ノートルダム清心女子大学

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manaba folio

教員紹介|教員・スタッフのプロフィールをご紹介します。

北畠直文
北畠直文
キタバタケ ナオフミ
生年 1950年12月7日
所属 人間生活学部 食品栄養学科
職名 教授

教員からのメッセージ

食品科学の奥深さ,重要性,面白さを知り,科学的視野・精神・態度を身につけ,偏見や先入観から解放され,自分で物事を理解し,判断できる人間になることを目指しています(自分も含め)。
さらに,食品科学の講義と両輪の関係にある実験化学を通して,食品科学の本質を体得し,学問的方法論を会得して頂くことが次の目標です。
これらの幅広い勉強と研究活動によって,自分を見つめ,自然に学び,人類の知恵を知る人間に成長することを願っています(自分も含め)。

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連絡先

〒700-8516岡山市北区伊福町2-16-9
ノートルダム清心女子大学
人間生活学部 食品栄養学科
電話:  086-252-5389
E-mail: kitabatake@post.ndsu.ac.jp

所属学会

日本食品科学工学会
日本農芸化学会
日本生化学会
日本栄養食糧学会
日本アフリカ学会

取得学位

農学博士(京都大学)

出身大学院・研究科等

昭和51年 京都大学 農学研究科 食品工学専攻 修士課程修了
昭和54年 京都大学 農学研究科 食品工学専攻 博士後期課程単位取得

出身大学・専攻等

昭和49年 京都大学 農学部 食品工学科卒業

研究分野(キーワード)

食品の味,匂い,食感に関する研究
(1) 渋味の研究
渋味は柿渋や茶渋に見られる味刺激です。また,雑味と呼ばれる不快な味の主成分であると云われています。この渋味の実体解明をめざしています。
(2) 食品香気,香料の成分分析
食品香料ならびに食品中の香気成分の分析を進めています。
(3) デンプン食品の物性
キャッサバ芋,キャッサバデンプンの物性と構造との関係について,生化学的手法,レオロジー的方法論を用いて解析を行います。

論文

●片桐実菜,北畠直文;ドウとバッターの構造と特性 小麦粉の非グルテン系成分のドウ,バッターの特性に与える影響,化学と生物, 52(8), 530-534, 2014.

●Murakami T., Kitabatake N., Tani F.; Dispersion in the presence of acetic acid or ammonia confers gliadin-like characteristics to the glutenin in wheat gluten., J Food Sci. 80(2):C269-278, 2015.

●Kubo R, Ohta K, Funakawa S, Kitabatake N, Araki S, Izawa S.; Isolation of lactic acid-tolerant Saccharomyces cerevisiae from Cameroonian alcoholic beverage., J Biosci Bioeng. 118(6):657-660, 2014.

 Masuda T., Taguchi W., Sano A., Ohta K., Kitabatake N., Tani F.: Five amino acid residues in cysteine-rich domain of human T1R3 were involved in the response for sweet-tasting protein, thaumatin., Biochimie. (2013)

●Masuda T., Ohta K., Mikami B., Kitabatake N., Tani F.: Atomic structure of the sweet-tasting protein thaumatin I at pH 8.0 reveals the large disulfide-rich region in domain II to be sensitive to a pH change, Biochem Biophys. Res. Commun., 419(1), 72-76 (2012).

●Ohue R., Nakamoto M., Kitabatake N., Tani F.: Changes in lamina propria dendritic cells on the oral administration of exogenous protein antigens during weaning., Cytotechnology64(3), 221-230 (2012).

●Katagiri M., Masuda T., Tani F., Kitabatake N., Changes in textural properties of Japanese tenobe somen noodles during storage, J. Food Sci., 76(9), S500-507 (2011).

●Ohta K., Masuda T., Tani F., Kitabatake N.: Introduction of a negative charge at Arg82 in thaumatin abolished responses to human T1R2-T1R3 sweet receptors., Biochem Biophys Res Commun., 413(1), 41-45 (2011).

