SARAN

V. SIMPULAN DAN SARAN

5.2. SARAN

Berbagai data dan hipotesa berdasarkan analisis yang dilakukan pada penelitian ini memberikan referensi kepada industri tahu agar dapat menggunakan suhu koagulasi dan konsentrasi koagulan CaSO4 optimum agar memperoleh tahu yang disukai konsumen. Dengan persamaan linear

yang mengkorelasikan tekstur objektif dan subjektif yang sudah ada, industri dapat melakukan uji ranking kesukaan terhadap curd tahu (telah terukur secara objektif) sekaligus mendeskripsikannya secara kualitatif. Selain itu, memungkinkan juga bagi industri untuk menganalisis varietas kedeleai yang digunakan sebagai bahan baku produksi. Sehingga dapat memilih varietas yang sejak awalnya memliki glisinin lebih banyak agar produksi tahu menghasilkan rendemen, kadar air, dan teksturnya lebih baik dan sesuai dengan keinginan konsumen.

Pengamatan pengaruh suhu koagulasi dan konsentrasi koagulan terhadap perubahan tekstur akan lebih jelas diketahui dengan mengamati struktur fisik jaringan secara mikroskopis dengan menggunakan scanning electron microscope (SEM). Selain itu, dapat dilakukan juga fraksinasi 11S dan 7S protein tahu dengan metode yang tepat untuk mengetahui komponen subuinit protein yang lebih terkelompokkan jelas dan terperinci ketika dilakukan analisis protein dengan elektroforesis. Dan sebagai upaya peningkatakan kontras antar subunit protein, terutama subunit asam dari protein 11S, kepadatan gel elektroforesis dapat ditingkatkan dari yang dilakukan pada penelitian ini.

Kemudian, dari segi analisis konsentrasi optimum, penelitian lebih lanjut dapat difokuskan pada selang konsentrasi 0.030-0.045 N sehingga dapat diperoleh korelasi yang lebih akurat antar variabel transmittan whey, kadar protein whey, kadar air curd, total padatan curd, dan profil protein

curd. Analisis tekstur dan profil protein curd pun sebaiknya dilakukan dengan bahan analisis curd

yang dibuat pada skala yang sama. Di samping itu, waktu koagulasi pengamatan diperpanjang, lebih dari 10 menit, untuk mencapai koagulasi yang lebih sempurna. Koagulasi tersebut dilakukan pada suhu mulai dari 70°C, dan lebih baik pada suhu 93°C.

DAFTAR PUSTAKA

American Chemical Society. 2006. Reagent chemicals: specifications and procedures : American Chemical Society specifications, official from January 1, 2006. Oxford University Press. p. 242. ISBN 0841239452.

Anomima. -. http://www.texturetechnologies.com. [23 Februari 2011] Anomimb. -. http://iopscience.iop.org. [8 Juni 2011]

Anomimc. 2006. National Human Genome Research Institute. http://www.genome.gov/Pages/ Hyperion/DIR/VIP/Glossary/Illustration/Protein.shtml. National Institutes of Health. [8 Juni 2011]

Anomimd. 2008. Main Protein Structure Levels. http://kvhs.nbed.nb.ca/gallant/biology/quarternary_ structure.jpg. [8 Juni 2011]

Badley RA, Atkinson D, Hauser H, Oldani D, Green JP, Stubbs JM. 1975. The structure, physical, and chemical properties of the soybean protein glycinin. Biochem Biophys Acta 412: 214. Bailey PD. 1992. An Introduction to Peptide Chemistry. Chichester, New York: John Willey and

Sons.

Beddows CG, Wong J. 1987. Optimization of yield and properties of silken tofu from soybean iii. Coagulant concentration, mixing, and filtration pressure. Intl J Food Technol 22: 29-34. Beilinson V, Chen Z, Shoemaker RC, Fischer RL, Goldberg RB, Nielsen NC. 2002. Genome

organization of glycinin genes in soybean. TAG 104: 1132–1140.

Belitz HD, Grosch W. 1999. Food Chemistry. Berlin: Springer-Verlag.

Blazek V. 2008. Chemical and biochemical factors that influence the gelation of soybean protein and the yield of tofu [tesis]. Sydney: Faculty of Agriculture, Food and Natural Resources, The University of Sydney.

Boyer RF. 1993. Modern Experimental Biochemistry. 2nd ed. California: The Benjamin Cumming Pb. Co., Inc.

Burks AW, Butler HL, Brooks JR, Hardin J, Connaughton C. 1988. Identification and comparison of differences in antigens in two commercially available soybean protein isolates. J Food Sci 53: 1456.

Cai TD, Chang KC. 1998. Characteristic of production scale tofu as afected by soymilk coagulation method: propellerblade size, mixintime and coagulation concentration. Food Res Intl 31: 289- 295.

