Carbohydrate-Active Enzymes of a Novel Halotolerant
            <i>Alkalihalobacillus</i>
            Species for Hydrolysis of Starch and Other Algal Polysaccharides

Masasa, Matan; Kushmaro, Ariel; Chernova, Helena; Shashar, Nadav; Guttman, Louis

doi:10.1128/spectrum.01078-22

Cited by 5 publications

(3 citation statements)

References 48 publications

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“…Alpha-amylase and α-glucosidase are essential enzymes involved in the hydrolysis of starch into disaccharides and their subsequent conversion into glucose ( Masasa et al, 2022 ). The inhibition of α-amylase is an important strategy in the management of diabetes ( Koh et al, 2010 ).…”

Section: Resultsmentioning

confidence: 99%

Multi-Strain Probiotics Enhance the Bioactivity of Cascara Kombucha during Microbial Composition-Controlled Fermentation

Van,

Phan,

Quang

et al. 2023

Prev. Nutr. Food Sci.

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Kombucha is a widely consumed fermented tea beverage with diverse health benefits. In a previous study, we demonstrated that the use of cascara as a substrate results in a special kombucha beverage with high bioactivity. Traditional kombucha fermentation using a symbiotic culture of bacteria and yeast (SCOBY) can lead to inconsistent product quality because of the lack of control over microbial composition. We successfully isolated and identified yeast and bacteria, including Saccharomyces cerevisiae, Komagataeibacter rhaeticus, and Lactobacillus brevis that are appropriate starter cultures for cascara kombucha fermentation. We also demonstrated that a supplementation with lactic acid bacteria (LAB) and a mixture of S. cerevisiae and K. rhaeticus resulted in higher total polyphenol and flavonoid content of cascara kombucha compared with the traditionally fermented product using SCOBY as the inoculum. The free radical scavenging activity, inhibitory effects on -amylase, tyrosinase activity, and antibacterial properties of cascara kombucha were also enhanced as a result of LAB supplement. These findings provide valuable insights into the controlled microbiological composition required for the fermentation of cascara kombucha, thereby ensuring consistent quality and enhanced bioactivity of the product. Further, the use of cascara as a substrate for kombucha production not only offers various health benefits and biological effects, but also repurposes by-products from the coffee industry, which contributes to sustainable development and is eco-friendly.

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Section: Resultsmentioning

confidence: 99%

Multi-Strain Probiotics Enhance the Bioactivity of Cascara Kombucha during Microbial Composition-Controlled Fermentation

Van,

Phan,

Quang

et al. 2023

Prev. Nutr. Food Sci.

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“…Halotolerant α-amylases have received considerably less consideration. However, most are thermostable and generate oligosaccharides in low-water or nonaqueous solvents, where hydrolytic processes are blocked ( Masasa et al, 2022 ). This study’s amylases had optimum activity in the alkalinity range and at high temperatures.…”

Section: Discussionmentioning

confidence: 99%

Discovery of novel carbohydrate degrading enzymes from soda lakes through functional metagenomics

et al. 2022

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Extremophiles provide a one-of-a-kind source of enzymes with properties that allow them to endure the rigorous industrial conversion of lignocellulose biomass into fermentable sugars. However, the fact that most of these organisms fail to grow under typical culture conditions limits the accessibility to these enzymes. In this study, we employed a functional metagenomics approach to identify carbohydrate-degrading enzymes from Ethiopian soda lakes, which are extreme environments harboring a high microbial diversity. Out of 21,000 clones screened for the five carbohydrate hydrolyzing enzymes, 408 clones were found positive. Cellulase and amylase, gave high hit ratio of 1:75 and 1:280, respectively. A total of 378 genes involved in the degradation of complex carbohydrates were identified by combining high-throughput sequencing of 22 selected clones and bioinformatics analysis using a customized workflow. Around 41% of the annotated genes belonged to the Glycoside Hydrolases (GH). Multiple GHs were identified, indicating the potential to discover novel CAZymes useful for the enzymatic degradation of lignocellulose biomass from the Ethiopian soda Lakes. More than 73% of the annotated GH genes were linked to bacterial origins, with Halomonas as the most likely source. Biochemical characterization of the three enzymes from the selected clones (amylase, cellulase, and pectinase) showed that they are active in elevated temperatures, high pH, and high salt concentrations. These properties strongly indicate that the evaluated enzymes have the potential to be used for applications in various industrial processes, particularly in biorefinery for lignocellulose biomass conversion.

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“…Amylases are important degradative hydrolases involved in starch metabolism [12], although surprisingly little is known about their characteristics and production in A. apis. Amylases are also used in a variety of biotechnological applications, including starch saccharification, textile production and treatments, food, baking, brewing, pharmaceutics, detergents, and distillation industries [13][14][15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Characterization of an α-Amylase from the Honeybee Chalk Brood Pathogen Ascosphaera apis

Li,

Liu,

Yang

et al. 2023

JoF

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The insect pathogenic fungus, Ascosphaera apis, is the causative agent of honeybee chalk brood disease. Amylases are secreted by many plant pathogenic fungi to access host nutrients through the metabolism of starch, and the identification of new amylases can have important biotechnological applications. Production of amylase by A. apis in submerged culture was optimized using the response surface method (RSM). Media composition was modeled using Box–Behnken design (BBD) at three levels of three variables, and the model was experimentally validated to predict amylase activity (R2 = 0.9528). Amylase activity was highest (45.28 ± 1.16 U/mL, mean ± SE) in media composed of 46 g/L maltose and1.51 g/L CaCl2 at a pH of 6.6, where total activity was ~11-fold greater as compared to standard basal media. The enzyme was purified to homogeneity with a 2.5% yield and 14-fold purification. The purified enzyme had a molecular weight of 75 kDa and was thermostable and active in a broad pH range (> 80% activity at a pH range of 7–10), with optimal activity at 55 °C and pH = 7.5. Kinetic analyses revealed a Km of 6.22 mmol/L and a Vmax of 4.21 μmol/mL·min using soluble starch as the substrate. Activity was significantly stimulated by Fe2+ and completely inhibited by Cu2+, Mn2+, and Ba2+ (10 mM). Ethanol and chloroform (10% v/v) also caused significant levels of inhibition. The purified amylase essentially exhibited activity only on hydrolyzed soluble starch, producing mainly glucose and maltose, indicating that it is an endo-amylase (α-amylase). Amylase activity peaked at 99.38 U/mL fermented in a 3.7 L-bioreactor (2.15-fold greater than what was observed in flask cultures). These data provide a strategy for optimizing the production of enzymes from fungi and provide insight into the α-amylase of A. apis.

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Carbohydrate-Active Enzymes of a Novel Halotolerant Alkalihalobacillus Species for Hydrolysis of Starch and Other Algal Polysaccharides

Cited by 5 publications

References 48 publications

Multi-Strain Probiotics Enhance the Bioactivity of Cascara Kombucha during Microbial Composition-Controlled Fermentation

Multi-Strain Probiotics Enhance the Bioactivity of Cascara Kombucha during Microbial Composition-Controlled Fermentation

Discovery of novel carbohydrate degrading enzymes from soda lakes through functional metagenomics

Characterization of an α-Amylase from the Honeybee Chalk Brood Pathogen Ascosphaera apis

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