Stain removing, juice-clarifying, and starch-liquefying potentials of amylase from Pleurotus tuberregium in submerged fermentation system

Abstract

Background Amylase is used commercially in food, textiles, sugar syrup, paper, and detergent industries. Bacteria and fungi remain a significant source of industrial enzymes. Pleurotus tuberregium is a macro-fungi that can exist as a fruiting body, sclerotium, mycelium, and spores. Some studies have been conducted on this fungus, with minimal studies on its enzyme activity (s) using the submerged fermentation technique. Results The purified amylase has a specific activity of 5.26 U/mg, total activity of 189.20 U, maximally active at 70 °C, pH of 5, and retaining 100% of its activity at 30 oC for 4 min. P. tuberregium amylase showed optimal activity with plantain peel, followed by starch and pineapple peel (42, 30, and 29 μg/mL/min respectively). The presence of Ca2+, Mg2+, and Na+ ions in the reaction mixture activated the enzyme activity, but was slightly and moderately inhibited by KCl and Na2H2PO4 respectively. The crude enzyme effectively clarified juice, liquefied soluble cassava starch (with a release of appreciable glucose quantity), and partially de-stained white fabric. Conclusions The amylase obtained from the submerged fermentation of Pleurotus tuberregium has potential applications in food and detergent industries.

Purification and characterization of moderately thermostable raw-starch digesting α-amylase from endophytic <i>Streptomyces mobaraensis </i>DB13<i> </i>associated with <i>Costus speciosus</i>

“…Another study showed that 7.9-fold purification with a 53.33% enzyme yield from B. cereus GA6 (Roohi et al, 2013). The variations in microbial strains and purification techniques may be responsible for variations in amylase percentage yields (Bamigboye et al, 2022). The molecular weight of the purified enzyme was found to be 55 kDa based on SDS-PAGE as well as zymographic analysis which is concomitant with that of B. cereus GA6, and Bacillus sp.…”

“…The pH stability is also an important factor for industrial applications. Amylase that would retain its activity at a specific pH would be a viable candidate for such uses (Bamigboye et al, 2022). The stability of the α-amylase enzyme from S. mobaraensis DB13 at pH 6.0, 7.0 and 8.0 after 90-120 min of incubation at 50°C suggests that the enzyme could be suitable for industrial application.…”

Effects of two kinds of Bacillus on flavour formation of Baijiu solid‐state fermentation with pure mixed bacteria

“…Liquefaction enzymes (deactivation temperature about 100 °C) were not completely inactivated when the temperature increased, but the glucoamylase (the optimum temperature is 35 °C) that decomposed polysaccharides into oligosaccharides and monosaccharides was easily inactivated at high temperatures International Journal of Food Science and Technology 2023 (Fig. 3b; Bamigboye et al, 2022). This showed that when the temperature of the fermentation system was close to the maximum temperature, the accumulated polysaccharides in the fermentation system were difficult to decompose; yet, the microbial metabolism continued, and instead, the small molecular sugars accumulated in the system were consumed, reducing their content.…”

“…LWT-Food Science and Technology, 130, 109620. Li, W., Fan, G., Fu, Z. et al (2020) Bacillus licheniformis affects the microbial community and metabolic profile in the spontaneous fermentation of Daqu starter for Chinese liquor making. International Journal of Food Microbiology, 250, 59-67.…”

“…Saccharomyces cerevisiae generated high ethanol production, and Aspergillus niger, as an important fungal strain in the production of Maotai-flavoured Baijiu, produced excellent liquefaction and saccharification (Adeyemo et al, 2021;. Actinomycetes, as the most popular Baijiu microorganism, were of great significance to the formation of Baijiu flavour (Fan et al, 2020). The unique nut and sauce flavours produced by actinomycetes were of great benefit to the formation of Baijiu flavour (Zhao et al, 2021).…”