreatic α-amylase. Int. J. Mol. Sci. 2010, 11, 3387-3396.
    • (2010) Int. J. Mol. Sci , vol.11 , pp. 3387-3396
    • Akkarachiyasit, S.1    Charoenlertkul, P.2    Yibchok-Anun, S.3    Adisakwattana, S.4
  • 8
    • 0031853586 scopus 로고    scopus 로고
    • Postprandial hyperglycaemia and alpha-glucosidase inhibitors
    • Baron, A.D. Postprandial hyperglycaemia and alpha-glucosidase inhibitors. Diabetes Res. Clin. Pract. 1998, 40, S51-S55.
    • (1998) Diabetes Res. Clin. Pract. , vol.40
    • Baron, A.D.1
  • 9
    • 0029893643 scopus 로고    scopus 로고
    • Studies on the inhibition of pancreatic and carboxylester lipases by protamine
    • Tsujita, T.; Matsuura, Y.; Okuda, H. Studies on the inhibition of pancreatic and carboxylester lipases by protamine. J. Lipid Res. 1996, 37, 1481-1487.
    • (1996) J. Lipid Res. , vol.37 , pp. 1481-1487
    • Tsujita, T.1    Matsuura, Y.2    Okuda, H.3
  • 10
    • 0024849004 scopus 로고
    • Isolation and properties of lipolysis inhibitory proteins from wheat germ and wheat bran
    • Borel, P.; Lairon, D.; Termine, E.; Grataroli, R.; Lafont, H. Isolation and properties of lipolysis inhibitory proteins from wheat germ and wheat bran. Plant Foods Hum. Nutr. 1989, 39, 339-348.
    • (1989) Plant Foods Hum. Nutr. , vol.39 , pp. 339-348
    • Borel, P.1    Lairon, D.2    Termine, E.3    Grataroli, R.4    Lafont, H.5
  • 11
    • 0001474412 scopus 로고
    • Purification and characterization of proteinous inhibitor of lipase from wheat flour
    • Tani, H.; Ohishi, H.; Watanabe, K. Purification and characterization of proteinous inhibitor of lipase from wheat flour. J. Agric. Food Chem. 1994, 42, 2382-2385.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 2382-2385
    • Tani, H.1    Ohishi, H.2    Watanabe, K.3
  • 12
    • 0015971903 scopus 로고
    • Characterization of inhibitor protein for lipase in soybean seeds
    • Satouchi, K.; Mori, T.; Matsushita, S. Characterization of inhibitor protein for lipase in soybean seeds. Agric. Biol. Chem. 1974, 38, 97-101.
    • (1974) Agric. Biol. Chem. , vol.38 , pp. 97-101
    • Satouchi, K.1    Mori, T.2    Matsushita, S.3
  • 13
    • 0346726203 scopus 로고    scopus 로고
    • Proteins of white lupin seed, a naturally isoflavone-poor legume, reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells
    • Sirtori, C.R.; Lovati, M.R.; Manzoni, C.; Castiglioni, S.; Duranti, M.; Magni, C.; Morandi, S.; D'Agostina, A.; Arnoldi, A. Proteins of white lupin seed, a naturally isoflavone-poor legume, reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells. J. Nutr. 2004, 134, 18-23.
    • (2004) J. Nutr. , vol.134 , pp. 18-23
    • Sirtori, C.R.1    Lovati, M.R.2    Manzoni, C.3    Castiglioni, S.4    Duranti, M.5    Magni, C.6    Morandi, S.7    D'Agostina, A.8    Arnoldi, A.9
  • 16
    • 35348991559 scopus 로고    scopus 로고
    • Purification and identification of adipogenesis inhibitory peptide from black soybean protein hydrolysate
    • Hyun, J.K.; In, Y.B.; Chang-Won, A.; Suyong, L.; Hyeon, G.L. Purification and identification of adipogenesis inhibitory peptide from black soybean protein hydrolysate. Peptides 2007, 28, 2098-2103.
    • (2007) Peptides , vol.28 , pp. 2098-2103
    • Hyun, J.K.1    In, Y.B.2    Chang-Won, A.3    Suyong, L.4    Hyeon, G.L.5
  • 17
    • 34147093109 scopus 로고    scopus 로고
    • Dietetic and hypocholesterolaemic action of black soy peptide in dietary obese rats
    • Rho, S.J.; Park, S.; Ahn, C.W.; Shin, J.K.; Lee, H.G. Dietetic and hypocholesterolaemic action of black soy peptide in dietary obese rats. J. Sci. Food Agric. 2007, 87, 908-913.