●Ohue R., Hashimoto K., Nakamoto M., Furukawa Y., Masuda T., Kitabatake N., Tani F.: Bacterial heat shock protein 60, GroEL, can induce the conversion of naïve T cells into a CD4 CD25(+) Foxp3-expressing phenotype. J. Innate Immun., 3(6), 605-613 (2011).

●Ohta K., Masuda T., Tani F., Mikami B., Kitabatake N.: Crystal structure of the sweet-tasting protein thaumatin II at 1.27Å. Biochem Biophys Res Commun., 410(3), 457-460 (2011).

●Ohta K., Mikami B., Kitabatake N.: High-resolution structure of the recombinant sweet-tasting protein thaumatin I. Masuda T., Acta Crystallogr Sect F Struct Biol Cryst Commun., 67(Pt 6), 652-658 (2011).

●Ohta K., Masuda T., Tani F., Kitabatake N.: The cysteine-rich domain of human T1R3 is necessary for the interaction between human T1R2-T1R3 sweet receptors and a sweet-tasting protein, thaumatin., Biochem Biophys Res Commun.406(3), 435-438 (2011).

●Katagiri M., Masuda T., Tani F., Kitabatake N.: Expression and development of wheat proteins during maturation of wheat kernel and the rheological properties of dough prepared from the flour of mature and immature wheat. Food Sci. Technol. Res.,17(2), 111-120 (2011).

●Masuda T., Ide N., Ohta K., Kitabatake N.: High-yield secretion of the recombinant sweet-tasting protein thaumatin I. Food Sci. Technol. Res., 16(6), 585-592 (2010).

●Tani F, Nishikawa S, Yokoyama I, Hashimoto K, Nakamoto M, Nomura M, Tao Y, Kitabatake N.: Lymphoid neoplastic P388D1 cells express membrane protein candidates that discriminate among the C-terminal phylogenetic diversity I heat shock protein 70 sequences. Mol Immunol., 48, 191-202 (2010).

●Katagiri M, Kitabatake N.: Rheological properties of somen noodles: a traditional Japanese wheat product.: J Food Sci., 75, E51-8 (2010).

Ide N., Sato E. Ohta K.,Masuda T., Kitabatake N.: Interactions of the sweet-tasting proteins thaumatin and lysozyme with the human sweet-taste receptor. , J Agric Food Chem., 57, 5884-5890 (2009).

●Tani F., Ohno M., Furukawa Y., Sakamoto M., Masuda S., Kitabatake N.: Surface expression of a C-terminal alpha-helix region in heat shock protein 72 on murine LL/2 lung carcinoma can be recognized by innate immune sentinels. Mol. Immunol. ,46, 1326-1339 (2009).

●Ohta K, Masuda T, Ide N, Kitabatake N.: Critical molecular regions for elicitation of the sweetness of the sweet-tasting protein, thaumatin I. FEBS J., 275; 3644-3652 (2008).

●Ohue R., Tani F., Kitabatake N.: Effects of CpG-oligodeoxynucleotides on dendritic cell development. Nucleic Acids Symp Ser (Oxf).,52, 647-648 (2008).

●Ohta K, Masuda T, Ide N, Kitabatake N.: Critical molecular regions for elicitation of the sweetness of the sweet-tasting protein, thaumatin I. FEBS J. 275, 3644-3652 (2008).

Ide N, Masuda T, Kitabatake N.: Effects of pre- and pro-sequence of thaumatin on the secretion by Pichia pastoris. Biochem Biophys Res Commun.363(3),708-714(2007)

Ide N, Kaneko R, Wada R, Mehta A, Tamaki S, Tsuruta T, Fujita Y, Masuda T, Kitabatake N. Cloning of the thaumatin I cDNA and characterization of recombinant thaumatin I secreted by Pichia pastoris.  Biotechnol Prog.;23(5):1023-1030 (2007).

●Tao Y., Nomura M., Kitabatake N., and Tani F.; Mouse CD40-transfected cell lines cannot exhibit the binding and RANTES-stimulating activity of exogenous heat shock protein 70. Mol. Immunol. 44; 1262-1273 (2007).

