Preparation of α-Amylase Inhibitor from Seeds of White Kidney Bean Using a Novel and Scalable Process Based on Enzymatic Hydrolysis
International Journal of Nutrition and Food Sciences
Volume 8, Issue 3, May 2019, Pages: 52-58
Received: Jul. 13, 2019;
Accepted: Aug. 13, 2019;
Published: Sep. 6, 2019
Views 95 Downloads 27
Yifeng Rang, Department of Research and Development, New Industry Health Technology (Zhuhai) Co., Ltd., Zhuhai, China
Wei Zhao, School of Food Science and Technology, Jiangnan University, Wuxi, China
This study proposed and evaluated a novel and scalable process based on enzymatic hydrolysis for the preparation of α-amylase inhibitor (α-AI) in seeds of white kidney bean (Phaseolus vulgaris). The process mainly involved heat treatment (70°C/30 min), enzymatic hydrolysis, isoelectric precipitation and 70% ethanol precipitation. The optimal preparation parameters for enzymatic hydrolysis and isoelectric precipitation were as follows: Flavourzyme 500MG was used for enzymatic hydrolysis and the ultimate hydrolysate was obtained at 180 min, followed by isoelectric precipitation at pH 3.6. The loss of miscellaneous proteins and purification fold in the novel process were relatively low (85.84% and 4.74, respectively), while the α-AI activity yield (67.12%) was much higher than the values obtained by chromatography. Combined with the SDS-PAGE analysis, enzymatic hydrolysis proved to have modified the pI and alcohol-solubility of the miscellaneous proteins, which has a favorable influence on isoelectric precipitation and ethanol precipitation for the preparation of the α-AI.
Preparation of α-Amylase Inhibitor from Seeds of White Kidney Bean Using a Novel and Scalable Process Based on Enzymatic Hydrolysis, International Journal of Nutrition and Food Sciences. Special Issue: Natural Active Ingredients for the Management of Diabetes and Obesity.
Vol. 8, No. 3,
2019, pp. 52-58.
Broughton WJ, Hernandez G, Blair M, et al. 2003. Beans (Phaseolus spp.) – model food legumes. Plant Soil, 252, 55–128.
Du SK, Jiang H, Ai Y, et al. 2014. Physicochemical properties and digestibility of common bean (Phaseolus vulgaris L.) starches. Carbohydrate Polymers, 108, 200-205.
Bowman DE. 1945. Amylase inhibitor of navy beans. Science, 102, 358-359.
Obiro WC, Zhang T & Jiang B. 2008. The nutraceutical role of the Phaseolus vulgaris α-amylase inhibitor. British Journal of Nutrition, 100, 1–12.
Wu CT, Chiu CY, Huang CF, et al. 2018. Genotoxicity and 28-day oral toxicity studies of a functional food mixture containing maltodextrin, white kidney bean extract, mulberry leaf extract, and niacin-bound chromium complex. Regul Toxicol Pharmacol, 92, 67-74.
Kusaba NM, Ki M, Iwamoto M, et al. 2000. CM3, one of the wheat α-amylase inhibitor subunits, and binding of IgE in Sera from Japanese with atopic dermatitis related to wheat. Food and chemical toxicology, 38, 179–185.
Ho MF & Whitaker JR. 2010. Subunit structures and essential amino acid residues of white kidney bean (Phaseolus vulgaris) alpha-amylase inhibitors. Journal of Food Biochemistry, 17 (1), 35-52.
Chen XP & Yang WY. 2014. Epidemic trend of diabetes in China. Journal of Diabetes Investigation, 5, 478-481.
Mokdad AH, Bowman BA, Ford ES, et al. 2001. The continuing epidemics of obesity and diabetes in the United States. Jama, 286, 1195-1200.
None. 2016. Fabenol? max, a standardised aqueous extract from phaseolus vulgaris l. and ‘reduces the absorption of carbohydrates’: evaluation of a health claim pursuant to article 13 (5) of regulation (ec) no 1924/2006. EFSA Journal, 14 (2).
Skop M & Chokshi D. 2006. Purified amylase inhibitor and novel process for obtaining the same. http://www.freepatentsonline.com/20060147565.html (accessed 10 April 2007).
