Background: Cellulose, the most versatile biomolecule on earth, is available in large quantities from plants. However, cellulose in plants is accompanied by other polymers like hemicellulose, lignin, and pectin. On the other hand, pure cellulose can be produced by some microorganisms, with the most active producer being Acetobacter xylinum. A. senengalensis is a gram-negative, obligate aerobic, motile coccus, isolated from Mango fruits in Senegal, capable of utilizing a variety of sugars and produce cellulose. Besides, the production is also influenced by other culture conditions. Previously, we isolated and identified A. senengalensis MA1, and characterized the bacterial cellulose (BC) produced. Results: The maximum cellulose production by A. senengalensis MA1 was pre-optimized for different parameters like carbon, nitrogen, precursor, polymer additive, pH, temperature, inoculum concentration, and incubation time. Further, the pre-optimized parameters were pooled, and the best combination was analyzed by using Central Composite Design (CCD) of Response Surface Methodology (RSM). Maximum BC production was achieved with glycerol, yeast extract, and PEG 6000 as the best carbon and nitrogen sources, and polymer additive, respectively, at 4.5 pH and an incubation temperature of 33.5 °C. Around 20% of inoculum concentration gave a high yield after 30 days of inoculation. The interactions between culture conditions optimized by CCD included alterations in the composition of the HS medium with 50 mL L^− 1 of glycerol, 7.50 g L^− 1 of yeast extract at pH 6.0 by incubating at a temperature of 33.5 °C along with 7.76 g L^− 1 of PEG 6000. This gave a BC yield of wet weight as 469.83 g L^− 1. Conclusion: The optimized conditions of growth medium resulted in enhanced production of bacterial cellulose by A. senegalensis MA1, which is around 20 times higher than that produced using an unoptimized HS medium. Further, the cellulose produced can be used in food and pharmaceuticals, for producing high-quality paper, wound dressing material, and nanocomposite films for food packaging.

Laccases couple the oxidation of phenolic compounds to the reduction of molecular oxygen and thus span a wide variety of applications. While laccases of eukaryotes and bacteria are well characterized, these enzymes have not been described in archaea. Here, we report the purification and characterization of a laccase (LccA) from the halophilic archaeon Haloferax volcanii . LccA was secreted at high levels into the culture supernatant of a recombinant H. volcanii strain, with peak activity (170 ± 10 mU·ml ^{− 1} ) at stationary phase (72 to 80 h). LccA was purified 13-fold to an overall yield of 72% and a specific activity of 29.4 U·mg ^{− 1} with an absorbance spectrum typical of blue multicopper oxidases. The mature LccA was processed to expose an N-terminal Ala after the removal of 31 amino acid residues and was glycosylated to 6.9% carbohydrate content. Purified LccA oxidized a variety of organic substrates, including bilirubin, syringaldazine (SGZ), 2,2,-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and dimethoxyphenol (DMP), with DMP oxidation requiring the addition of CuSO ₄ . Optimal oxidation of ABTS and SGZ was at 45°C and pH 6 and pH 8.4, respectively. The apparent K _m values for SGZ, bilirubin, and ABTS were 35, 236, and 670 μM, with corresponding k _cat values of 22, 29, and 10 s ^{− 1} , respectively. The purified LccA was tolerant of high salt, mixed organosolvents, and high temperatures, with a half-life of inactivation at 50°C of 31.5 h.

Background: Amylases produced by fungi during solid-state fermentation are the most widely used commercial enzymes to meet the ever-increasing demands of the global enzyme market. The use of low-cost substrates to curtail the production cost and reuse solid wastes are seen as viable options for the commercial production of many enzymes. Applications of α-amylases in food, feed, and industrial sectors have increased over the years. Additionally, the demand for processed and ready-to-eat food has increased because of the rapid growth of food-processing industries in developing economies. These factors significantly contribute to the global enzyme market. It is estimated that by the end of 2024, the global α-amylase market would reach USD 320.1 million (Grand View Research Inc., 2016). We produced α-amylase usingAspergillus oryzaeand low-cost substrates obtained from edible oil cake, such as groundnut oil cake (GOC), coconut oil cake (COC), sesame oil cake (SOC) by solid-state fermentation. We cultivated the fungus using these nutrient-rich substrates to produce the enzyme. The enzyme was extracted, partially purified, and tested for pH and temperature stability. The effect of pH, incubation period and temperature on α-amylase production usingA. oryzaewas optimized. Box–Behnken design (BBD) of response surface methodology (RSM) was used to optimize and determine the effects of all process parameters on α-amylase production. The overall cost economics of α-amylase production using a pilot-scale fermenter was also studied.Results: The substrate optimization for α-amylase production by the Box–Behnken design of RSM showed GOC as the most suitable substrate forA. oryzae, as evident from its maximum α-amylase production of 9868.12 U/gds. Further optimization of process parameters showed that the initial moisture content of 64%, pH of 4.5, incubation period of 108 h, and temperature of 32.5 °C are optimum conditions for α-amylase production. The production increased by 11.4% (10,994.74 U/gds) by up-scaling and using optimized conditions in a pilot-scale fermenter. The partially purified α-amylase exhibited maximum stability at a pH of 6.0 and a temperature of 55 °C. The overall cost economic studies showed that the partially purified α-amylase could be produced at the rate of Rs. 622/L.Conclusions: The process parameters for enhanced α-amylase secretion were analyzed using 3D contour plots by RSM, which showed that contour lines were more oriented toward incubation temperature and pH, having a significant effect (p < 0.05) on the α-amylase activity. The optimized parameters were subsequently employed in a 600 L-pilot-scale fermenter for the α-amylase production. The substrates were rich in nutrients, and supplementation of nutrients was not required. Thus, we have suggested an economically viable process of α-amylase production using a pilot-scale fermenter.

Biotic stresses in plants have a significant impact on agricultural productivity. In the present study, in vivo experiments were conducted to determine the physiological responses of tomato (Solanum lycopersicum L.) seedlings by inoculation with an endophytic actinobacterium, Streptomyces thermocarboxydus isolate BPSAC147 under greenhouse conditions. Further, photochemical quantum yield of photosystem II (PSII) (F_v/F_m), photochemical quenching (qP) and non-photochemical (NPQ) were calculated in seedlings inoculated with S. thermocarboxydus (T1) and were compared with control (T0) plants. Furthermore, the electron transport rate (ETR) of PSII exhibited a significant increase in T1 plants, relative to T0 plants. These results indicate that inoculation of tomato seedlings with S. thermocarboxydus had a positive effect on the process of photosynthesis, resulting in enhanced chlorophyll fluorescence parameters due to increased ETR in the thylakoid membrane. GC-MS analysis showed significant differences in the volatile compounds in the different treatments performed under greenhouse conditions. The present study suggests that S. thermocarboxydus can be used as new biocontrol agent to control Fusarium wilt in tomato crops and enhance productivity by enhancing photosynthesis.