●Ohno M., Kitabatake N., and Tani F.; Functional region of mouse heat shock protein 72 for its binding to lymphoid neoplastic P388D1 cells. Mol. Immunol. 44; 2344-2354 (2007).

●Masuda T. Kitabatake N.; Developments in biotechnological production of sweet proteins. J. Biosci. Bioeng. 102; 375-389 (2006).

●Wada R., Fujita Y., and Kitabatake N.; Effects of heating at neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy. Biochim. Biophys. Acta 1760, 841-847 (2006).

●Hirose, J., Doi Y., Kitabatake N., Narita H.; Ovalbumin-related gene Y protein bears carbohydrate chains of the ovomucoid type. Biosci Biotechnol Biochem. 70, 144-151. (2006).

●Masuda T., Ide N., and Kitabatake N.; Structure-sweetness relationship in egg white lysozyme: role of lysine and arginine residues on the elicitation of lysozyme sweetness. Chem. Senses. 30, 667-681 (2005).

●Tao Y., Nishikawa S., Nomura M., Kitabatake N. and Tani F.; Biotinylation of heat shock protein 70 induces RANTES production in HEK293 cells in a CD40-independent pathway. Biochem. Biophys. Res. Commun. 338, 700-709 (2005).

●Hirose J. Murakami-Yamaguchi, Ikeda, Kitabatake N., and Narita H.: Oligoclonal enzyme-immunosorbent assay capable of determining the major food allergen, ovomucoid, irrespective of the degree of heat denaturation Cytotechnol. 47, 145-149 (2005).

●Sano H., Egashira T., Kinekawa Y., Kitabatake N.; Astringency of bovine milk whey protein, J. Dairy Sci., 88, 2312-2317 (2005).

●Masuda T., Ide N., Kitabatake N.; Effects of chemical modification of lysine residues on the sweetness of lysozyme. Chemical Senses. 30, 253-264 (2005).

●Hirose J., Yamaguchi Y. M., Ikeda M., Kitabatake N., Narita H., Determination of the major food allergen, ovomucoid, with an Oligoclonal Sandwich ELISA. Biosci. Biotechnol. Biochem.

●Masuda, T., Ueno, Y., Kitabatake N., High yield secretion of the sweet-tasting protein lysozyme from the yeast Pichia pastoris, Protein Expression and Purification, 39, 35-42 (2005)

●Ohno M., Kitabatake N., Tani F., Role of the C-terminal region of mouse inducible Hsp 72 in the recognition of peptide substrate for chaperone activity., FEBS Lett., 576(3) 381-386 (2005).

●Hirose J., Kitabatake N., Kimura A., Narita H., Recognition of native and/or thermally induced denatured forms of the major food allergen, ovomucoid, by human IgE and mouse monoclonal IgG anitibodies. Biosci. Biotechnol. Biochem., 68(12), 2490-2497 (2004).

●Gimbi D. M., Kitabatake N., Effects of storage temperature and relative humidity on a-amylase activity in germinated finger millet grains and flour, Int. J. Food Sci. Nutr.

●Tani F., Shirai, N. Nakanishi, Y. Yasumoto K., Kitabatake N.: Role of a carbohydrate chain and two phosphate moieties in the kinetic refolding of hen ovalbumin., Biosci. Biotechnol. Biochem., 68 (12) 2466-2476 (2004).

●Masuda, T., Tamaki, S., Kaneko, R.,, Wada, R., Fujita, Y., Mehta, A., Kitabatake, N.: Cloning, expression and characterization of recombinant sweet-protein thaumatin II using the methylotrophic yeast Pichia pastoris. Biotechnol Bioeng., 85(7):761-9 (2004).

Kitabatake N., Gimbi, D. M. and Oi Y.: Traditional Non-alcoholic Beverage, Togwa, in East Africa, produced from maize flour and germinated finger millet. Int. J. Food Sci. Nutr. 54 (6) 447-455 (2003).

●Oi Y., Kitabatake N.: Chemical composition of an East African traditional beverage. Togwa. J. Agric. Food Chem. 51 (24), 7024-7028 (2003).

