메뉴 건너뛰기




Volumn 31, Issue , 2016, Pages 20-28

Effects of ultrasound and ultrasound assisted alkaline pretreatments on the enzymolysis and structural characteristics of rice protein

Author keywords

Enzymatic hydrolysis; Multi frequency energy gathered; Rice protein; ultrasound; Ultrasound assisted alkaline pretreatments

Indexed keywords

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; DICHROISM; EMISSION SPECTROSCOPY; MICROSTRUCTURE; PARTICLE SIZE; PROTEOLYSIS; ULTRASONICS;

EID: 84949557708     PISSN: 13504177     EISSN: 18732828     Source Type: Journal    
DOI: 10.1016/j.ultsonch.2015.11.019     Document Type: Article
Times cited : (201)

References (40)
  • 1
    • 84939151482 scopus 로고    scopus 로고
    • 15 - Vegetable protein isolates
    • G.O. Phillips, P.A. Williams, second ed. Woodhead Publishing
    • S. González-Pérez, and J.B. Arellano 15 - Vegetable protein isolates G.O. Phillips, P.A. Williams, Handbook of Hydrocolloids second ed. 2009 Woodhead Publishing 383 419
    • (2009) Handbook of Hydrocolloids , pp. 383-419
    • González-Pérez, S.1    Arellano, J.B.2
  • 2
    • 68949215592 scopus 로고    scopus 로고
    • Differences in functional properties and biochemical characteristics of congenetic rice proteins
    • X. Cao, H. Wen, C. Li, and Z. Gu Differences in functional properties and biochemical characteristics of congenetic rice proteins J. Cereal Sci. 50 2009 184 189
    • (2009) J. Cereal Sci. , vol.50 , pp. 184-189
    • Cao, X.1    Wen, H.2    Li, C.3    Gu, Z.4
  • 3
    • 84921888259 scopus 로고    scopus 로고
    • Mechanistic insights into solubilization of rice protein isolates by freeze-milling combined with alkali pretreatment
    • W. Tao, Z. Hao, W. Li, W. Ren, and Z. Chen Mechanistic insights into solubilization of rice protein isolates by freeze-milling combined with alkali pretreatment Food Chem. 178 2015 82 88
    • (2015) Food Chem. , vol.178 , pp. 82-88
    • Tao, W.1    Hao, Z.2    Li, W.3    Ren, W.4    Chen, Z.5
  • 4
    • 0034246767 scopus 로고    scopus 로고
    • Preparation and characterization of rice protein isolates
    • F.F. Shih, and K.W. Daigle Preparation and characterization of rice protein isolates J. Am. Oil. Chem. Soc. 77 2000 885 889
    • (2000) J. Am. Oil. Chem. Soc. , vol.77 , pp. 885-889
    • Shih, F.F.1    Daigle, K.W.2
  • 6
    • 84861092332 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of rice dreg protein: Effects of enzyme type on the functional properties and antioxidant activities of recovered proteins
    • Q. Zhao, H. Xiong, C. Selomulya, X.D. Chen, H. Zhong, S. Wang, W. Sun, and Q. Zhou Enzymatic hydrolysis of rice dreg protein: effects of enzyme type on the functional properties and antioxidant activities of recovered proteins Food Chem. 134 2012 1360 1367
    • (2012) Food Chem. , vol.134 , pp. 1360-1367
    • Zhao, Q.1    Xiong, H.2    Selomulya, C.3    Chen, X.D.4    Zhong, H.5    Wang, S.6    Sun, W.7    Zhou, Q.8
  • 7
    • 84893954819 scopus 로고    scopus 로고
    • Exploitation of starch industry liquid by-product to produce bioactive peptides from rice hydrolyzed proteins
    • L. Dei Piu, A. Tassoni, D.I. Serrazanetti, M. Ferri, E. Babini, D. Tagliazucchi, and A. Gianotti Exploitation of starch industry liquid by-product to produce bioactive peptides from rice hydrolyzed proteins Food Chem. 155 2014 199 206
    • (2014) Food Chem. , vol.155 , pp. 199-206
    • Dei Piu, L.1    Tassoni, A.2    Serrazanetti, D.I.3    Ferri, M.4    Babini, E.5    Tagliazucchi, D.6    Gianotti, A.7
  • 8
    • 0028122920 scopus 로고
    • Isolation and characterization of oryzatensin: A novel bioactive peptide with ileum-contracting and immunomodulating activities derived from rice albumin
    • M. Takahashi, S. Moriguchi, M. Yoshikawa, and R. Sasaki Isolation and characterization of oryzatensin: a novel bioactive peptide with ileum-contracting and immunomodulating activities derived from rice albumin Biochem. Mol. Biol. Int. 33 1994 1151 1158
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 1151-1158
