15 Nippon Shokuhin Kagaku Kogaku Kaishi Vol. //, No.., +.- +/* (,**2) 143 bo Modification of Functional Properties of Fatty Acid Salt-Induced Gel of b

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1 15 Nippon Shokuhin Kagaku Kogaku Kaishi Vol. //, No.., +.- +/* (,**2) 143 bo Modification of Functional Properties of Fatty Acid Salt-Induced Gel of b-lactoglobulin by the Addition of Fish Water-Soluble Protein Concentrate Naoko Yuno-Ohta and Noriko Masuda Junior College at Mishima, Nihon University,,-++./ Bunkyo-Cho, Mishima City, Shizuoka.++ 2/// The physicochemical properties (dynamic viscoelastic properties and sensuousness) of water-soluble protein concentrate (WSPC) of fish meat were investigated to improve its utilization with or without b-lactoglobulin ( b-lg) and fatty acid salt. The secondary structure of the proteins was also investigated using Fourier transform infrared spectroscopy (FT-IR). Although WSPC is unstable in water and easily precipitates, the stability was increased by the addition of sodium caprate. Whereas b-lg has high gel-forming ability in the presence of fatty acid salt, WSPC itself could not form a fatty acid salt-induced gel. b-lg is a b-sheet protein and changes during the formation of a fatty acid salt-induced b-lg gel were mainly due to a conversion from intramolecular b-sheets to intermolecular b-sheets in b-lg. The secondary structure of WSPC at the sol stage mainly comprised a-helices. The a-helix and intramolecular b-sheet structures in WSPC were slightly changed to intermolecular b-sheet structure by the addition of sodium caprate. The WSPC with sodium caprate a# ected the rheological properties of b-lg and the b-lg-wspc mixture formed homogeneous and a high water-holding gel. These results suggest that WSPC could contribute to fatty acid salt-induced b-lg gel as a texture modifier. (Received Sep. 0,,**1 ; Accepted Jan.,,,,**2) Keywords : fish water soluble protein, gelation, fatty acid salt, mixed protein gel, b-lactoglobulin : bo,* /* - +** *** + *** +,, Ficoll - Water Soluble Pro-,- tein Concentrate, WSPC 0 +*./.++ 2///, -+ +./ Corresponding author naokoohta@bitcat.net 1

2 144 //.,**2. 16,/ mm,/ + 13 mm 0,2. rad s + Hz ++ WSPC bo bolg 3 bolg WSPC FT-IR 2-** + + 0/* cm -* ** cm. *** cm. cm - -*.*,/ 1 * 3 *** g, -*. Ficoll PM.**.** *** +- + Uppsala, GE,. cm +/ *. +*. mm,,, WSPC + L *.*,/ -0. +, *,. M FT-IR. + mm, +/ m : : Branchiostegus japonicus Lowry, + //-, + /00 + cm + WSPC bo LG cm */. + L-3*2 + 0** + 1** cm +* C-.+/+ *,. M ph * wv / +. ph 1 +* / mm +* +** l,/ 2 +. *., M, - 0.,. ph 2 /* g WSPC RFS WSPC TA bolg 3 WSPC

3 17 : 145 Fig. + Appearance of WSPC and b-lg mixture containing sodium caprate at various mixing conditions The gel syneresis was measured by centrifuge at /* g for -min at room temperature and followed by calculating the weight of water which came out from the + g gel. *, No water took o# from gel. Fig ,. bolg Fig. + a-c WSPC b-lg -0..,. WSPC bo LG + : + Fig., Dynamic strain sweep tests of sample solutions Fig. + e + f WSPC containing sodium caprate Symbols :, 1 WSPC and 1 b-lg mixture ;, +. WSPC ;, +. b-lg. Fig. + g-o +. + : Fig. le ph 12., WSPC b-lg Fig., - WSPC b-lg +. + : G G GG G WSPCboLG - WSPC bolg G bolg G Fig.,

4 146 //.,**2. 18 WSPC bolg WSPC bo LG + : + - +* - 2** Fig. -,/ 3* WSPC Fig. -b -** 2** Fig. -a +* 2** GG GG *.*+ +** b-lg bolg 3* Fig. - Changes of storage modulus and loss modulus G G + with strain by incubation at,/ of the sample Fig. -c solutions containing sodium caprate a, 1 WSPC and 1 b-lg mixture ; b, +. WSPC ; c, +. b-lg Symbols :, storage modulus (G ) and, loss modulus Fig. -a -c (G ) of sample immediately after mixed with sodium b-lg caprate ;, storage modulus (G ) and, loss modulus (G ) of sample after dynamic time sweep test. WSPC Fig.. Fig.. a,/,0 Fig. + * bolg +** G G WSPC G G, - FT-IR Fig.. b bolg Fig.. c +. +, FT-IR I 2* bolg bolg bo +/ 0 G WSPC

5 19 : 147 Fig. / Deconvoluted spectra in the amide I region of +. WSPC with or without sodium caprate Heavy line, with sodium caprate ; thin line, without sodium caprate. The pd of the solution was adjusted to 2*. with sodium deuteroxide. Fig.. Dynamic time sweep tests of the sample solutions at,/ a, 1 WSPC and 1 b-lg mixture ; b, +. WSPC ; c, +. b-lg. Heavy line, storage modulus ; dashed line, loss modulus cm b b bo Fig. 0 - Fig. 0a 0b 0 c WSPCb-LG WSPC b-lg WSPC Fig. 0b * cm + 0** + 1** cm I cm cm Fig. 0b bo ao OVA ao.* /* ao +0 bo bo WSPC bolg Fig. 0a 2 + bo + 0-* cm bo + bolg bo /* + 0./ cm ao bolg bo + 0+/ 3 + bo cm bo Fig. / +1 WSPC Fig. 0c bolg bolg OVA WSPC ao OVA / cm bolg + b cm + 01* +0,2