Chaftel JC, Cu JJ. 1985. Amino Acids, Peptides, and Proteins. In: Copeland RA (ed). Methods for Protein Analysis: A Practical Guide Laboratory Protocol. 3rd ed. New York, London: Chapman and Hall.

Copeland RA. 1994. Methods for Protein Analysis : A Practical Guide Laboratory Protocol. 3rded. New York, London: Chapman and Hall.

Damodaran S. 1982. Functional properties. In: Fox PF, Condon JJ (eds). Food Proteins. London, New York: Applied Science Publisher.

Danielson CE. 1949. Seed globulins of the gramineae and leguminosae. J Biochem 44: 387.

Eldridge AC, Wolf WJ. 1967. Purification of the 11S Component of Soybean Protein. Cereal Chem 44: 645-652.

Fahmi R. 2010. Mempelajari pengaruh jenis dan konsentrasi koagulan terhadap pola elektroforesis koagulasi protein serta korelasinya terhadap tekstur curd yang dihasilkan [skripsi]. Bogor: Fakultas Teknologi Pertanian, Institut Pertanian Bogor.

Faridi H, Faubion JM. 1990. Dough Rheology and Baked Product Texture. New York: An AVI Book.

Foegeding EA. 1989. Molecular properties and functionality of proteins in food gels. In: Zayas JF (ed). Functionality of Protein in Food. Verlag Berlin Heidelberg: Springer.

Genovese MI, Lajolo FM. 1993. Composition and structural characteristics of isolated soy proteins from broken and damaged seeds. J Food Sci 58: 148.

Hang YD, Jackson H. 1967. Preparation of soybean cheese using lactic acid starter organism. J Food Technol 21:95-100.

[ISO] International Organization for Standardization. 1981. Sensory Analysis Vocabulary. Jenewa: International Organization for Standardization.

Johnson LD, Wilson LA. 1984. Influence of soybean variety and the method of processing in tofu manufacturing: comparison of methods for measuring soluble solids in soymilk. J Food Sci 49: 202.

Kao FJ, Su NW, Lee MH. 2003. Effect of calcium sulfate consentration in soymilk on the microstructure of firm tofu and the protein constitution in tofu whey. J Agric Food Chem 66: 159-165.

Kim SH, Kinsella JE. 1986. Effects of reduction with dithiothreitol on some molecular properties of soy glycinin. J of Agricl and Food Chem 34: 623-627.

Kinsella JE. 1976. Functional properties of proteins in foods: A survey. CRC Critical Reviews in Food Science and Nutrition 7: 219-280.

Kinsella JE. 1979. Functional properties of soybean protein. J Am Oil Chem Soc 56: 242.

Kinsella JE. 1982. Relationship Between Structure and Functional Properties of Food Proteins. In:

Fox PF, Condon JJ (eds). Food Proteins. London, New York: Applied Science Publisher. Kohyama K, Sano Y, Doi E. 1995. Rheological characteristic and gelation mechanism of tofu

(soybean curd). J Agric Food Chem 43: 1808-1812.

Koshiyama, I. 1972. Comparison of Acid-induced Conformation Changes Between 7S and 11S Globulin in Soybean Seeds. J Sci Food Agric 23: 853-859.

Kusnandar F. 2010. Kimia Pangan: Komponen Makro. Jakarta: Dian Rakyat.

Lakemond CMM, deJongh HHJ, Hessing M, Gruppen H, Voragen AGJ. 2000. Soy Glycinin: Influence of pH and Ionic Strength on Solubility and Molecular Structure at Ambient Temperatures. J Agric Food Chem 48: 1985-1995.

Lehninger. 1995. Dasar-dasar Biokimia. Vol 1. Jakarta: Erlangga.

Lewis BA, Chen JH. 1979. Effect of Conformation and Structure Change Induced by Solvent and Limited Enzyme Modification on the Functionality of Soy Protein. In: El AP (ed).

Functionality and Protein Structure. Washington DC: American Chemical Society.

Liu C, Wang X, Ma H, Zhang Z, Gao W, Xiao L. 2008. Functional properties of protein isolates from soybeans stored under various conditions. J Food Chem 111:29-37.

Liu KS. 1997. Soybean-Chemistry, Technology, and Utilization. New York: Chapman & Hall. Margono T, Suryati D, Hartinah S. 1993. Buku Panduan Teknologi Pangan. Jakarta: Pusat

Informasi Wanita dalam Pembangunan PDII-LIPI bekerjasama dengan Swiss Development Cooperation.

Maruyama N, Fukuda T, Saka S, Inui N, Kotoha J, Miyagawa M, Hayashi M, Sawada M, Moriyama T, Utsumi S. 2003. Molecular and structural analysis of electrophoretic variants of soybean seed storage proteins. Phytochem 64: 701–708.