●Oi Y., Kitabatake N.; Analysis of carbohydrate in an East African traditional beverage, Togwa., J. Agric. Food Chem. 51 (24) 7029-7033 (2003).

●Tani F., Shirai N., Nakanishi N., Y., Kitabatake N.: Analysis of molecular Interactions in heat-induced aggregation of a non-inhibitory serpin ovalbumin using molecular chaperone. Biosci. Biotechnol. Biochem., 67 1030-1038 (2003).

●Photchanachai S., Kitabatake N.: Heating of an ovalbumin solution at neutral pH and high temperature, Biosci. Biotechnol. Biochem., 66(8), 1635-1640 (2002).

●Gimbi D. M., Kitabatake N.: Changes in α and β-amylse activities during seed germination of African finger millet, Int. J. Food Sci. Nutr., 53(6):481-488 (2002).

●Hirota M., Alka B. Mehta, Yoneyama K., Kitabatake N.: A major decomposition product, citrinin H2, from citrinin on heating with moisture. Biosci. Biotechnol. Biochem., 66 (1), 206-210 (2002).

●Hirose J., Ito S., Kido S., Kitabatake N., Narita H., Occurrence of the major food allergen, ovomucoid, in human breast milk as an immune complex. Biosci. Biotechnol. Biochem., 65 (6), 1438-1440 (2001).

●Wada R.. Kitabatake N.: β-Lactoglobulin A, of which sulfhydryl residue was completely modified with N-ethylmaleimide, polymerized through intermolecular disulfide bridge on heating in the presence of dithiothreitol. J. Agric. Food Chem. 49 (10), 4971-4976 (2001).

●Masuda T., Ueno Y., Kitabatake N.: Sweetness and hydrolytic activity of lysozyme, J. Agric. Food Chem. 49(10), 4937-4941 (2001).

●Koga Y., Koga T., Kinekawa Y., and Kitabatake N., Properties of thermostable emulsion prepared with the process whey protein and olive oil; use for a cream-substitute and its practical application to panna-cotta, J. Cookery Sci. Jp., 34, 32-41(2001). 

●Photchanachai S., Kitabatake N.: Heating of β-lactoglobulin A solution in a closed system at high temperatures. J. Food Sci., 66 (5), 647-652 (2001).

Kitabatake N., Wada R., and Fujita Y.: Reversible conformational change in the β-lactoglobulin A modified with N-ethylmaleimide and resistance to molecular aggregation on heating. J. Agric. Food Chem., 49(10), 4011-4018 (2001).

●Kaneko R., Kitabatake N.: Structure-sweetness relationship in thaumatin: importance of lysine residues. Chemical Senses, 26, 167-177 (2001).

●Kaneko R., Kitabatake N.: Sweetness of sweet protein thaumatin is more thermoresistant under acid conditions than under neutral or alkaline conditions. Biochem., Biophys. Biosci. 65(2), 409-413 (2001).

Kitabatake N., Fujita Y.: Functionality of dialyzed soybean extract. J. Amer. Oil Chem. Soc. 77 (4) 441- 446 (2000).

●Masuda T., Koseki S-Y., Yasumoto K., Kitabatake N.: Characterization of anti irradiation-denatured ovalbumin monoclonal antibodies. Immunochemical and structural analysis of irradiation-denatured ovalbumin. J. Agric Food Chem. 48 (7) 2670-2674 (2000).

●Masuda T., Yasumoto K., Kitabatake N.: Monitoring the irradiation-induced conformational changes of ovalbumin using monoclonal antibodies and surface plasmon resonance. Biosci. Biotech. Biochem. 64 (4) 710-716 (2000).

●Kaneko, R., Kitabatake N.: Heat-induced formation of intermolecular disulfide linkages between thaumatin molecules that do not contain cysteine residues. J. Agric. Food Chem., 47, 4950-4955 (1999).

●Koga Y., Izumi T., Kinekawa Y., Kitabatake N.: Effects of NaCl, sucrose and heat treatment on the emulsification properties of Process Whey Protein. J. Cookery Sci. Jp., 32, 2-9 (1999).

