메뉴 건너뛰기




Volumn 9, Issue 3-4, 2011, Pages 101-106

Ultrasound-accelerated enzymatic hydrolysis of defatted larva flour of Tenebrio molitor (L.)

Author keywords

Alcalase; Defatted larva flour of Tenebrio molitor (L.); Enzymatic hydrolysis; Protein; Ultrasound

Indexed keywords

SUBTILISIN; TRYPTOPHAN;

EID: 80655148023     PISSN: 14590255     EISSN: 14590263     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (10)

References (25)
  • 1
    • 0034975753 scopus 로고    scopus 로고
    • Effect of ultrasound on ester hydrolysis in aqueous ethanol
    • Tuulmets, A. and Salmar, S. 2001. Effect of ultrasound on ester hydrolysis in aqueous ethanol. Ultrason. Sonochem. 8:209-212.
    • (2001) Ultrason. Sonochem. , vol.8 , pp. 209-212
    • Tuulmets, A.1    Salmar, S.2
  • 2
    • 0030152619 scopus 로고    scopus 로고
    • Influence of ultrasound irradiation on hydrolysis of sucrose catalyzed by invertase
    • Sakakibara, M., Wang, D., Takahashi, R., Takahashi, K. and Mori, S. 1996. Influence of ultrasound irradiation on hydrolysis of sucrose catalyzed by invertase. Enzyme Microb. Technol. 18:444-448.
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 444-448
    • Sakakibara, M.1    Wang, D.2    Takahashi, R.3    Takahashi, K.4    Mori, S.5
  • 3
    • 44249092534 scopus 로고    scopus 로고
    • The effect of ultrasound on lipase-catalyzed hydrolysis of soy oil in solvent-free system
    • Liu, Y. X., Jin, Q. Z., Shan, L., Liu, Y. F., Shen, W. and Wang, X. G. 2008. The effect of ultrasound on lipase-catalyzed hydrolysis of soy oil in solvent-free system. Ultrason. Sonochem. 15:402-407.
    • (2008) Ultrason. Sonochem. , vol.15 , pp. 402-407
    • Liu, Y.X.1    Jin, Q.Z.2    Shan, L.3    Liu, Y.F.4    Shen, W.5    Wang, X.G.6
  • 4
    • 0036028132 scopus 로고    scopus 로고
    • Ultrasound mediated alkaline hydrolysis of methyl benzoate-reinvestigation with crucial parameters
    • Sivakumar, M., Senthilkumar, P., Majumdar, S. and Pandit, A. B. 2002. Ultrasound mediated alkaline hydrolysis of methyl benzoate-reinvestigation with crucial parameters. Ultrason. Sonochem 9:25-30.
    • (2002) Ultrason. Sonochem , vol.9 , pp. 25-30
    • Sivakumar, M.1    Senthilkumar, P.2    Majumdar, S.3    Pandit, A.B.4
  • 5
    • 36448966723 scopus 로고    scopus 로고
    • Ultrasound-accelerated enzymatic hydrolysis of solid leather waste
    • Song, J., Tao, W. Y. and Chen, W. Y. 2008. Ultrasound-accelerated enzymatic hydrolysis of solid leather waste. J. Clean. Prod. 16:591-597.
    • (2008) J. Clean. Prod. , vol.16 , pp. 591-597
    • Song, J.1    Tao, W.Y.2    Chen, W.Y.3
  • 6
    • 70349835623 scopus 로고    scopus 로고
    • The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein
    • Jia, J. Q., Ma, H. L., Zhao, W. R., Wang, Z. B., Tian, W. M., Luo, L. and He, R. H. 2010. The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein. Food Chem. 119:336-342.
    • (2010) Food Chem. , vol.119 , pp. 336-342
    • Jia, J.Q.1    Ma, H.L.2    Zhao, W.R.3    Wang, Z.B.4    Tian, W.M.5    Luo, L.6    He, R.H.7
  • 8
    • 80655129651 scopus 로고    scopus 로고
    • Analysis on the nutrient composition in the larva and pupa of Tenebrio molitor (L.)
    • Dai, C. H., Ma, H. L., Gu, X. H. and Tang, J. 2009. Analysis on the nutrient composition in the larva and pupa of Tenebrio molitor (L.). Sci. Techno. Food Ind. 30:315-317.
    • (2009) Sci. Techno. Food Ind. , vol.30 , pp. 315-317
    • Dai, C.H.1    Ma, H.L.2    Gu, X.H.3    Tang, J.4
  • 9
    • 80655134084 scopus 로고    scopus 로고
    • Isolation and purification of antibacterial peptides with anti-K562 activity from the Tenebrio molitor Linnaeus larvae
    • Liu, Y. G., Cheng, J. X., Zhao, R. J. and Fan, H. Y. 2009. Isolation and purification of antibacterial peptides with anti-K562 activity from the Tenebrio molitor Linnaeus larvae. Chin. J. Vector Biol. Control. 20:565-568.
    • (2009) Chin. J. Vector Biol. Control. , vol.20 , pp. 565-568
    • Liu, Y.G.1    Cheng, J.X.2    Zhao, R.J.3    Fan, H.Y.4
  • 10
    • 70349841743 scopus 로고
    • Petroleum Industry Press, Beijing
    • Zhou, X. Y. 1995. Enzyme Technology. Petroleum Industry Press, Beijing, pp. 284-286.
    • (1995) Enzyme Technology , pp. 284-286
    • Zhou, X.Y.1
  • 13