    • (2007) J. Sci. Food Agric , vol.87 , pp. 908-913
    • Rho, S.J.1    Park, S.2    Ahn, C.W.3    Shin, J.K.4    Lee, H.G.5
  • 18
    • 0029871992 scopus 로고    scopus 로고
    • Globin digest, acidic protease hydrolysate, inhibits dietary hypertriglyceridemia and Val-Val-Tyr-Pro, one of its constituents, possesses most superior effect
    • Kagawa, K.; Matsutaka, H.; Fukuhama, C.; Watanabe, Y.; Fujino, H. Globin digest, acidic protease hydrolysate, inhibits dietary hypertriglyceridemia and Val-Val-Tyr-Pro, one of its constituents, possesses most superior effect. Life Sci. 1996, 58, 1745-1755.
    • (1996) Life Sci , vol.58 , pp. 1745-1755
    • Kagawa, K.1    Matsutaka, H.2    Fukuhama, C.3    Watanabe, Y.4    Fujino, H.5
  • 19
    • 2642545831 scopus 로고    scopus 로고
    • Fish protein hydrolysate reduces plasma total cholesterol, increases the proportion of HDL cholesterol, and lowers acyl-CoA: Cholesterol acyltransferase activity in liver of Zucker rats
    • Wergedahl, H.; Liaset, B.; Gudbrandsen, O.A.; Lied, E.; Espe, M.; Muna, Z.; Mork, S.; Berge, R.K. Fish protein hydrolysate reduces plasma total cholesterol, increases the proportion of HDL cholesterol, and lowers acyl-CoA: Cholesterol acyltransferase activity in liver of Zucker rats. J. Nutr. 2004, 134, 1320-1327.
    • (2004) J. Nutr , vol.134 , pp. 1320-1327
    • Wergedahl, H.1    Liaset, B.2    Gudbrandsen, O.A.3    Lied, E.4    Espe, M.5    Muna, Z.6    Mork, S.7    Berge, R.K.8
  • 20
    • 11144233214 scopus 로고    scopus 로고
    • A novel Angiotensin I converting enzyme inhibitory peptide from Alaska Pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je, J.Y.; Park, P.J.; Kwon, J.Y.; Kim, S.K. A novel Angiotensin I converting enzyme inhibitory peptide from Alaska Pollack (Theragra chalcogramma) frame protein hydrolysate. J. Agric. Food Chem. 2004, 52, 7842-7845.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 7842-7845
    • Je, J.Y.1    Park, P.J.2    Kwon, J.Y.3    Kim, S.K.4
  • 21
    • 7444222906 scopus 로고    scopus 로고
    • Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je, J.Y.; Park, P.J.; Kim, S.K. Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Res. Int. 2005, 38, 45-50.
    • (2005) Food Res. Int , vol.38 , pp. 45-50
    • Je, J.Y.1    Park, P.J.2    Kim, S.K.3
  • 22
    • 84862754340 scopus 로고    scopus 로고
    • Purification and identification of antioxidant peptides from the skin protein hydrolysate of two marine fishes, horse mackerel (Magalaspis cordyla) and croaker (Otolithes ruber)
    • Sampath Kumar, N.S.; Nazeer, R.A.; Jaiganesh, R. Purification and identification of antioxidant peptides from the skin protein hydrolysate of two marine fishes, horse mackerel (Magalaspis cordyla) and croaker (Otolithes ruber). Amino Acids 2012, 42, 1641-1649.
    • (2012) Amino Acids , vol.42 , pp. 1641-1649
    • Sampath Kumar, N.S.1    Nazeer, R.A.2    Jaiganesh, R.3
  • 23
    • 33846610587 scopus 로고    scopus 로고
    • Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type
    • Klompong, V.; Benjakul, S.; Kantachote, D.; Shahidi, F. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chem. 2007, 102, 1317-1327.
    • (2007) Food Chem , vol.102 , pp. 1317-1327
    • Klompong, V.1    Benjakul, S.2    Kantachote, D.3    Shahidi, F.4
  • 24
    • 67349149012 scopus 로고    scopus 로고
    • Application of response surface methodology to optimise the antioxidant activity of a Saithe (Pollachius virens) hydrolysate
    • Chabeaud, A.; Dutournié, P.; Guérard, F.; Vandanjon, L.; Bourseau, P. Application of response surface methodology to optimise the antioxidant activity of a Saithe (Pollachius virens) hydrolysate. Mar. Biotechnol. 2009, 11, 445-455.