Kitabatake N., Kinekawa Y.: Digestibility of bovine milk whey protein and β-lactoglobulin in vitro and in vivo. J. Agric. Food Chem. 46, 4917-4923 (1998).

●Kinekawa Y., Fuyuki T., Kitabatake N.: Effects of salts on the properties of sols and gels prepared from whey protein isolate and Process Whey Protein. J. Dairy Sci., 81, 1532-1544 (1998).

●Laswai H.S., Wendelin A.M., Kitabatake N., Mosha T.C.E.: The Under- exploited indigenous alcoholic beverages of Tanzania: production, consumption and quality of the undocumented "Denge". African Study Monographs, 18, 29-44 (1997).

Kitabatake N., Fujita Y., Kinekawa Y.: Viscous sol and gel formation from Process Whey Protein below 25oC. J. Food Sci., 61, 500-503 (1996).

●Kinekawa Y., Kitabatake N.: Purification of β-lactoglobulin from whey protein concentrate by pepsin treatment. J. Dairy Sci., 79, 350-356 (1996).

Kitabatake N., Kinekawa Y.: Turbidity measurement of heated egg proteins using a microplate system. Food Chem., 54, 201-203 (1995).

●Kinekawa Y., Kitabatake N.: Turbidity and rheological properties of gels and sols by heating process whey protein. Biosci. Biotech. Biochem., 59, 834-840 (1995).

●Tani F., Murata M., Higasa T., Goto M., Kitabatake N., Doi E.: Molten globule state of protein molecules in heat-induced transparent food gels. J. Agric. Food Chem., 43, 2325-2331 (1995). 

Kitabatake N., Doi E. and Kinekawa Y.: Simple and rapid method for measuring turbidity in gels and sols from milk whey protein. J. Food Sci., 59, 769-772 (1994).

●Watanabe T., Kitabatake N., Doi E.: Method for the accurate measurement of freezing-induced denaturation of ovalbumin with 5, 5-Dithiobis-(2-nitrobenzoic acid). Biosci. Biotech. Biochem., 58, 359-362 (1994).

●Doi E., Tani F., Murata M., Koseki T., Kitabatake N.: Heat-induced transparent gels of globular proteins. Food Hydrocolloids, 8, 317-325 (1994).

●Fouler S., Trivedi A., Kitabatake N.: Detoxification of citrinin and ochratoxin A by hydrogen Peroxide. J. Assoc. Off. Anal. Chem., 77, 631-637 (1994).

●Murata M., Tani F., Higasa T., Kitabatake N., Doi E.: Heat-induced transparent gel formation of bovine serum albumin. Biosci. Biotech. Biochem., 57, 43-46 (1993).

●Tani F., Mutara M., Higasa T., Goto M., Kitabatake N., Doi E.: Heat-induced transparent gel from hen egg lysozyme by a two-step heating method. Biosci. Biotech. Biochem., 57, 209-214 (1993).

●Trivedi A., Hirota M., Kitabatake N.: Formation of a new toxic compound, citrinin H1, from citrinin on mild heating in water. J. Chem. Soc. Perkin Trans. I., 2167-2171 (1993).

Kitabatake N., Doi E., Trivedi A.: Toxicity evaluation of mycotoxins, citrinin and ochratoxin A using several animal cell lines. Com. Biochem. Physiol., 105, 429-433 (1993).

●Trivedi A., Doi E., Kitabatake N.: Toxic compounds formed on prolonged heating of citrinin under watery conditions. J. Food Sci., 58, 229-232 (1993).

●Koseki M., Seki H., Funayama K., Tsuji K., Kitabatake N., Tochikura T.: Effects of corn oil and pectin on the production of short-chain fatty acids in the cecum, on the growth of colonic bacteria, and on the liver cholesterol level in rats. Biosci. Biotech. Biochem., 57, 315-316 (1993).

●Yonemoto Y., Tanaka H., Yamashita T., Kitabatake N., Ishida Y., Kimura A., Murata K., Promotion of germination and shoot elongation of some plants by alginate oligomers prepared with bacteiral alginate lyase. J. Ferment. Bioeng., 75, 68-70 (1993).

