
Optimization of High-Protein Glutinous Rice Flour Production Using Response Surface Method
Received date: 2018-08-27
Accepted date: 2018-12-09
Online published: 2019-09-30
A response surface method was employed to study the effect of α-amylase concentration, hydrolysis temperature and time on the production of high protein glutinous rice flour (HPGRF). The suspension of glutinous rice flour (15%) that contained 6.52% protein was gelatinized and subsequently hydrolyzed by thermostable α-amylase. The hydrolysis yielded 0.144-0.222 g/g HPGRF with 29.4%-45.4% protein content. Hydrolysis time exerted a significant effect, while enzyme concentration and hydrolysis temperature showed insignificant effect on the protein content and production yield of HPGRF. The result of response surface method showed that the optimum condition for the production of HPGRF that contained at least 36% protein was treating gelatinized 15% glutinous rice flour suspension with 0.90 Kilo Novo α-amylase Unit (KNU)/g α-amylase at 80 ºC for 99 min. By carrying out the predicted hydrolysis condition, HPGRF with 35.9% protein and 61.8% carbohydrates was resulted. The process yielded 0.172 g/g HPGRF. HPGRF contained higher amount of essential amino acids compared to glutinous rice flour. HPGRF had higher solubility and lower swelling power, and also showed no pasting peak compared with glutinous rice flour.
Key words: high protein flour; glutinous rice; α-amylase; amino acid; response surface method
Eakkanaluksamee Kanjanapa, Anuntagool Jirarat . Optimization of High-Protein Glutinous Rice Flour Production Using Response Surface Method[J]. Rice Science, 2020 , 27(1) : 75 -80 . DOI: 10.1016/j.rsci.2019.12.008
| [1] | Alvarez A M, Adachi T, Nakase M, Aoki N, Nakamura R, Matsuda T.1995. Classification of rice allergenic protein cDNAs belonging to the α-amylase/trypsin inhibitor gene family.Biochim Biophy Acta (BBA): Protein Struct Mol Enzymol, 1251(2): 201-204. |
| [2] | AOAC (Association of Official Analytical Chemists). 1995. Official Methods of Analysis. 17th edn. Washington D C, USA: AOAC. |
| [3] | Asero R, Amato S, Alfieri B, Folloni S, Mistrello G.2007. Rice: Another potential cause of food allergy in patients sensitized to lipid transfer protein.Int Arch Allerg Immunol, 143(1): 69-74. |
| [4] | Besler M, Tanabe S, Urisu A.2001. Allergen Data Collection-Update: Rice (Oryza sativa). Internet Sympos Food Allerg, 3: 1-17. |
| [5] | Chang K C, Lee C C, Brown G.1986. Production and nutritional evaluation of high-protein rice flour.J Food Sci, 51(2): 464-467. |
| [6] | Enrique E, Ahrazem O, Bartra J, Latorre M D, Castello J V, de Mateo J A, Montoya E, Malek T, Barber D, Salcedo G.2005. Lipid transfer protein is involved in rhinoconjunctivitis and asthma produced by rice inhalation.J Aller Clin Immun, 116(4): 926-928. |
| [7] | Ferreira S L C, Bruns R E, Ferreira H S, Matos G D, David J M, Brandão G C, da Silva E FG P, Portugal L A, dos Reis P S, Souza A S, dos Santos W N L.2007. Box-Behnken design: An alternative for the optimization of analytical methods.Anal Chim Acta, 597(2): 179-186. |
| [8] | Gomes I, Gomes J, Steiner W.2003. Highly thermostable amylase and pullulanase of the extreme thermophilic eubacteriumRhodothermus marinus: Production and partial characterization. Biores Technol, 90(2): 207-214. |
| [9] | Hoogenkamp H, Kumagai H, Wanasundara J P D. 2017. Rice protein and rice protein products. In: Nadathur S R, Wanasundara J P D, Scanlin L. Sustainable Protein Sources. San Diego, USA: Academic Press: 47-65. |
| [10] | Izumi H, Sugiyama M, Matsuda T, Nakamura R.1999. Structural characterization of the 16-kDa allergen, RA17, in rice seeds: Prediction of the secondary structure and identification of intramolecular disulfide bridges.Biosci Biotechnol Biochem, 63(12): 2059-2063. |