    • (2009) Mar. Biotechnol. , vol.11 , pp. 445-455
    • Chabeaud, A.1    Dutournié, P.2    Guérard, F.3    Vandanjon, L.4    Bourseau, P.5
  • 25
    • 33646572566 scopus 로고    scopus 로고
    • Immunomodulating capacity of commercial fish protein hydrolysate for diet supplementation
    • Duartea, J.; Vinderola, G.; Ritzc, B.; Perdigón, G.; Matar, C. Immunomodulating capacity of commercial fish protein hydrolysate for diet supplementation. Immunobiology 2006, 211, 341-350.
    • (2006) Immunobiology , vol.211 , pp. 341-350
    • Duartea, J.1    Vinderola, G.2    Ritzc, B.3    Perdigón, G.4    Matar, C.5
  • 26
    • 0037437064 scopus 로고    scopus 로고
    • Effects of various feed supplements containing fish protein hydrolysate or fish processing by-products on the innate immune functions of juvenile coho salmon (Oncorhynchus kisutch)
    • Murraya, A.L.; Pascho, R.J.; Alcornb, S.W.; Fairgrievec, W. T; Shearerc, K. D; Roley, D. Effects of various feed supplements containing fish protein hydrolysate or fish processing by-products on the innate immune functions of juvenile coho salmon (Oncorhynchus kisutch). Aquaculture 2003, 220, 643-653.
    • (2003) Aquaculture , vol.220 , pp. 643-653
    • Murraya, A.L.1    Pascho, R.J.2    Alcornb, S.W.3    Fairgrievec, W.T.4    Shearerc, K.D.5    Roley, D.6
  • 27
    • 18844397356 scopus 로고    scopus 로고
    • Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases
    • Nilsang, S.; Lertsiri, S.; Suphantharika, M.; Assavanig, A. Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases. J. Food Eng. 2005, 70, 571-578.
    • (2005) J. Food Eng. , vol.70 , pp. 571-578
    • Nilsang, S.1    Lertsiri, S.2    Suphantharika, M.3    Assavanig, A.4
  • 28
    • 7444233676 scopus 로고    scopus 로고
    • Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates
    • Gbogouri, G.A.; Linder, M.; Fanni, J.; Parmentier, M. Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. J. Food Sci. 2004, 69, 615-622.
    • (2004) J. Food Sci. , vol.69 , pp. 615-622
    • Gbogouri, G.A.1    Linder, M.2    Fanni, J.3    Parmentier, M.4
  • 29
    • 35448999201 scopus 로고    scopus 로고
    • Optimization of enzymatic hydrolysis of visceral waste proteins of Catla (Catla catla) for preparing protein hydrolysate using a commercial protease
    • Bhaskar, N.; Benila, T.; Radha, C.; Lalitha, R.G. Optimization of enzymatic hydrolysis of visceral waste proteins of Catla (Catla catla) for preparing protein hydrolysate using a commercial protease. Bioresour. Technol. 2008, 99, 335-343.
    • (2008) Bioresour. Technol. , vol.99 , pp. 335-343
    • Bhaskar, N.1    Benila, T.2    Radha, C.3    Lalitha, R.G.4
  • 30
    • 84856585065 scopus 로고    scopus 로고
    • Optimization of enzymatic hydrolysis of visceral waste proteins of yellowfin tuna (Thunnus albacares)
    • Ovissipour, M.; Kenari, A.A.; Motamedzadegan, A.; Nazari, R.M. Optimization of enzymatic hydrolysis of visceral waste proteins of yellowfin tuna (Thunnus albacares). Food Bioprocess Technol. 2012, 5, 696-705.
    • (2012) Food Bioprocess Technol. , vol.5 , pp. 696-705
    • Ovissipour, M.1    Kenari, A.A.2    Motamedzadegan, A.3    Nazari, R.M.4
  • 31
    • 35048818457 scopus 로고    scopus 로고
    • Optimization of free radical scavenging activity by response surface methodology in the hydrolysis of shrimp processing discards
    • Guerard, F.; Sumaya-Martinez, M.T.; Laroque, D.; Chabeaud, A.; Dufossé, L. Optimization of free radical scavenging activity by response surface methodology in the hydrolysis of shrimp processing discards. Process Biochem. 2007, 42, 1486-1491.