Maruyama N, Sato R, Wada Y, Matsumura Y, Goto H, Okuda E, Nakagawa S, Utsumi S. 1999. Strucure-physicochemical function relationships of soybean β-conglycinin constituent subunits. Journal of Agricultural and Food Chemistry 47, 5278-5284.

Micha P. 1987. The Basic of Solid Foods Rheology. In: Moskowitz HR (ed). Food Texture Instrumental and Sensory Measurement. New York: Marcel Dekker, Inc.

Mohamed A, Xu J. 2003. Effect of ionic strength and pH on the thermal and rheological properties of soy protein–amylopectin blend. Food Chem 83: 227–236.

Mujoo R, Trinh DT, Ng P. 2003. Characterization of storage proteins in different soybean varieties and their relationship to tofu yield and texture. Food Chemistry 82: 265–273.

Nagano T, Akasaka T., and Nishinari, K. 1994a. Dynamic viscoelastic properties of glycinin and β- conglycinin gels from soybeans. Biopolymers 34: 1303–1309.

Nagano T, Mori H, Nishinari K. 1994b. Effect of heating and cooling on the gelation kinetics of 7S globulin from soybeans. J of Agric and Food Chem 42: 1415-1419.

Nielsen NC, Dickinson CD, Cho T, Thanh VH, Scallon BJ, Fischer RL. 1989. Characterization of the glycinin gene family is soybean. Plant Cell 1: 313–328.

Nielsen SS. 2003. Food Analysis. 3rded. New York: Plenum Publisher.

Nur AM, Adijuwana H. 1989. Teknik Pemisahan dan Analisis Biologi. Bogor: Pusat Antar Universitas, Institut Pertanian Bogor.

Oakenfull D, Pearce J, Burley RW. 1997. Protein gelation. In: Damodaran S, Paraf A (eds). Foods Protein and Their Applications. New York: Marcel Dekker, Inc., pp 111-142.

Obatolu VA. 2007. Effect of different coagulants on yield and quality of tofu from soymilk. Eur Food Res Technol 226: 467-427.

Oboh G. 2006. Coagulants modulate the hypocholesterolemic effect of tofu (coagulated soymilk). Afr J Biotecnol 5(3): 290-294.

Peng IC, Quass DW, Dayton WR, Allen CE. 1984. The Physicochemical and Functional Properties of Soybean 11S Globulin - A Review. Cereal Chem 61: 480-490.

Poedjiadi A. 1994. Dasar-dasar Biokimia. Jakarta: UI Press.

Pomeranz Y, Meloan CL. 1994. Food Analysis: Theory and Practice. 3rded. New York: Chapman and Hall an International Thomson Publ. Co.

Poysa V, Woodrow L. 2004. Stability of soybean composition and its effect on soymilk and tofu yield and quality. Food Res Intl 35: 337-345.

Poysa V, Woodrow L, YuK. 2006. Effect of soy protein subunit composition on tofu quality. Food Res Int 39: 309–317

Puppo MC, Anon MC. 1999. Soybean protein dispersions at acid pH: Thermal and rheological properties. J of Food Sci 64: 50–56.

Ramlan BMSM, Maruyama N, Takahashi K, Yagasaki K, Higasa T, Matsumura Y. 2004. Gelling properties of soybean β-conglycinin having different subunit compositions. Biosci Biotech and Biochem 68: 1091–1096.Staswick PE, Hermodson MA, Nielsen NC. 1984. Identification of the cystines which link the acidic and basic components of glycinin subunits. J of Biological Chem 259: 13431–13435.

Renkema JMS. 2004. Relations between rheological properties and network structure of soy protein gels. Food Hydrocolloids 18: 39–47.

Renkema JMS, Knabben JHM, van Vliet T. 2001. Gel formation by β-conglycinin and glycinin and their mixtures. Food Hydrocolloids 15(4-6): 407–414.

Rickert DA, Johnson LA, Murphy PA. 2004. Functional properties of improved glycinin and β- conglycinin fractions. J Food Sci 69(4): 303–311.

Rhodes AP , Jenkins G. 1978. Improving the protein quality of cereal grain legumes and oilseed by breeding. In: Norton (ed). Plant Protein. London: Buterworth Ltd.

Rosenthal AJ. 1999. Food Texture, Measurement and Perception. Maryland: An Aspen Publication. Rybicki E, Purves M. 1996. SDS Poliacrylamide Gel Electrophoresis (SDS-PAGE). In: Coyne VE,

James MD, Reid SJ, Rybicki EP (eds). Molecular Bology Techniques Manual. 3rded. http://web.uct.ac.za/microbiology/sdspage.htm.

