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521 result(s) for "Xiao-Yan, Song"
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Nitrogen Starvation Impacts the Photosynthetic Performance of Porphyridium cruentum as Revealed by Chlorophyll a Fluorescence
Nitrogen is one of the most important nutrients needed for plants and algae to survive, and the photosynthetic ability of algae is related to nitrogen abundance. Red algae are unique photosynthetic eukaryotic organisms in the evolution of algae, as they contain phycobilisomes (PBSs) on their thylakoid membranes. In this report, the in vivo chlorophyll (Chl) a fluorescence kinetics of nitrogen-starved Porphyridium cruentum were analyzed to determine the effects of nitrogen deficiency on photosynthetic performance using a multi-color pulse amplitude modulation (PAM) chlorophyll fluorometer. Due to nitrogen starvation, the photochemical efficiency of PSII and the activity of PSII reaction centers (RCs) decreased, and photoinhibition of PSII occurred. The water-splitting system on the donor side of PSII was seriously impacted by nitrogen deficiency, leading to the inactivation of the oxygen-evolving complex (OEC) and decreased light energy conversion efficiency. In nitrogen-starved cells, a higher proportion of energy was used for photochemical reactions, and thermal dissipation was reduced, as shown by qP and qN. The ability of nitrogen-starved cells to tolerate and resist high photon flux densities was weakened. Our results showed that the photosynthetic performance of P. cruentum was severely impacted by nitrogen deficiency.
A pathway for chitin oxidation in marine bacteria
Oxidative degradation of chitin, initiated by lytic polysaccharide monooxygenases (LPMOs), contributes to microbial bioconversion of crystalline chitin, the second most abundant biopolymer in nature. However, our knowledge of oxidative chitin utilization pathways, beyond LPMOs, is very limited. Here, we describe a complete pathway for oxidative chitin degradation and its regulation in a marine bacterium, Pseudoalteromonas prydzensis . The pathway starts with LPMO-mediated extracellular breakdown of chitin into C1-oxidized chitooligosaccharides, which carry a terminal 2-(acetylamino)−2-deoxy-D-gluconic acid (GlcNAc1A). Transmembrane transport of oxidized chitooligosaccharides is followed by their hydrolysis in the periplasm, releasing GlcNAc1A, which is catabolized in the cytoplasm. This pathway differs from the known hydrolytic chitin utilization pathway in enzymes, transporters and regulators. In particular, GlcNAc1A is converted to 2-keto-3-deoxygluconate 6-phosphate, acetate and NH 3 via a series of reactions resembling the degradation of D-amino acids rather than other monosaccharides. Furthermore, genomic and metagenomic analyses suggest that the chitin oxidative utilization pathway may be prevalent in marine Gammaproteobacteria. Lytic polysaccharide monooxygenases contribute to microbial degradation of chitin, but how the resulting oxidized chitooligosaccharides are utilized by microbes is unclear. Here, the authors describe a complete pathway for oxidative chitin utilization in marine bacteria.
Promotion of Wound Healing and Prevention of Frostbite Injury in Rat Skin by Exopolysaccharide from the Arctic Marine Bacterium Polaribacter sp. SM1127
Many marine microorganisms synthesize exopolysaccharides (EPSs), and some of these EPSs have been reported to have potential in different fields. However, the pharmaceutical potentials of marine EPSs are rarely reported. The EPS secreted by the Artic marine bacterium Polaribacter sp. SM1127 has good antioxidant activity, outstanding moisture-retention ability, and considerable protective property on human dermal fibroblasts (HDFs) at low temperature. Here, the effects of SM1127 EPS on skin wound healing and frostbite injury prevention were studied. Scratch wound assay showed that SM1127 EPS could stimulate the migration of HDFs. In the full-thickness cutaneous wound experiment of Sprague–Dawley (SD) rats, SM1127 EPS increased the wound healing rate and stimulated tissue repair detected by macroscopic observation and histologic examination, showing the ability of SM1127 EPS to promote skin wound healing. In the skin frostbite experiment of SD rats, pretreatment of rat skin with SM1127 EPS increased the rate of frostbite wound healing and promoted the repair of the injured skin significantly, indicating the good effect of SM1127 EPS on frostbite injury prevention. These results suggest the promising potential of SM1127 EPS in the pharmaceutical area to promote skin wound healing and prevent frostbite injury.