    • (2007) Process Biochem. , vol.42 , pp. 1486-1491
    • Guerard, F.1    Sumaya-Martinez, M.T.2    Laroque, D.3    Chabeaud, A.4    Dufossé, L.5
  • 32
    • 0001005379 scopus 로고    scopus 로고
    • Fish protein hydrolysates as nitrogen sources for microbial growth and metabolite production
    • Dufossé, L.; De La Broise, D.; Guérard, F. Fish protein hydrolysates as nitrogen sources for microbial growth and metabolite production. Recent Res. Dev. Microbiol. 1997, 1, 365-381.
    • (1997) Recent Res. Dev. Microbiol , vol.1 , pp. 365-381
    • Dufossé, L.1    De La Broise, D.2    Guérard, F.3
  • 33
    • 18144402070 scopus 로고    scopus 로고
    • Optimization of hydrolysis conditions for the production of thread finbream (Nemipterus japonicus) hydrolysate by Alcalase
    • Normah I.; Jamilah, B. Optimization of hydrolysis conditions for the production of thread finbream (Nemipterus japonicus) hydrolysate by Alcalase. J. Muscle Food. 2005, 16, 87-102.
    • (2005) J. Muscle Food , vol.16 , pp. 87-102
    • Normah, I.1    Jamilah, B.2
  • 34
    • 47649089068 scopus 로고    scopus 로고
    • Optimization of anti-oxidant peptide production from grass carp sarcoplasmic protein using response surface methodology
    • Ren, J.Y.; Zhao, M.M.; Shi, J.; Wang, J.S.; Jiang, Y.M.; Cui, C.; Kakuda, Y.; Xue, S.J. Optimization of anti-oxidant peptide production from grass carp sarcoplasmic protein using response surface methodology. Food Sci. Technol. 2008, 41, 1624-1632.
    • (2008) Food Sci. Technol. , vol.41 , pp. 1624-1632
    • Ren, J.Y.1    Zhao, M.M.2    Shi, J.3    Wang, J.S.4    Jiang, Y.M.5    Cui, C.6    Kakuda, Y.7    Xue, S.J.8
  • 35
    • 68449104771 scopus 로고    scopus 로고
    • Optimization of antioxidant activity by response surface methodology in hydrolysates of jellyfish (Rhopilema esculentum) umbrella collagen
    • Zhuang, Y.L.; Zhao, X.; Li, B.F. Optimization of antioxidant activity by response surface methodology in hydrolysates of jellyfish (Rhopilema esculentum) umbrella collagen. J. Zhejiang Univ.-Sci. B 2009, 10, 572-579.
    • (2009) J. Zhejiang Univ.-Sci. B , vol.10 , pp. 572-579
    • Zhuang, Y.L.1    Zhao, X.2    Li, B.F.3
  • 36
    • 84878477027 scopus 로고    scopus 로고
    • Optimization of debittering of soybean antioxidant hydrolysates with β-cyclodextrins using response surface methodology
    • doi:10.1007/s13197-011-0358-4
    • Hou, L.X.; Wang, J.S.; Zhang, D. Optimization of debittering of soybean antioxidant hydrolysates with β-cyclodextrins using response surface methodology. J. Food Sci. Technol. 2011, doi:10.1007/s13197-011-0358-4.
    • (2011) J. Food Sci. Technol
    • Hou, L.X.1    Wang, J.S.2    Zhang, D.3
  • 37
    • 85078684629 scopus 로고    scopus 로고
    • High-pressure enzymatic hydrolysis of oil
    • Habulin, M.; Knez, Z. High-pressure enzymatic hydrolysis of oil. Eur. J. Lipid Sci. Technol. 2002, 104, 381-386.
    • (2002) Eur. J. Lipid Sci. Technol. , vol.104 , pp. 381-386
    • Habulin, M.1    Knez, Z.2
  • 38
    • 39149145826 scopus 로고    scopus 로고
    • Response surface methodology for autolysis parameters optimization of shrimp head and amino acids released during autolysis
    • Cao, W.H.; Zhang, C.H.; Hong, P.Z.; Ji, H.W. Response surface methodology for autolysis parameters optimization of shrimp head and amino acids released during autolysis. Food Chem. 2008, 109, 176-183.
