Effect of paprika extracts on growth performance, haemolymph chemistry, intestinal microbiota and antioxidant enzyme activities of white-leg shrimp (Litopenaeus vannamei).

This study aims to evaluate the effects of paprika extract on the survival rate, growth performance and stimulation of the innate immune system of Litopenaeus vannamei. In this experiment, 240 healthy shrimp (3.22 ± 0.12 g) were randomly divided into four groups. The shrimp were fed diets with different concentrations of paprika oil extracts (0%, 0.5%, 1% and 2%) for 8 weeks. The results showed that growth performance, urea, uric acid, creatinine, cholesterol levels, aspartate aminotransferase and alkaline phosphatase activities were not significantly affected by adding paprika extract to the shrimp diet (p > 0.05). Diets containing 1% and 0.5% paprika extract showed the highest levels of total protein and triglyceride, respectively (p < 0.05). There was a significant decrease in haemolymph glucose concentration in shrimp-fed diets containing 1% and 2% paprika extract (p < 0.05). Moreover, a diet containing 0.5% paprika extract resulted in the highest levels of total heamocyte count, hyaline cells and large-granular cells in shrimp (p < 0.05). Higher catalase and superoxide dismutase activities were also exhibited in the paprika groups (p < 0.05). Vibrio sp. bacteria were not significantly reduced by paprika extract in the intestines of L. vannamei (p > 0.05). A significant decrease in heterotrophic bacteria was observed with increasing extract concentrations (p < 0.05). The shrimp culture industry can utilize paprika extract as a cost-effective, efficient and environmentally friendly immune stimulant at a concentration of 0.5%.

The first reporting of prevalence Vibrio species and expression of HSP genes in rayed pearl oyster (Pinctada radiata) under thermal conditions.

The main goal of the present study was to evaluate the influence of thermal exposure on Vibrio population and HSP genes expression (HSP 90, HSP70, and HSP20) in rayed pearl oyster (P. radiata). To this end, the oysters were reared for 30 days at temperatures of 22 °C (control), 25 °C, 27 °C, and 29 °C. The results showed that five dominate Vibrio strains including Vibrio hepatarius, V. harveyi, V. alginolyticus, V. parahaemolyticus, and V. rotiferianus were identified. The highest population of V. parahaemolyticus, V. alginolyticus, and V. harveyi, was found in 29οC group. According to real-time PCR, mantle exhibited the highest expression levels of HSP20, HSP70, and HSP90 genes. A higher level of HSP20 expression was observed at high temperatures (25 °C, 27 °C, and 29 °C) in the gonad and mantle compared to the control group (22 °C) while decrease in HSP90 expression level was recorded in 25 °C, 27 °C, and 29 °C groups. HSP20 expression level in adductor muscle was remarkably down-regulated in 27 °C and 29 °C groups. In this tissue, HSP70 was detected at highest levels in the 29οC group. In mantle, HSP90 gene expression was lowest at 22 °C water temperature. Several Vibrio strains have been identified from pearl Gulf oyster that haven't been previously reported. The identification of dominant Vibrio species is essential for epidemiological management strategies to control and prevent Vibrio outbreaks in pearl oyster farms. The expression pattern of HSP genes differs in rayed pearl oyster tissues due to differences in their thermal tolerance capability and physiological and biological characteristics. The present study provides useful molecular information for the ecological adaptation of rayed pearl oysters after exposure to different temperature levels.

Marine Bacterial Dextranases: Fundamentals and Applications.

Dextran, a renewable hydrophilic polysaccharide, is nontoxic, highly stable but intrinsically biodegradable. The α-1, 6 glycosidic bonds in dextran are attacked by dextranase (E.C. 3.2.1.11) which is an inducible enzyme. Dextranase finds many applications such as, in sugar industry, in the production of human plasma substitutes, and for the treatment and prevention of dental plaque. Currently, dextranases are obtained from terrestrial fungi which have longer duration for production but not very tolerant to environmental conditions and have safety concerns. Marine bacteria have been proposed as an alternative source of these enzymes and can provide prospects to overcome these issues. Indeed, marine bacterial dextranases are reportedly more effective and suitable for dental caries prevention and treatment. Here, we focused on properties of dextran, properties of dextran-hydrolyzing enzymes, particularly from marine sources and the biochemical features of these enzymes. Lastly the potential use of these marine bacterial dextranase to remove dental plaque has been discussed. The review covers dextranase-producing bacteria isolated from shrimp, fish, algae, sea slit, and sea water, as well as from macro- and micro fungi and other microorganisms. It is common knowledge that dextranase is used in the sugar industry; produced as a result of hydrolysis by dextranase and have prebiotic properties which influence the consistency and texture of food products. In medicine, dextranases are used to make blood substitutes. In addition, dextranase is used to produce low molecular weight dextran and cytotoxic dextran. Furthermore, dextranase is used to enhance antibiotic activity in endocarditis. It has been established that dextranase from marine bacteria is the most preferable for removing plaque, as it has a high enzymatic activity. This study lays the groundwork for the future design and development of different oral care products, based on enzymes derived from marine bacteria.

Cellulolytic and Xylanolytic Enzymes from Yeasts: Properties and Industrial Applications.