    • 34249088376 scopus 로고    scopus 로고
    • Influence of the extent of enzymatic hydrolysis on the functional properties of protein hydrolysate from grass carp (Ctenopharyngodon idella) skin
    • Wasswa, J., Tang, J., Gu, X. H. and Yuan, X. Q. 2007. Influence of the extent of enzymatic hydrolysis on the functional properties of protein hydrolysate from grass carp (Ctenopharyngodon idella) skin. Food Chem. 104:1698-1704.
    • (2007) Food Chem. , vol.104 , pp. 1698-1704
    • Wasswa, J.1    Tang, J.2    Gu, X.H.3    Yuan, X.Q.4
  • 14
    • 0001115974 scopus 로고    scopus 로고
    • Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate
    • Mutilangi, W. A. M., Panyam, D. and Kilara, A. 1996. Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate. J. Food Sci. 61:270-274.
    • (1996) J. Food Sci. , vol.61 , pp. 270-274
    • Mutilangi, W.A.M.1    Panyam, D.2    Kilara, A.3
  • 16
    • 78149416204 scopus 로고    scopus 로고
    • Effect of ultrasound on the activity of alliinase from fresh garlic
    • Wang, J., Cao, Y. P., Sun, B. G., Wang, C. T. and Mo, Y. J. 2011. Effect of ultrasound on the activity of alliinase from fresh garlic. Ultrason. Sonochem. 18:534-540.
    • (2011) Ultrason. Sonochem. , vol.18 , pp. 534-540
    • Wang, J.1    Cao, Y.P.2    Sun, B.G.3    Wang, C.T.4    Mo, Y.J.5
  • 17
    • 35348986671 scopus 로고    scopus 로고
    • Ultrasonic inactivation of Bacillus alpha-amylase. I. Effect of gas content and emitting face of probe
    • Kadkhodaee, R. and Povey, M. J. 2008. Ultrasonic inactivation of Bacillus alpha-amylase. I. Effect of gas content and emitting face of probe. Ultrason. Sonochem. 15:133-142.
    • (2008) Ultrason. Sonochem. , vol.15 , pp. 133-142
    • Kadkhodaee, R.1    Povey, M.J.2
  • 18
    • 47949115489 scopus 로고    scopus 로고
    • Ultrasound-enhanced lipase activity in the synthesis of sugar ester using ionic liquids
    • Lee, S. H., Nguyen, H. M., Koo, Y. M. and Ha, S. H. 2008. Ultrasound-enhanced lipase activity in the synthesis of sugar ester using ionic liquids. Process Biochem. 43:1009-1012.
    • (2008) Process Biochem. , vol.43 , pp. 1009-1012
    • Lee, S.H.1    Nguyen, H.M.2    Koo, Y.M.3    Ha, S.H.4
  • 21
    • 24144467835 scopus 로고    scopus 로고
    • Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase
    • Tang, C. H., Yang, X. Q., Chen, Z., Wu, H. and Peng, Z. Y. 2005. Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase. J. Food Biochem. 29:402-421.
    • (2005) J. Food Biochem. , vol.29 , pp. 402-421
    • Tang, C.H.1    Yang, X.Q.2    Chen, Z.3    Wu, H.4    Peng, Z.Y.5
  • 22
    • 0036379879 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on the molecular properties of mushroom polyphenoloxidase
    • Sun, N., Lee, S. and Song, K. B. 2002. Effect of high-pressure treatment on the molecular properties of mushroom polyphenoloxidase. Lebensm-wiss. Technol. 35:315-318.
    • (2002) Lebensm-wiss. Technol. , vol.35 , pp. 315-318
    • Sun, N.1    Lee, S.2    Song, K.B.3
  • 23
    • 0028180075 scopus 로고
    • High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence
    • Dufour, E., Hoa, G. H. and Haertlé, T. 1994. High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence. BBA-Protein Struct. Mol. Enzym. 1206:166-172.
    • (1994) BBA-Protein Struct. Mol. Enzym. , vol.1206 , pp. 166-172
    • Dufour, E.1    Hoa, G.H.2    Haertlé, T.3
  • 24
    • 15744402967 scopus 로고    scopus 로고
    • Thermal unfolding of bovine β-lactoglobulin studied by UV spectroscopy and fluorescence quenching
    • Busti, P., Gatti, C. A. and Delorenzi, N. J. 2005. Thermal unfolding of bovine β-lactoglobulin studied by UV spectroscopy and fluorescence quenching. Food Res. Int. 38:543-550.
    • (2005) Food Res. Int. , vol.38 , pp. 543-550
    • Busti, P.1    Gatti, C.A.2    Delorenzi, N.J.3
  • 25
    • 4143097041 scopus 로고    scopus 로고
    • Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
    • Pallarès, I., Vendrell, J., Avilés, F. X. and Ventura, S. 2004. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin. J. Mol. Biol. 342:321-331.
    • (2004) J. Mol. Biol. , vol.342 , pp. 321-331
    • Pallarès, I.1    Vendrell, J.2    Avilés, F.X.3    Ventura, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.