    • (2008) Food Chem , vol.109 , pp. 176-183
    • Cao, W.H.1    Zhang, C.H.2    Hong, P.Z.3    Ji, H.W.4
  • 39
    • 84862128060 scopus 로고    scopus 로고
    • Optimization of the antibacterial activity of Half-Fin Anchovy (Setipinna taty) Hydrolysates
    • Song, R.; Wei, R.B.; Zhang, B.; Wang, D.F. Optimization of the antibacterial activity of Half-Fin Anchovy (Setipinna taty) Hydrolysates. Food Bioprocess Technol. 2012, 5, 1979-1989.
    • (2012) Food Bioprocess Technol , vol.5 , pp. 1979-1989
    • Song, R.1    Wei, R.B.2    Zhang, B.3    Wang, D.F.4
  • 40
    • 79959299899 scopus 로고    scopus 로고
    • Probing the interaction between 3 flavonoids and pancreatic lipase by methods of fluorescence spectroscopy and enzymatic kinetics
    • Li, Y.Q.; Yang, P.; Gao, F.; Zhang, Z.W.; Wu, B. Probing the interaction between 3 flavonoids and pancreatic lipase by methods of fluorescence spectroscopy and enzymatic kinetics. Eur. Food Res. Technol. 2011, 233, 63-69.
    • (2011) Eur. Food Res. Technol , vol.233 , pp. 63-69
    • Li, Y.Q.1    Yang, P.2    Gao, F.3    Zhang, Z.W.4    Wu, B.5
  • 41
    • 35448934436 scopus 로고    scopus 로고
    • Development of inhibitors against lipase and alpha-glucosidase from derivatives of monascus pigment
    • Kim, J.H.; Kim, H.J.; Park, H.W.; Youn, S.H.; Choi, D.Y.; Shin, C.S. Development of inhibitors against lipase and alpha-glucosidase from derivatives of monascus pigment. FEMS Microbiol. Lett. 2007, 276, 93-98.
    • (2007) FEMS Microbiol. Lett , vol.276 , pp. 93-98
    • Kim, J.H.1    Kim, H.J.2    Park, H.W.3    Youn, S.H.4    Choi, D.Y.5    Shin, C.S.6
  • 42
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 3, 426-428.
    • (1959) Anal. Chem , vol.3 , pp. 426-428
    • Miller, G.L.1
  • 43
    • 84875086914 scopus 로고
    • The United States Pharmacopeial Convention. 22nd ed.; Rockville, MD, USA
    • The United States Pharmacopeial Convention. United States Pharmacopea, 22nd ed.; Rockville, MD, USA, 1989.
    • (1989) United States Pharmacopea
  • 44
    • 0003995078 scopus 로고
    • Association of Official Analytical Chemists. 15th ed.; Washington, DC, USA
    • Association of Official Analytical Chemists. Official Methods of Analysis, 15th ed.; Washington, DC, USA, 1990.
    • (1990) Official Methods of Analysis
  • 45
    • 25844527274 scopus 로고    scopus 로고
    • Covalent-bonded immobilization of lipase on poly(phenylene sulfide) dendrimers and their hydrolysis ability
    • Yemul, O.; Imae, T. Covalent-bonded immobilization of lipase on poly(phenylene sulfide) dendrimers and their hydrolysis ability. Biomacromolecules 2005, 6, 2809-2814.
    • (2005) Biomacromolecules , vol.6 , pp. 2809-2814
    • Yemul, O.1    Imae, T.2
  • 46
    • 0347915737 scopus 로고    scopus 로고
    • Kinetics of hydrolysis of tetrahydrofurfuryl butyrate in a three phase system containing immobilized lipase from Candida Antarctica
    • Yadav, G.D.; Devi, K.M. Kinetics of hydrolysis of tetrahydrofurfuryl butyrate in a three phase system containing immobilized lipase from Candida Antarctica. Biochem. Eng. J. 2003, 17, 57-63.
    • (2003) Biochem. Eng. J. , vol.17 , pp. 57-63
    • Yadav, G.D.1    Devi, K.M.2
  • 47
    • 0344141392 scopus 로고    scopus 로고
    • Hydrolysis of emulsified mixtures of triacylglycerols by pancreatic lipase
    • Kaambre, T.; Tougu, V.; Kaambre, P.; Vija, H.; Sikk, P. Hydrolysis of emulsified mixtures of triacylglycerols by pancreatic lipase. Biochim. Biophys. Acta 1999, 1431, 97-106.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 97-106
    • Kaambre, T.1    Tougu, V.2    Kaambre, P.3    Vija, H.4    Sikk, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.