    • Takahashi, M.1    Moriguchi, S.2    Yoshikawa, M.3    Sasaki, R.4
  • 9
    • 70349816703 scopus 로고    scopus 로고
    • Isolation and identification of antioxidative peptides from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS
    • J. Zhang, H. Zhang, L. Wang, X. Guo, X. Wang, and H. Yao Isolation and identification of antioxidative peptides from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS Food Chem. 119 2010 226 234
    • (2010) Food Chem. , vol.119 , pp. 226-234
    • Zhang, J.1    Zhang, H.2    Wang, L.3    Guo, X.4    Wang, X.5    Yao, H.6
  • 10
    • 58849118402 scopus 로고    scopus 로고
    • Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates
    • A.P. Adebiyi, A.O. Adebiyi, J. Yamashita, T. Ogawa, and K. Muramoto Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates Eur. Food Res. Technol. 228 2009 553 563
    • (2009) Eur. Food Res. Technol. , vol.228 , pp. 553-563
    • Adebiyi, A.P.1    Adebiyi, A.O.2    Yamashita, J.3    Ogawa, T.4    Muramoto, K.5
  • 12
    • 84946499313 scopus 로고    scopus 로고
    • Effects of thermal, microwave, and ultrasound pretreatments on antioxidative capacity of enzymatic milk protein concentrate hydrolysates
    • H. Uluko, S. Zhang, L. Liu, M. Tsakama, J. Lu, and J. Lv Effects of thermal, microwave, and ultrasound pretreatments on antioxidative capacity of enzymatic milk protein concentrate hydrolysates J. Funct. Foods 18 Part B 2015 1138 1146
    • (2015) J. Funct. Foods , vol.18 , Issue.PART B , pp. 1138-1146
    • Uluko, H.1    Zhang, S.2    Liu, L.3    Tsakama, M.4    Lu, J.5    Lv, J.6
  • 13
    • 84936887133 scopus 로고    scopus 로고
    • Ultra-high pressure homogenization enhances physicochemical properties of soy protein isolate-stabilized emulsions
    • C. Fernández-Ávila, R. Escriu, and A.J. Trujillo Ultra-high pressure homogenization enhances physicochemical properties of soy protein isolate-stabilized emulsions Food Res. Int. 75 2015 357 366
    • (2015) Food Res. Int. , vol.75 , pp. 357-366
    • Fernández-Ávila, C.1    Escriu, R.2    Trujillo, A.J.3
  • 14
    • 37349070789 scopus 로고    scopus 로고
    • Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions
    • A.R. Jambrak, T.J. Mason, V. Lelas, Z. Herceg, and I.L. Herceg Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions J. Food Eng. 86 2008 281 287
    • (2008) J. Food Eng. , vol.86 , pp. 281-287
    • Jambrak, A.R.1    Mason, T.J.2    Lelas, V.3    Herceg, Z.4    Herceg, I.L.5
  • 15
    • 84859828412 scopus 로고    scopus 로고
    • Enzymolysis kinetics and activities of ACE inhibitory peptides from wheat germ protein prepared with SFP ultrasound-assisted processing
    • W. Qu, H. Ma, J. Jia, R. He, L. Luo, and Z. Pan Enzymolysis kinetics and activities of ACE inhibitory peptides from wheat germ protein prepared with SFP ultrasound-assisted processing Ultrason. Sonochem. 19 2012 1021 1026
    • (2012) Ultrason. Sonochem. , vol.19 , pp. 1021-1026
    • Qu, W.1    Ma, H.2    Jia, J.3    He, R.4    Luo, L.5    Pan, Z.6
  • 17
    • 84859211760 scopus 로고    scopus 로고
    • Ultrasound-assisted alkaline pretreatment of sugarcane bagasse for fermentable sugar production: Optimization through response surface methodology
    • R. Velmurugan, and K. Muthukumar Ultrasound-assisted alkaline pretreatment of sugarcane bagasse for fermentable sugar production: optimization through response surface methodology Bioresour. Technol. 112 2012 293 299
    • (2012) Bioresour. Technol. , vol.112 , pp. 293-299
    • Velmurugan, R.1    Muthukumar, K.2
  • 18
    • 84883749229 scopus 로고    scopus 로고
    • Ultrasound assisted alkaline hydrolysis of poly(ethylene terephthalate) in presence of phase transfer catalyst
    • N.R. Paliwal, and A.K. Mungray Ultrasound assisted alkaline hydrolysis of poly(ethylene terephthalate) in presence of phase transfer catalyst Polym. Degrad. Stab. 98 2013 2094 2101
    • (2013) Polym. Degrad. Stab. , vol.98 , pp. 2094-2101
    • Paliwal, N.R.1    Mungray, A.K.2
  • 19
    • 84884354340 scopus 로고    scopus 로고