| [11] | Ji Y, Zhu K X, Qian H F, Zhou H M.2007. Staling of cake prepared from rice flour and sticky rice flour.Food Chem, 104(1): 53-58. |
| [12] | Ju Z Y, Hettiarachchy N S, Rath N.2001. Extraction, denaturation and hydrophobic properties of rice flour proteins.J Food Sci, 66(2): 229-232. |
| [13] | Kato T, Katayama E, Matsubara S, Omi Y, Matsuda T.2000. Release of allergenic proteins from rice grains induced by high hydrostatic pressure.J Agric Food Chem, 48(8): 3124-3129. |
| [14] | Krishna P N.2011. Enzymes: An overview. In: Krishna P N. Enzyme Technology: Pacemaker of Biotechnology. PHI Learning Pvt. Ltd: 1-67. |
| [15] | Li Y, Zhang H E, Shoemaker C F, Xu Z T, Zhu S, Zhong F.2013. Effect of dry heat treatment with xanthan on waxy rice starch.Carbohyd Polymer, 92(2): 1647-1652. |
| [16] | Nakamura R, Matsuda T.1996. Rice allergenic protein and molecular- genetic approach for hypoallergenic rice.Biosci Biotechnol Biochem, 60(8): 1215-1221. |
| [17] | Nakase M, Usui Y, Alvarez-Nakase A M, Adachi T, Urisu A, Nakarnura R, Aoki N, Kitajima K, Matsuda T.1998. Cereal allergens: Rice-seed allergens with structural similarity to wheat and barley allergens.Allergy, 53: 55-57. |
| [18] | Keawsompong S, Laohapattanalert K, Piyachomkwan K, Chotineeranat S, Sriroth K.2004. Utilization of broken rice for glucose syrup and high protein rice flour production. In: Starch 2004: Structure and Functionality. Cambridge, UK: The Royal Society of Chemistry. |
| [19] | Poznanski J, Sodano P, Suh S W, Lee J Y, Ptak M, Vovelle F.1999. Solution structure of a lipid transfer protein extracted from rice seeds: Comparison with homologous proteins.Eur J Biochem, 259(3): 692-708. |
| [20] | Qin Y, Liu C Z, Jiang S S, Cao J M, Xiong L, Sun Q J.2016. Functional properties of glutinous rice flour by dry-heat treatment.PLoS One, 11(8): e0160371. |
| [21] | Reche M, Pascual C, Fiandor A, Polanco I, Rivero-Urgell M, Chifre R, Johnston S, Martín-Esteban M.2010. The effect of a partially hydrolysed formula based on rice protein in the treatment of infants with cow’s milk protein allergy.Pediatr Aller Immunol, 21: 577-585. |
| [22] | Schoch T J.1964. Welling power and solubility of granular starches. In: Whistler R L, Smith R J, BeMiller J N. Method in Carbohydrates Chemistry. New York: Acedemic Press: 106-108. |
| [23] | Shaw J F, Sheu J R.1992. Production of high-maltose syrup and high- protein flour from rice by an enzymatic method.Biosci Biotechnol Biochem, 56(7): 1071-1073. |
| [24] | Shih F F.2003. An update on the processing of high-protein rice products.Nahrung, 47(6): 420-424. |
| [25] | Shih F F, Champagne E T, Daigle K, Zarins Z.1999. Use of enzymes in the processing of protein products from rice bran and rice flour.Food Nahrung, 43(1): 14-18. |
| [26] | Usui Y, Nakase M, Hotta H, Urisu A, Aoki N, Kitajima K, Matsuda T.2001. A 33-kDa allergen from rice (Oryza sativa L. japonica): cDNA cloning, expression, and identification as a novel glyoxalase I. J Biol Chem, 276(14): 11376-11381. |
| [27] | van der Maarel M J E C, van der Veen B, Uitdehaag J C M, Leemhuis H, Dijkhuizen L.2002. Properties and applications of starch-converting enzymes of the α-amylase family.J Biotechnol, 94(2): 137-155. |
| [28] | van Ree R, Voitenko V, van Leeuwen W A, Aalberse R C.1992. Profilin is a cross-reactive allergen in pollen and vegetable foods.Int Arch Allerg Immunol, 98(2): 97-104. |
| [29] | Yamada C, Yamashita Y, Seki R, Izumi H, Matsuda T, Kato Y.2006. Digestion and gastrointestinal absorption of the 14-16-kDa rice allergens.Biosci Biotechnol Biochem, 70(8): 1890-1897. |
| [30] | Zhu L J, Liu Q Q, Sang Y J, Gu M H, Shi Y C.2010. Underlying reasons for waxy rice flours having different pasting properties.Food Chem, 120(1): 94-100. |
/
| 〈 |
|
〉 |