title: Thermostability of Probiotics and Their α -Galactosidases and the Potential for Bean Products.
abstract: Soybeans and other pulses contain oligosaccharides which may cause intestinal disturbances such as flatulence. This study was undertaken to investigate α -galactosidase-producing probiotics added to frozen foods which can survive warming treatments used in thawing and consumption of the pulses. The maximum α -galactosidase activity (1.26 U/mg protein) was found in Bifidobacterium breve S46. Lactobacillus casei had the highest α -galactosidase thermostability among the various strains, with D values of 35, 29, and 9.3 minutes at 50°C, 55°C, and 60°C, respectively. The enzyme activity was less affected than viable cells by heating. However, the D values of two bacterial enzymes were lower than those of three commercial α -galactosidase-containing products. Freshly grown cells and their enzymes were more stable than the rehydrated cultures and their enzymes. Practical Application. Enzymes and cultures can be added to foods in order to enhance the digestibility of carbohydrates in the gastrointestinal tract. However since many foods are warmed, it is important that the thermostability of the enzymes be assessed. This paper provides data on the stability of α -galactosidase, which could potentially be added to food matrices containing stachyose or raffinose, such as beans.
authors.affiliation: Institute of Agro-Product Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China.
authors.forename: Xiaoli
authors.initials: X
authors.lastname: Liu
authors.affiliation: Agriculture and Agri-Food Canada, Food Research and Development Centre, 3600 Casavant O. Saint-Hyacinthe, QC, Canada J2S 8E3.
authors.forename: Claude P
authors.initials: CP
authors.lastname: Champagne
authors.affiliation: Agriculture and Agri-Food Canada, Food Research and Development Centre, 3600 Casavant O. Saint-Hyacinthe, QC, Canada J2S 8E3 ; School of Biotechnology, Jiangnan University, Wuxi 214122, China.
authors.forename: Byong H
authors.initials: BH
authors.lastname: Lee
authors.affiliation: Agriculture and Agri-Food Canada, Food Research and Development Centre, 3600 Casavant O. Saint-Hyacinthe, QC, Canada J2S 8E3.
authors.forename: Joyce I
authors.initials: JI
authors.lastname: Boye
authors.affiliation: Bonduelle North America, 540, Chemin des Patriotes, Saint-Denis-sur-Richelieu, QC, Canada J0H 1K0.
authors.forename: Michel
authors.initials: M
authors.lastname: Casgrain
references.citation: BMC Microbiol. 2008 Jan 29;8:22
references.pmid: 18230145
references.citation: Am J Gastroenterol. 2000 May;95(5):1231-8
references.pmid: 10811333
references.citation: Int J Food Microbiol. 2011 Oct 3;149(3):185-93
references.pmid: 21803436
references.citation: Int J Food Microbiol. 2005 Jul 15;102(2):221-30
references.pmid: 15992621
references.citation: J Food Sci. 2009 May-Jul;74(4):E191-8
references.pmid: 19490324
references.citation: Appl Environ Microbiol. 2010 May;76(9):2747-53
references.pmid: 20305033
references.citation: Curr Pharm Des. 2009;15(13):1403-14
references.pmid: 19442165
references.citation: Appl Microbiol Biotechnol. 2009 Oct;84(6):1137-47
references.pmid: 19529931
references.citation: Enzyme Microb Technol. 1998 Apr;22(5):383-90
references.pmid: 9549105
references.citation: J Biotechnol. 2007 Jan 30;128(1):61-71
references.pmid: 17049401
references.citation: J Appl Microbiol. 2007 Oct;103(4):1170-83
references.pmid: 17897222
references.citation: Proteomics. 2004 Jan;4(1):106-22
references.pmid: 14730676
references.citation: Curr Microbiol. 2006 Nov;53(5):374-8
references.pmid: 17048069
references.citation: Curr Pharm Des. 2008;14(14):1382-99
references.pmid: 18537661