    • Alkaline and ultrasound assisted alkaline pretreatment for intensification of delignification process from sustainable raw-material
    • P.B. Subhedar, and P.R. Gogate Alkaline and ultrasound assisted alkaline pretreatment for intensification of delignification process from sustainable raw-material Ultrason. Sonochem. 21 2014 216 225
    • (2014) Ultrason. Sonochem. , vol.21 , pp. 216-225
    • Subhedar, P.B.1    Gogate, P.R.2
  • 20
    • 58149199483 scopus 로고    scopus 로고
    • Sono-chemical preparation of cellulose nanocrystals from lignocellulose derived materials
    • P.B. Filson, and B.E. Dawson-Andoh Sono-chemical preparation of cellulose nanocrystals from lignocellulose derived materials Bioresour. Technol. 100 2009 2259 2264
    • (2009) Bioresour. Technol. , vol.100 , pp. 2259-2264
    • Filson, P.B.1    Dawson-Andoh, B.E.2
  • 21
    • 84912015323 scopus 로고    scopus 로고
    • Biodiesel production from soybean oil deodorizer distillate enhanced by counter-current pulsed ultrasound
    • X. Yin, Q. You, H. Ma, C. Dai, H. Zhang, K. Li, and Y. Li Biodiesel production from soybean oil deodorizer distillate enhanced by counter-current pulsed ultrasound Ultrason. Sonochem. 23 2015 53 58
    • (2015) Ultrason. Sonochem. , vol.23 , pp. 53-58
    • Yin, X.1    You, Q.2    Ma, H.3    Dai, C.4    Zhang, H.5    Li, K.6    Li, Y.7
  • 23
    • 0022553040 scopus 로고
    • Determination of proteins and sulfobetaine with the folin-phenol reagent
    • M. Ledoux, and F. Lamy Determination of proteins and sulfobetaine with the folin-phenol reagent Anal. Biochem. 157 1986 28 31
    • (1986) Anal. Biochem. , vol.157 , pp. 28-31
    • Ledoux, M.1    Lamy, F.2
  • 24
    • 84879030357 scopus 로고    scopus 로고
    • Pretreatment of defatted wheat germ proteins (by-products of flour mill industry) using ultrasonic horn and bath reactors: Effect on structure and preparation of ACE-inhibitory peptides
    • C. Zhou, H. Ma, X. Yu, B. Liu, A.E.-G.A. Yagoub, and Z. Pan Pretreatment of defatted wheat germ proteins (by-products of flour mill industry) using ultrasonic horn and bath reactors: effect on structure and preparation of ACE-inhibitory peptides Ultrason. Sonochem. 20 2013 1390 1400
    • (2013) Ultrason. Sonochem. , vol.20 , pp. 1390-1400
    • Zhou, C.1    Ma, H.2    Yu, X.3    Liu, B.4    Yagoub, A.E.-G.A.5    Pan, Z.6
  • 25
    • 84922419259 scopus 로고    scopus 로고
    • Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal
    • J. Jin, H. Ma, K. Wang, A.E.-G.A. Yagoub, J. Owusu, W. Qu, R. He, C. Zhou, and X. Ye Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal Ultrason. Sonochem. 24 2015 55 64
    • (2015) Ultrason. Sonochem. , vol.24 , pp. 55-64
    • Jin, J.1    Ma, H.2    Wang, K.3    Yagoub, A.E.-G.A.4    Owusu, J.5    Qu, W.6    He, R.7    Zhou, C.8    Ye, X.9
  • 26
    • 84910053123 scopus 로고    scopus 로고
    • The effect of ultrasound treatment on the structural, physical and emulsifying properties of dairy proteins
    • J. O'Sullivan, M. Arellano, R. Pichot, and I. Norton The effect of ultrasound treatment on the structural, physical and emulsifying properties of dairy proteins Food Hydrocolloids 42 2014 386 396
    • (2014) Food Hydrocolloids , vol.42 , pp. 386-396
    • O'Sullivan, J.1    Arellano, M.2    Pichot, R.3    Norton, I.4
  • 27
    • 0002461718 scopus 로고
    • Molecular interaction in alkali denatured soybean proteins
    • K. Ishino, and S. Okamoto Molecular interaction in alkali denatured soybean proteins Cereal Chem. 52 1975 9 21
    • (1975) Cereal Chem. , vol.52 , pp. 9-21
    • Ishino, K.1    Okamoto, S.2
  • 28
    • 77953132023 scopus 로고    scopus 로고
    • Impact of ultrasonic treatment on properties of starch film-forming dispersion and the resulting films
    • W. Cheng, J. Chen, D. Liu, X. Ye, and F. Ke Impact of ultrasonic treatment on properties of starch film-forming dispersion and the resulting films Carbohydr. Polym. 81 2010 707 711
    • (2010) Carbohydr. Polym. , vol.81 , pp. 707-711
    • Cheng, W.1    Chen, J.2    Liu, D.3    Ye, X.4    Ke, F.5
  • 29
    • 39049095766 scopus 로고    scopus 로고