High-Level Extracellular Production of a Trisaccharide-Producing Alginate Lyase AlyC7 in Escherichia coli and Its Agricultural Application
Alginate oligosaccharides (AOS), products of alginate degradation by endotype alginate lyases, possess favorable biological activities and have broad applications. Although many have been reported, alginate lyases with homogeneous AOS products and secretory production by an engineered host are scarce. Herein, the alginate lyase AlyC7 from Vibrio sp. C42 was characterized as a trisaccharide-producing lyase exhibiting high activity and broad substrate specificity. With PelB as the signal peptide and 500 mM glycine as the additive, the extracellular production of AlyC7 in Escherichia coli reached 1122.8 U/mL after 27 h cultivation in Luria-Bertani medium. The yield of trisaccharides from sodium alginate degradation by the produced AlyC7 reached 758.6 mg/g, with a purity of 85.1%. The prepared AOS at 20 μg/mL increased the root length of lettuce, tomato, wheat, and maize by 27.5%, 25.7%, 9.7%, and 11.1%, respectively. This study establishes a robust foundation for the industrial and agricultural applications of AlyC7.
Potential of Marine Bacterial Metalloprotease A69 in the Preparation of Antarctic Krill Peptides with Multi-Bioactivities
Antarctic krill (Euphausia superba) is a nutrient-rich marine resource. Although several terrestrial proteases have been used to prepare Antarctic krill peptides (AKPs), there has been no report on the preparation of AKPs using a marine protease. Here, marine bacterial protease A69 was used to prepare AKPs with multi-bioactivities. Through optimizing hydrolysis parameters, we established a process for AKPs preparation by hydrolyzing Antarctic krill powder with A69. In the prepared AKPs, peptides less than 3000 Da and 1000 Da accounted for 99.23% and 88.37%, respectively. The scavenging ratios of the AKPs to ABTS+, DPPH· and ·OH reached 93.23 ± 0.09%, 99.90 ± 0.15%, and 93.90 ± 0.47%, respectively. The AKPs also had high angiotensin-converting enzyme (ACE)-inhibitory activity, with an IC50 of 0.22 ± 0.04 mg/mL. At 40 mg/mL, the AKPs inhibited α-glucosidase and dipeptidyl peptidase IV (DPP-IV) activities by 7.18% and 13.62%, respectively, and displayed antibacterial activity to Escherichia coli. Moreover, 14 antioxidant peptides, 24 ACE-inhibitory peptides, 2 α-glucosidase-inhibitory peptides, and 10 DPP-Ⅳ-inhibitory peptides were identified from the AKPs. These results demonstrate that the prepared AKPs contain diverse bioactive peptides and have multi-bioactivities. This study indicates that marine bacterial protease A69 has promising application potential in preparing AKPs with multi-bioactivities.
Potential of Thermolysin-like Protease A69 in Preparation of Bovine Collagen Peptides with Moisture-Retention Ability and Antioxidative Activity
Bovine bone is rich in collagen and is a good material for collagen peptide preparation. Although thermolysin-like proteases (TLPs) have been applied in different fields, the potential of TLPs in preparing bioactive collagen peptides has rarely been evaluated. Here, we characterized a thermophilic TLP, A69, from a hydrothermal bacterium Anoxybacillus caldiproteolyticus 1A02591, and evaluated its potential in preparing bioactive collagen peptides. A69 showed the highest activity at 60 °C and pH 7.0. We optimized the conditions for bovine bone collagen hydrolysis and set up a process with high hydrolysis efficiency (99.4%) to prepare bovine bone collagen peptides, in which bovine bone collagen was hydrolyzed at 60 °C for 2 h with an enzyme–substrate ratio of 25 U/g. The hydrolysate contained 96.5% peptides that have a broad molecular weight distribution below 10000 Da. The hydrolysate showed good moisture-retention ability and a high hydroxyl radical (•OH) scavenging ratio of 73.2%, suggesting that the prepared collagen peptides have good antioxidative activity. Altogether, these results indicate that the thermophilic TLP A69 has promising potential in the preparation of bioactive collagen peptides, which may have potentials in cosmetics, food and pharmaceutical industries. This study lays a foundation for the high-valued utilization of bovine bone collagen.
Pollen Analysis of Natural Honeys from the Central Region of Shanxi, North China
Based on qualitative and quantitative melissopalynological analyses, 19 Chinese honeys were classified by botanical origin to determine their floral sources. The honey samples were collected during 2010-2011 from the central region of Shanxi Province, North China. A diverse spectrum of 61 pollen types from 37 families was identified. Fourteen samples were classified as unifloral, whereas the remaining samples were multifloral. Bee-favoured families (occurring in more than 50% of the samples) included Caprifoliaceae (found in 10 samples), Laminaceae (10), Brassicaceae (12), Rosaceae (12), Moraceae (13), Rhamnaceae (15), Asteraceae (17), and Fabaceae (19). In the unifloral honeys, the predominant pollen types were Ziziphus jujuba (in 5 samples), Robinia pseudoacacia (3), Vitex negundo var. heterophylla (2), Sophora japonica (1), Ailanthus altissima (1), Asteraceae type (1), and Fabaceae type (1). The absolute pollen count (i.e., the number of pollen grains per 10 g honey sample) suggested that 13 samples belonged to Group I (<20,000 pollen grains), 4 to Group II (20,000-100,000), and 2 to Group III (100,000-500,000). The dominance of unifloral honeys without toxic pollen grains and the low value of the HDE/P ratio (i.e., honey dew elements/pollen grains from nectariferous plants) indicated that the honey samples are of good quality and suitable for human consumption.