●Trivedi A., Doi E., Kitabatake N., Detoxification of ochratoxin A on heating under acidic and alkaline conditions. Biosci. Biotech. Biochem., 56, 741-745 (1992).

●Trivedi A., Doi E., Kitabatake N.: Cytotoxicity of citrinin heated at temperatures above 100C. Biosci. Biotech. Biochem., 56, 423-426 (1992).

●Ikura K., Higashiguchi, F., Kitabatake N., Doi E., Narita H., and Sasaki R.: Thermally induced epitope regions of ovalbumin identified with monoclonal antibodies. J. Food Sci., 57, 635-639 (1992) .

●Fukuda T., Tsuji Y., Koseki T., Kitabatake N., Doi E.: Conformation of linear aggregates of thermally denatured ovalbumin. Macromol., 24, 6786-6787 (1991).

●Doi E., Shimizu A., Oe H., Kitabatake N.: Melting of heat-induced ovalbumin gel by pressure. Food Hydrocolloids, 5, 409-425 (1991)

Kitabatake N., Trivedi A. and Doi E.: Thermal decomposition and detoxification of citrinin under various moisture conditions. J. Agric. Food Chem., 39, 2240-2244 (1991).

●Shimizu A., Kitabatake N., Higasa T. and Doi E.: Melting of the ovalbumin gels by heating: reversibility between gel and sol. Nippon Shokuhin Kogyo Gakkaishi, 38, 1052-1056 (1991).

●Koseki M., Tsuji K., Kazama, M., Kitabatake N., Doi E.: Interaction between dietary cholesterol or fatty acids and water-soluble fibers and increase in cholesterol excretion by pectin in rats. Nippon Shokuhin Kogyo Gakkaishi, 37, 559-564 (1990).  

●Kitabatake N., Tahara M., Doi E.: Thermal denaturation of soybean protein at low water contents. Agric. Biol. Chem., 54, 2205-2212 (1990).

●Trivedi A. B., Kitabatake N., Doi E.: Toxicity of dimethyl sulfoxide as a solvent in bioassay system with HeLa Cells evaluated colorimetrically with 3-(4, 5 dimethyl hiazol-2-yl)-2,5-diphenyl-tetrazolium bromide. Agric. Biol. Chem., 54, 2961-2966 (1990).

●Koseki T., Kitabatake N., Doi E.: Freezing denaturation of ovalbumin at acid pH. J. Biochem., 107, 389-394 (1990).

●Koseki T., Kitabatake N., Doi E.: Irreversible thermal denaturation and formation of linear aggregates of ovalbumin. Food Hydrocolloids, 3, 123-134 (1989).

●Koseki T., Fukuda T., Kitabatake N., Doi E.: Characterization of linear polymers Induced by thermal denaturation of ovalbumin. Food Hydrocolloids, 3, 135-148 (1989).

●Doi E., Kitabatake N.: Structure of glycinin and ovalbumin gels. Food Hydrocolloids, 3, 327-337 (1989).

Kitabatake N., Tahara M., Doi E.: Denaturation temperature of soy protein under low moisture conditions. Agric Biol.Chem., 53, 1201-1202 (1989).

●Koseki M., Tsuji K., Nakagawa Y., Kawamura M., Ichikawa T., Kazama M., Kitabatake N., Doi E.: Effects of gum arabic and pectin on the emulsification, the lipase reaction, and the plasma cholesterol level in rats. Agric. Biol. Chem., 53, 3127-3132 (1989).

Kitabatake N., Shimizu A., Doi E.: Comparison of transparent gels with turbid gels prepared from egg white, creep analysis of gels. J. Food Sci., 54, 1209-1212 (1989).

Kitabatake N., Indo K. and Doi E.: Changes in interfacial properties of hen egg ovalbumin caussed by freeze-drying and spray-drying. J. Agric. Food Chem., 37, 905-910 (1989).

Kitabatake N., Tani Y. and Doi E.: Rheological propereties of heat-induced ovalbumin gels prepared by two-step and one-step heating methods. J. Food Sci., 54, 1632-1638 (1989).

