Thermostability of Probiotics and Their α -Galactosidases and the Potential for Bean Products.

Biotechnology Research International Pub Date : 2014-01-01 Epub Date: 2014-02-18 DOI:10.1155/2014/472723
Xiaoli Liu, Claude P Champagne, Byong H Lee, Joyce I Boye, Michel Casgrain
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引用次数: 24

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.

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益生菌及其α -半乳糖苷酶的热稳定性及其在豆制品中的应用潜力。
大豆和其他豆类含有低聚糖,可能引起肠道紊乱,如肠胃胀气。本研究旨在研究在冷冻食品中添加产生α -半乳糖苷酶的益生菌,使其能够在解冻和食用豆类的加热处理中存活下来。短双歧杆菌S46的α -半乳糖苷酶活性最高,为1.26 U/mg蛋白。在不同菌株中,干酪乳杆菌的α -半乳糖苷酶热稳定性最高,在50°C、55°C和60°C条件下,D值分别为35、29和9.3 min。与活细胞相比,加热对酶活性的影响较小。然而,这两种细菌酶的D值低于三种含α -半乳糖苷酶的商业产品。新鲜培养的细胞及其酶比复水培养的细胞及其酶更稳定。实际的应用程序。可以在食物中添加酶和培养物,以提高胃肠道对碳水化合物的消化率。然而,由于许多食物都是加热的,因此对酶的热稳定性进行评估是很重要的。本文提供了α -半乳糖苷酶的稳定性数据,该酶可能被添加到含有水苏糖或棉子糖的食物基质中,如豆类。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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