Preparation and functional evaluation of collagen oligopeptide-rich hydrolysate from fish skin with the serine collagenolytic protease from Pseudoalteromonas sp. SM9913
Although several serine collagenolytic proteases from bacteria were reported, none has been used to prepare bioactive collagen peptides. MCP-01 is the most abundant extracellular protease of deep-sea Pseudoalteromonas sp. SM9913 and is a serine collagenolytic protease with high efficiency on fish collagen hydrolysis. Here, we set up a pilot scale process to ferment SM9913 for extracellular protease production. With SM9913 extracellular protease as a tool, a process to prepare collagen oligopeptide-rich hydrolysate from codfish skin was set up, which was further scaled up to pilot (100 L) and plant (2000 L) levels with yields >66%. The hydrolysates from laboratory-, pilot- and plant-scales had quite similar quality, containing ~95% peptides with molecular weights lower than 3000 Da and approximately 60% lower than 1000 Da, in which collagen oilgopeptides account for approximately 95%. Bioactivity analyses showed that the hydrolysate had moisture-retention ability, antioxidant activity, and promoting effect on cell viability of human dermal fibroblasts. Safety evaluation showed that the hydrolysate was nontoxic and nonirritating to skin. Therefore, SM9913 extracellular protease is a good enzyme to prepare bioactive oligopeptides from fish skin. The results also suggest that the collagen oligopeptides-rich hydrolysate may have potentials in biomedical, functional food, pharmaceutical and cosmetic industries.
Pedobacter indicus sp. nov., isolated from deep-sea sediment
A Gram-stain negative, aerobic, non-flagellated, rod-shaped bacterium, designated strain SM1810T, was isolated from deep-sea sediment collected from the Southwest Indian Ocean. Strain SM1810T grows at 15–40 °C (optimum, 28 °C), at pH 5.0–9.0 (optimum, pH 6.0–7.0) and with 0–8% (w/v) NaCl (optimum, 1.5%). Phylogenetic analysis of 16S rRNA gene sequences revealed that strain SM1810T is affiliated with the genus Pedobacter, sharing high sequence similarity (95.8%) with the type strain of Pedobacter bauzanensis. The major fatty acids of strain SM1810T are iso-C15:0, summed feature 3 (C16:1ω7c and/or C16:1ω6c) and iso-C17:0 3OH. The predominant respiratory quinone is MK-7. The polar lipids are phosphatidylethanolamine, an unidentified aminophospholipid, an unidentified phospholipid and eight unidentified lipids. The genomic DNA G + C content of strain SM1810T was determined to be 40.8 mol%. Based on the phylogenetic, chemotaxonomic and phenotypic data obtained in this study, strain SM1810T is concluded to represent a novel species of the genus Pedobacter, for which the name Pedobacter indicus sp. nov. is proposed. The type strain is SM1810T (KCTC 62798T = CCTCC AB 2018198T).
Improvement of the production of an Arctic bacterial exopolysaccharide with protective effect on human skin cells against UV-induced oxidative stress
Although microbial exopolysaccharides (EPSs) are applied in different fields, no EPS has been used to protect human skin cells against UV-induced oxidative stress. The EPS produced by the Arctic bacterium Polaribacter sp. SM1127 has high moisture-retention ability and antioxidant activity, suggesting its good industrial potentials. In this study, we improved the EPS production of SM1127 and evaluated its protective effect on human dermal fibroblasts (HDFs) against UV-induced oxidative stress. With glucose as carbon source, the EPS yield was increased from 2.11 to 6.12 g/L by optimizing the fermentation conditions using response surface methodology. To lower the fermentation cost and decrease corrosive speed in stainless steel tanks, whole sugar, whose price is only 8% of that of glucose, was used to replace glucose and NaCl concentration was reduced to 4 g/L in the medium. With the optimized conditions, fed-batch fermentation in a 5-L bioreactor was conducted, and the EPS production reached 19.25 g/L, which represents the highest one reported for a polar microorganism. Moreover, SM1127 EPS could maintain the cell viability and integrity of HDFs under UV-B radiation, probably via decreasing intracellular reactive oxygen species level and increasing intracellular glutathione content and superoxide dismutase activity. Therefore, SM1127 EPS has significant protective effect on HDFs against UV-induced oxidative stress, suggesting its potential to be used in preventing photoaging and photocarcinogenesis. Altogether, this study lays a good foundation for the industrialization of SM1127 EPS, which has promising potential to be used in cosmetics and medical fields.