Kitabatake N., Doi E.: Surface tension and foamability of protein and surfactant solutions., J. Food Sci., 53, 1542-1545, 1569 (1988).

●Watanabe T., Kitabatake N., Doi E.: Protective effects of non-ionic surfactants against denaturation of rabbit skeletal myosin by freezing and thawing. Agric.Biol.Chem., 52, 2517-2523 (1988).

Kitabatake N., Indo K., Doi E.: Limited proteolysis of ovalbumin by pepsin. J. Agric. Food Chem., 36, 417-420 (l988).

●Koseki T., Kitabatake N., Doi E.: Conformational changes in ovalbumin at acid pH., J. Biochem., 103, 425-430 (1988).

Kitabatake N., Shimizu A. and Doi E.: Protein components precipitated from egg white by removal of salt, J. Food Sci., 53, 292-293 (1988).

Kitabatake N., Shimizu A. and Doi E.: Preparation of transparent egg white gel with salt by two-step heating method. J. Food Sci., 53, 735-738 (1988).

Kitabatake N., Shimizu A. and Doi E.: Preparation of heat-induced transparent gels from egg white by the control of pH and ionic strength of the medium. J. Food Sci., 53, 1091-1095 (1988).

Kitabatake N., Ishida A. and Doi E.: Physicochemical and functional properties of hen ovalbumin dephosphorylated by acid phosphatase. Agric. Biol. Chem., 52, 967-973 (1988).

Kitabatake N., Ishida A., Yamamoto K., Tochikura T. , Doi E.: Deglycosylation of hen ovalbumin in native form by endo-β-N-acetylglucosaminidase. Agric. Biol. Chem., 52, 2511-2516 (l988).

Kitabatake N., Doi E.: Properties of ovalbumin limited-proteolyzed by pepsin on heating. Agric. Biol. Chem., 52, 3175-3176 (1988).

Kitabatake N., Shimizu Y. and Doi E.: Continuous production of fish meat sol using a twin-screw extruder., J. Food Sci., 53, 344-348 (1988).

●Koseki M., Kitabatake N., Doi E., Yasuno T., Ogino S., Kazama N., Doguchi M.: Binding of taurocholate by pectin in the presence of calcium ions. J. Food Sci., 52, 1744-1745 (1987).

Kitabatake N., Doi E.: Conformational change of hen egg ovalbumin during foam formation detected by 5,5'-dithiobis (2-nitrobenzoic acid). J. Agric. Food Chem., 35, 953-957(1987).

Kitabatake N., Hatta H., Doi E.: Heat-induced and transparent gel prepared from hen egg ovalbumin in the presence of salt by two-step heating method. Agric. Biol. Chem., 51, 771-778(1987).

●Doi E., Koseki T., Kitabatake N.: Effects of limited proteolysis on functional properties of ovalbumin. J. Amer. Oil Chemists Soc., 64. 1697-17O3 (1987).

●Hatta H., Kitabatake N., Doi E.: Turbidity and hardness of a heat-induced gel of hen egg ovalbumin. Agric. Biol. Chem., 50, 2083-2089 (1986).

Kitabatake N., Doi E. : Measurement of temperature of food material during extrusion cooking. Agric. Biol. Chem., 50, 1677-1678 (1986).

●Kato T., Kitabatake N., Doi E.: Effects of saliva on the viscosity of gum solutions. Agric. Biol. Chem., 50, 3207-3208 (1986).

●Koseki M., Kitabatake N., Doi E., Yasuno T., Ogino S., Ito A. and Endo F.: Determination of pectin in the Presence of food polysaccharides. J. Food Sci., 51, 1329-1332 (1986).

Kitabatake N., Doi E.: Heat-induced transparent gels prepared from pepsin treated ovalbumin and egg white. Agric. Biol. Chem. 49, 2457-2458 (1985).

Kitabatake N., Cuq J-L. and Cheftel J. C.: Covalent binding of glycosyl residues to β-lactoglobulin: effects on solubility and heat stability. J. Agric. Food Chem., 33, 125-130 (1985).

Kitabatake N., Megard D. and Cheftel J. C.: Continuous gel formation by HTST extrusion-cooking: soy proteins. J. Food Sci., 50, 1260-1265 (l985).