Wang H, Chen C, Jeng T, et al. 2011. Comparisons of α-amylase inhibitors from seeds of common bean mutants extracted through three phase partitioning. Food Chemistry, 128, 1066–1071.
Gupta M, Sharma P & Nath AK. 2014. Purification of a novel α-amylase inhibitor from local himalayan bean (Phaseolus vulgaris) seeds with activity towards bruchid pests and human salivary amylase. Journal of food science and technology, 51, 1286–1293.
Marshall JJ & Lauda CM. 1975. Purification and properties of phaseolamin, an inhibitor of α-amylase, from the kidney bean, Phaseolus vulgaris. Journal of Biological Chemistry, 250, 8030–8037.
Kumar S, Verma AK, Das M, et al. 2013. Clinical complications of kidney bean (Phaseolus vulgaris L.) consumption. Nutrition, 29, 821-827.
Golparvar Z & Naseri B. 2016. Comparative reproductive performance and digestive enzymatic activity of helicoverpa armigera (noctuidae) on seven bean cultivars. Journal of the Lepidopterists Society, 70 (2), 121-129.
Yanli M, Yifeng R, Ruijin Y, et al. 2018. Effect of white kidney bean extracts on estimated glycemic index of different kinds of porridge. LWT, 96, 576-582.
Nciri N & Cho N. 2018. New research highlights: impact of chronic ingestion of white kidney beans (Phaseolus vulgarisl. var. beldia) on small-intestinal disaccharidase activity in wistar rats. Toxicology Reports, 5, 46-55.
Betancur AD, Gallegos TS & Chel GL. 2004. Wet-fractionation of Phaseolus lunatus seeds: partial characterization of starch and protein. Journal of the Science of Food and Agriculture, 84, 1193–1201.
Singh N, Kaur M, Sandhu KS, et al. 2004. Physicochemical, thermal, morphological and pasting properties of starches from some Indian black gram (Phaseolus mungo L.) cultivars. Starch-Stärke, 56, 535-544.
Yang M, Zhang X, Ma Y, et al. 2008. Purification and partial characterization of a glycoprotein alpha-amylase inhibitor from white kidney bean (Phaseolus vulgaris L.). Journal of Food Biochemistry, 32, 72–84.
Betancur AD, Sosa ET, Ruiz RJ, et al. 2014. Enzymatic hydrolysis of hard-to-cook bean (Phaseolus vulgaris L.) protein concentrates and its effects on biological and functional properties. International Journal of Food Science & Technology, 49, 2–8.
Adler NJ. 1979. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. Journal of Agricultural and Food Chemistry, 27, 1256-1262.
Lowry OH, Rosebrough NJ, Farr AL, et al. 1951. Protein measurement with the Folin phenol reagent. J biol Chem, 193, 265–275.
Maria HCC, Arcy LA, Roy MH, et al. 2001. Aspartic protease in leaves of common bean (Phaseolus vulgaris L.) and cowpea (Vigna unguiculata L. Walp): enzymatic activity, gene expression and relation to drought susceptibility. FEBS Letters, 492, 242-246.
Zhao W, Yang R, Tang Y, et al. 2009. Investigation of the protein–protein aggregation of egg white proteins under pulsed electric fields. Journal of agricultural and food chemistry, 57, 3571–3577.
Mahomoodally MF & Ramalingum N. 2015. An investigation into the consumption patterns, attitude, and perception of mauritians towards common medicinal food plants. Journal of Herbal Medicine, 5 (2), 99-112.
Yu Z, Yin Y, Zhao W, et al. 2011. Novel peptides derived from egg white protein inhibiting alpha-glucosidase. Food Chemistry, 129, 1376–1382.
Jay U, Ollie T & Jhanna M. 2018. Systematic review and meta-analysis of a proprietary alpha-amylase inhibitor from white bean (phaseolus vulgaris l.) on weight and fat loss in humans. Foods, 7 (4), 63-72.
Bellincampi D, Camardella L, Delcour JA, et al. 2004. Potential physiological role of plant glycosidase inhibitors. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1696, 265–274.