Saidu JEP. 2005. Development, Evaluation And Characterization Of Protein- Isoflavone Enriched Soymilk. Disertasi. Faculty of Agricultural and Mechanical. Louisiana State University and College, Louisiana.

Saio K, Kamiya M, Watanabe T. 1969. Food processing characteristics of soybean 11S and 7S proteins. Agric and Biological Chem 33: 1301–1308.

Schmidt. 1981. Gelation and coagulation. In: Zayas JF (ed). Functionality of Protein in Food. Verlag Berlin Heidelberg: Springer.

Sheard PR, Fellows A, Ledward DA, Mitchell JR. 1986. Macromolecule changes associated with the heat treatment of soy flour. J of Food Tech 21: 55–60.

Shurtleff W, Aoyagi A. 1984. Tofu and Soymilk Production, The Book of Tofu. Vol II. Lafayete: New Age Food Study.

Smith AK. 1958. Vegetable protein isolates. In: Processed Plant Protein Food-stuff. New York: Academic Press Inc. Publ.

Subardjo SK, Ridwan IN, Handono SW. 1987. Penerapan Teknologi Pengawetan Tahu. Bogor: BPPIHP.

Suciono. 1995. Isolasi dan karakterisasi protein kacang merah (phaseous vulgaris) dan kacang tolo (Vigna unguiculata) lokal serta pengujian sifat antigeniknya sebelum dan sesudah fermentasi asam laktat [skripsi]. Bogor: Fakuktas Teknologi Pertanian, Institut Pertanian Bogor.

Takahashi K, Banba H, Kikuchi A, Ito M, Nakamura S. 1994. An induced mutant line lacking the a- subunit of β-conglycinin in soybean (Glycine max (L.) Merrill). Breeding Sci 46: 65–66.

Takahashi K, Mizuno Y, Yumoto S, Kitamura K, Nakamura S. 1996. Inheritence of a-subunit deficiency of β-conglycinin in soybean (Glycine max (L.) Merrill) line induced by (γ)-ray irradiation. Breeding Sci 46: 251–255.

Tezuka M, Taira H, Igarashi Y, Yagasaki K, Ono T. 2000. Properties of tofus and soy milks prepared from soybeans having different subunits of glycinin. J of Agric and Food Chem 48: 1111– 1117.

Thanh VH, Shibasaki K. 1976. Heterogeneity of betaconglycinin. Biochimica et Biophysica Acta 439: 326–338.

Tanh VH, Shibasaki K. 1977. β-conglycinin from soybean protein. Isolation and immunological and physicochemical properties of the monomeric forms. Biochim Biophys Acta 490: 370.

Thanh VH, Shibasaki K. 1978. Major proteins of soybean seeds: subunit structure of β-conglycinin. J of Agric and Food Chem 26: 692–695.

Utsumi S, Kinsella JE. 1985. Forces involved in soy protein gelation: effect of various reagents on the formation, hardness and solubility of heat-induced gels made from 7S, 11S, and soy isolate. J Food Sci 50: 1278.

Voet DJ, Voet G, Pratt GW. 1999. Fundamentals of Biochemistry. New York: John Willey and Sons, Inc.

Wang CH, Damodaran S. 1990. Thermal gelation of globular protein: weight-average molecular weight dependence of gel strength. J Agric Food Chem 38: 1157.

Wijaya SKS, Rohman L. 2001. Fraksinasi dan karakterisasi protein utama biji kedelai. J Ilmu Dasar 2(1): 49-54.Wilson K, Walker J. 2000. Principles and Techniques of Practical Biochemistry. 5thed. Cambridge: Cambridge University Press.

Wolf WJ, Briggs DR. 1956. Ultracentrifugal investigation of the effect of neutral salts on the extraction of soybean proteins. Arch Biochem Biophys 63: 40.

Wolf WJ, Babcock GE, Smith AK. 1961. Ultracentrifugal differences in soybean protein composition. Nature 191: 395.

Yagasaki K, Kaizuma N, Kitamura K. 1996. Inheritance of glycinin subunits and the characterization of glycinin molecules lacking the subunits in soybean (Glycine max (L) Merr.). Breeding Science 46: 11–15.

Yagasaki K, Kousaka F, Kitamura K. 2000. Potential improvement of soymilk gelation properties using soybean with modified protein subunit compositions. Breeding Sci 50: 101–107.

Yasir SBM, Sutton KH, Newberry MP, Andrews NR , Gerrard JA. 2007. The impact of Maillard cross-linking on soy proteins and tofu texture. Food Chemistry 104: 1502–1508.

Zayas JF. 1997. Functionality of Protein in Food. Verlag Berlin Heidelberg: Springer.

Zor T, Selinger T. 1996. Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal Biochem 236: 302-308.