●Megard D., Kitabatake N., Cheftel J. C.: Continuous restructuring of mechanically deboned chicken meat by HTST extrusion-cooking. J. Food Sci., 50, 1364-1369 (1985).

Kitabatake N., Doi E.: Surface tension and foaming of protein solutions. J. Food Sci., 47, 1214-1221 (1982).

Kitabatake N., Doi E.: A proposal for the expression of the foamability of protein solutions. Agric. Biol.Chem., 46, 2177-2178 (l982).

Kitabatake N., Sasaki H., Doi E.: Scanning electron microscopy of freeze-dried protein foams. Agric. Biol. Chem., 46, 2881-2883 (1982).

●Sasaki R., Okumura K., Kitabatake N., Kitabatake N., Chiba H.: Changes of aldehyde levels in defatted soybean extract. J. Food Sci., 47, 31-35 (1982).

Kitabatake N., Sasaki R., Chiba H.: Localization of bovine liver aldehyde dehydrogenase isozymes and thier immunological properties. J. Biochem., 89, 1223-1229 (1981).

Takahashi* N., Kitabatake N., Sasaki R., and Chiba H.: Enzymatic improvement of food flavor V. oxidation of aldehydes in soybean extracts by an NAD+-regenerating system made up of aldehyde dehydrogenase and diaphorase. Agric. Biol Chem., 44, 1669-1670 (1980).

Takahashi* N., Sasaki R., Chiba H.: Enzymatic improvement of food flavor IV. oxidation of aldehydes in soybean extracts by aldehyde oxidase. Agric. Biol. Chem., 43, 2557-2561 (1979).

●Chiba H., Takahashi* N., Kitabatake N., and Sasaki R.: Enzymatic improvement of food flavor III. oxidation of the soybean protein-bound aldehyde by aldehyde dehydrogenase. Agric. Biol. Chem., 43, 1891-1897 (1979).

●Chiba H., Takahashi* N., and Sasaki R.: Enzymatic improvement of flavor II. removal of beany flavor from soybean products by aldehyde dehydrogenase. Agric. Biol. Chem., 43, 1883-1889 (1979).

Takahashi* N., Kitabatake N., Sasaki R., and Chiba H.: Enzymatic improvement of food flavor I. Purification and characterization of bovine liver mitochondrial aldehyde dehydrogenase. Agric. Biol. Chem., 43, 1873-1882 (1979).

●Sugimoto E., Takahashi* N., Kitagawa Y., and Chiba H.: Intracellular localization and characterization of beef liver aldehyde dehydrogenase isozymes. Agric. Biol. Chem., 40, 2063- 2070 (1976) .

* Kitabatake (formerly Takahashi) Naofumi

 

学会及び学会活動(役員など)

2012年4月~  日本食品科学工学会 副会長
2011年4月~  日本農芸化学会中四国支部参与

著書

北畠直文|著作紹介|Webcat plus▶
※検索結果には、論文が網羅されない場合や、同姓同名の著者が含まれる場合があります。

外部資金・競争的資金:科研費

科学研究費基盤研究C(一般)平成25年度~平成29年度
「食物・食品の渋みの機構解析と評価」 代表

教育活動:作成した教科書・教材

●太田英明,北畠直文,白土英樹編集「食品の科学 食べ物と健康」2015 南江堂
●太田英明,北畠直文,白土英樹編集「食品の加工 食べ物と健康」2015 南江堂
 

その他教育活動

長崎大学非常勤講師

担当科目

所属学科

食品学Ⅰ,食品学Ⅱ,健康の保持・増進Ⅲ,
食品学実験a, 食品学実験b,栄養学基礎演習,栄養学応用演習,栄養学総合演習

大学院

食品学特論Ⅰ,食品学特論Ⅱ

学内組織における職歴(役職等)

食品栄養学科 学科長

その他活動

●岡山県食品新技術応用研究会 幹事
●中国四国農林水産・食品先進技術研究会 食品専門部会長
●産学連携支援事業コーディネーター(中四国アグリテック)