    • Spectrophotometric determination of protein concentration
    • Appendix 3
    • M.H. Simonian Spectrophotometric determination of protein concentration Curr. Protoc. Cell Biol. 2002 B1.3.1 B1.3.7 Appendix 3
    • (2002) Curr. Protoc. Cell Biol. , pp. B131-B137
    • Simonian, M.H.1
  • 30
    • 84933523111 scopus 로고    scopus 로고
    • Rheological behavior and bonding performance of an alkaline soy protein suspension
    • A. Bacigalupe, A.K. Poliszuk, P. Eisenberg, and M.M. Escobar Rheological behavior and bonding performance of an alkaline soy protein suspension Int. J. Adhes. Adhes. 62 2015 1 6
    • (2015) Int. J. Adhes. Adhes. , vol.62 , pp. 1-6
    • Bacigalupe, A.1    Poliszuk, A.K.2    Eisenberg, P.3    Escobar, M.M.4
  • 31
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • J.T. Pelton, and L.R. McLean Spectroscopic methods for analysis of protein secondary structure Anal. Biochem. 277 2000 167 176
    • (2000) Anal. Biochem. , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 32
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • L. Whitmore, and B.A. Wallace Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases Biopolymers 89 2008 392 400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 34
    • 0037735266 scopus 로고    scopus 로고
    • Application of fluorescence spectroscopy and chemometrics in the evaluation of processed cheese during storage
    • J. Christensen, V.T. Povlsen, and J. Sørensen Application of fluorescence spectroscopy and chemometrics in the evaluation of processed cheese during storage J. Dairy Sci. 86 2003 1101 1107
    • (2003) J. Dairy Sci. , vol.86 , pp. 1101-1107
    • Christensen, J.1    Povlsen, V.T.2    Sørensen, J.3
  • 35
    • 84857790267 scopus 로고    scopus 로고
    • Structural changes of soy proteins at the oil-water interface studied by fluorescence spectroscopy
    • M. Keerati-u-rai, M. Miriani, S. Iametti, F. Bonomi, and M. Corredig Structural changes of soy proteins at the oil-water interface studied by fluorescence spectroscopy Colloids Surf., B 93 2012 41 48
    • (2012) Colloids Surf., B , vol.93 , pp. 41-48
    • Keerati-U-Rai, M.1    Miriani, M.2    Iametti, S.3    Bonomi, F.4    Corredig, M.5
  • 36
    • 84940481210 scopus 로고    scopus 로고
    • Effect of freeze-thaw cycles on the emulsion activity and structural characteristics of soy protein isolate
    • J. Zhao, F. Dong, Y. Li, B. Kong, and Q. Liu Effect of freeze-thaw cycles on the emulsion activity and structural characteristics of soy protein isolate Process Biochem. 50 2015 1607 1613
    • (2015) Process Biochem. , vol.50 , pp. 1607-1613
    • Zhao, J.1    Dong, F.2    Li, Y.3    Kong, B.4    Liu, Q.5
  • 37
    • 70349835623 scopus 로고    scopus 로고
    • The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein
    • J. Jia, H. Ma, W. Zhao, Z. Wang, W. Tian, L. Luo, and R. He The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein Food Chem. 119 2010 336 342
    • (2010) Food Chem. , vol.119 , pp. 336-342
    • Jia, J.1    Ma, H.2    Zhao, W.3    Wang, Z.4    Tian, W.5    Luo, L.6    He, R.7
  • 38
    • 79851478055 scopus 로고    scopus 로고
    • Denaturation of soy proteins in solution and at the oil-water interface. A fluorescence study
    • M. Miriani, M. Corredig, S. Iametti, and F. Bonomi Denaturation of soy proteins in solution and at the oil-water interface. A fluorescence study Food Hydrocolloids 25 2011 620 626
    • (2011) Food Hydrocolloids , vol.25 , pp. 620-626
    • Miriani, M.1    Corredig, M.2    Iametti, S.3    Bonomi, F.4
  • 39
    • 84857790267 scopus 로고    scopus 로고
    • Structural changes of soy proteins at the oil-water interface studied by fluorescence spectroscopy
    • M. Miriani, S. Iametti, F. Bonomi, and M. Corredig Structural changes of soy proteins at the oil-water interface studied by fluorescence spectroscopy Colloids Surf., B 93 2012 41 48
    • (2012) Colloids Surf., B , vol.93 , pp. 41-48
    • Miriani, M.1    Iametti, S.2    Bonomi, F.3    Corredig, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.