6 148 //.,**2. 20 Fig. 0 Deconvoluted spectra in the amide I region of Fig. 1 Di# erence spectra between treated and nonthe protein solutions with sodium caprate treated samples a, 1 WSPC and 1 b-lg mixture ; b, +. WSPC ; c, The concentration and treatment condition of each +. b-lg. Dashed line, solution immediately after sample were the same as those in Fig. 0. Di# erence mixed with sodium caprate ; solid line, sample incu- spectrum was obtained by subtracting spectrum bated for 1 days at,/ ; decollated line, sample heated for -* min at 2* after 1 day-incubation. without treatment from that for incubated (heavy line) or heated samples (thin line). + cm Fig. c / cm bo cm bo WSPC, bolg Fig. 1a bolg Fig. 1c Fig. cm / WSPC bolg bolg WSPC Fig. 1b bo bo bolg bolg ao Fig. 1 Fig. 2

7 21 : 149 WSPC Fig. 2 Comparison of three kinds of di# erence spectra between incubated and non-incubated samples The incubation condition was the same as in Fig. 0. Heavy line, 1 WSPC and 1 b-lg mixture ; thin line, +. WSPC ; decollated line, +. b-lg. b-lg + : + bolg - Fig. 1a, b, c WSPC bolg bolg bolg FT-IR WSPC +/ bo LG + WSPC WSPC bo Surrey School of Biomedical and Life Science Nazlin K. Howell bolg Farah Baddi G FT-IR cm / +, Fig. 2 +3,* WSPC C +3/**01* WSPC bolg +,.1 0,. 0-*,**0, WSPC bolg Fig. -., +*,/ +* / /. Iwata, K., Ishizuka, S., Handa A. and Tanaka, M., Preparation and characterization of edible films from fish water-soluble proteins. Fisheries Sci., 00, -1, -12 (,***). / Tanaka, M., Ishizaki, S., Suzuki, T. and Takai, R., Water WSPC vapor permeability of edible films prepared from fish water soluble proteins as a# ected by lipid type. J. Tokyo Univ. Fish, 21, (,**+).

8 150 //.,** Yuno-Ohta, N., Maeda, H., Okada, M. and Hasegawa, K., +- Howell, N.K., Arteaga, G., Nakai, S. and Li-Chan, E.C.Y., Formation of transparent gels of sesame +-S globulin : Raman spectral analysis in the C-H stretching region of E# ects of fatty acid salts. J. Food Sci., /1, 203* ( +33, ). proteins and amino acids for investigation of hydro- 1 Yuno-Ohta, N., Higasa, T., Tatsumi, E., Sakurai, H., Asan, phobic interactions. J. Agric. Food Sci.,.1, 3,. 3-- ( +333). R. and Hirose, M. Formation of fatty acid salt-induced +. Ross-Murphy S.B. and Tobitani, A., Heat-set proteingel of ovalbumin and the mechanism for gelation. J. models for the concentration and temperature depend- Agric. Food Chem.,.0,./+2./,- ( +332). ence of the gelation time. In Hydrocolloids, Part +. ed. 2 Yuno-Ohta, N., Mechanism for formation of ovalbumin- Nishinari, K., Elsevier Science, Devon, pp (,***). fatty acid salt mixed gels. Food Hydrocolloids,,*, -/1 +/ Subirade, M., Kelly, I., Gueguen, J. and Pezolet, M., Mo- -0* (,**0). lecular basis of film formation from a soybean protein : 3 Yuno-Ohta, N., Murata, K., Miyahara, M. and Ohta, H. comparison between the conformation of glycinin in Rheological properties of sodium caprate-induced b- aqueous solution and in films. Int. J. Biol. Macromol.,,-, lactoglobulin gel and changes in secondary structure,.+,.3 ( +332). during gelation. JAOCS, 2+,,,/,-* (,**.). +0 Ngarize, S., Herman, H., Adams, A. and Howell, N., Com- +* Yuno-Ohta, N., Toryu, H., Higasa, T., Maeda, H., Okada M. and Ohta, H. Gelation properties of ovalbumin as parison of changes structure of unheated, heated, and high-pressure-treated b-lactoglobulin and ovalbumin a# ected by fatty acid salts. J. Food Sci., 0+, 3*03+* & 3,* proteins using fourier transform raman spectroscopy ( +330). and self-deconvolution. J. Agric. Food Chem., /,, 0.1* ++ Yuno-Ohta, N. and Corredig, M., Characterization of 0.11 (,**.). b-lactoglobulin A in the presence of sodium caprate by +1 Jackson M. and Mantsch, H.H., The use and misuse of ultrasound spectroscopy and electron microscopy. FTIR spectroscopy in the determination of protein Biomacromolecules, 2,,/.,,/.2 (,**1). structure, Crit. Rev. Biochem. Mol. Biol., -*, 3/ +,* ( +33/ ). +, Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall R. J., Protein measurement with the Folin phenol reagent, ,* +,, J. Biol. Chem., +3-,,0/,1/ ( +3/+ ).

9 Nippon Shokuhin Kagaku Kogaku Kaishi Vol. /,, No.0,,/+,/0 (,**/) 251 * * E#ects of Microbial Transglutaminase on Melting Point and Gel property of G

9 Nippon Shokuhin Kagaku Kogaku Kaishi Vol. /,, No.0,,/+,/0 (,**/) 251 * * E#ects of Microbial Transglutaminase on Melting Point and Gel property of Gelatins Takahiko Soeda, Tomoko Kaneko*, Akiko Hokazono,