ISSN: 0973-7510

E-ISSN: 2581-690X

Research Article | Open Access
Prachi R. Gandhi
Department of Microbiology and Biotechnology Centre, Faculty of Science, The Maharaja Sayajirao University of Baroda, Vadodara – 390 002, Gujarat, India.
J Pure Appl Microbiol. 2021;15(4):2003-2018 | Article Number: 7118
https://doi.org/10.22207/JPAM.15.4.22 | © The Author(s). 2021
Received: 19/06/2021 | Accepted: 16/09/2021 | Published: 11/10/2021
Abstract

Pigeon peas are an excellent source of carbohydrates, proteins and other nutrients. Many traditional fermented foods are prepared from cereals and combinations of cereals and pulses that usually contain Lactic acid bacteria (LAB), Bacillus, Enterococcus and yeast. Lactobacillus can be used as a starter culture for such fermentation using pulses, as very few reports are available on fermented pulse-based products. Hence, pulse dal flour was used as a source for isolation of Lactobacillus to maintain their functionality, growth characteristics and activity during food processing. In this study, we investigated the potential of lactobacilli from fermented pigeon pea to utilize carbohydrates, the ability to degrade non-digestible oligosaccharides and the production of the α-galactosidase enzyme. Lactobacillus isolated from six different pulse dal flour grew well during fermentation with carbohydrates in mMRS medium. Among Lactobacillus species, only Lactobacillus brevis displayed the highest α-galactosidase activity (1.24 U/ml), where raffinose was added as the sole carbohydrate source in the medium. The isolate was further tested in pigeon pea fermentation, where it showed maximum activity (1.86 U/ml) and complete hydrolysis of non-digestible oligosaccharides was observed. Overall, usage of Lactobacilli could be an excellent opportunity to design and develop a novel pulse-based fermented product contributing to beneficial bioactive compounds and improving the properties of food.

Keywords

Cajanus cajan, Lactobacillus, Fermentation, Carbohydrate utilization, Non-digestible oligosaccharides, α-galactosidase (α-gal) activity

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