Lignocellulose, the main component of plant cell walls, comprises polyaromatic lignin and fermentable materials, cellulose and hemicellulose. It is a plentiful and renewable feedstock for chemicals and energy. It can serve as a raw material for the production of various value-added products, including cellulase and xylanase. Cellulase is essentially required in lignocellulose-based biorefineries and is applied in many commercial processes. Likewise, xylanases are industrially important enzymes applied in papermaking and in the manufacture of prebiotics and pharmaceuticals. Owing to the widespread application of these enzymes, many prokaryotes and eukaryotes have been exploited to produce cellulase and xylanases in good yields, yet yeasts have rarely been explored for their plant-cell-wall-degrading activities. This review is focused on summarizing reports about cellulolytic and xylanolytic yeasts, their properties, and their biotechnological applications.

Marine microbial L-glutaminase: from pharmaceutical to food industry.

Deamination of L-glutamine to glutamic acid with the concomitant release of ammonia by the activity of L-glutaminase (L-glutamine amidohydrolase EC 3.5.1.2) is a unique reaction that also finds potential applications in different sectors ranging from therapeutics to food industry. Owing to its cost-effectiveness, rapidity, and compatibility with downstream processes, microbial production of L-glutaminase is preferred over the production by other sources. Marine microorganisms including bacteria, yeasts, and moulds have manifested remarkable capacity to produce L-glutaminase and, therefore, are considered as prospective candidates for large-scale production of this enzyme. The main focus of this article is to provide an overview of L-glutaminase producing marine microorganisms, to discuss strategies used for the lab- and large-scale production of these enzyme and to review the application of L-glutaminase from marine sources so that the future prospects can be understood. KEY POINTS: • L-glutaminase has potential applications in different sectors ranging from therapeutics to food industry • Marine microorganisms are considered as prospective candidates for large-scale production of L-glutaminase • Marine microbial L-glutaminase have great potential in therapeutics and in the food industry.

Cloning and Expression of N-CFTX-1 Antigen from Chironex fleckeri in Escherichia coli and Determination of Immunogenicity in Mice.

BACKGROUND: Most jellyfish species are poisonous. Human victims of jellyfish sting each year are 120 million. Chironex fleckeri is a venomous box jellyfish that inflicts painful and potentially fatal stings to humans. The CfTX-1 is one of the antigenic proteins of venom that is suggested to stimulate the immune system for treatment and vaccine. This study aimed to clone and express the CfTX-1 antigen in E. coli and then to determine the synthesis of related antibody in the mice. METHODS: The study was performed in the Persian Gulf and Oman Sea Ecology Research Center, Bandar Abbas, Iran in autumn 2016. The synthetic CfTX-1 gene in PUC57 plasmid was purchased from Nedaye Fan Company. The 723 bp fragment of N-CfTX-1 was amplified by PCR, PUC57 plasmid containing CfTX-1 with BamHI SalI restriction enzyme sites were subcloned in pET28a [+] expression vector and transformed into E. coli BL21 (DE3). The CfTX-1 gene expression was induced by IPTG. Then antibody produced from the mice serum were isolated and confirmed by ELISA. After protein purification, resulted antigen was injected to mice in 4 repeats and then evaluated the rate of antibody in mice serum. Mice were challenged by the Carybdea alata. RESULTS: The 726 bp of N-CfTX-1 were cloned in a vector of expression pET28a [+] and confirmed by PCR, sequencing and enzymatic analysis. Moreover, the recombinant protein was confirmed by SDS-PAGE and Western blotting. Then the antibody was isolated from mice serum and confirmed by ELISA test. The results showed that immunized mice tolerated 50x LD501 of jellyfish venom. CONCLUSION: The CfTX-1 recombinant protein was able to protect the BALB/c mice against jellyfish venom. The produced protein can be used as a candidate for vaccine against jellyfish venom.

Marine Bacterial Esterases: Emerging Biocatalysts for Industrial Applications.

The marine ecosystem has been known to be a significant source of novel enzymes. Esterase enzymes (EC 3.1.1.1) represent a diverse group of hydrolases that catalyze the cleavage and formation of ester bonds. Although esterases are widely distributed among marine organisms, only microbial esterases are of paramount industrial importance. This article discusses the importance of marine microbial esterases, their biochemical and kinetic properties, and their stability under extreme conditions. Since culture-dependent techniques provide limited insights into microbial diversity of the marine ecosystem, therefore, genomics and metagenomics approaches have widely been adopted in search of novel esterases. Additionally, the article also explains industrial applications of marine bacterial esterases particularly for the synthesis of optically pure substances, the preparation of enantiomerically pure drugs, the degradation of human-made plastics and organophosphorus compounds, degradation of the lipophilic components of the ink, and production of short-chain flavor esters.

A critical review on marine serine protease and its inhibitors: A new wave of drugs?

Marine organisms are rich sources of enzymes and their inhibitors having enormous therapeutic potential. Among different proteolytic enzymes, serine proteases, which can be obtained from various marine organisms show a potential to biomedical application as thrombolytic agents. Although this type of proteases plays a crucial role in almost all biological processes, their uncontrolled activity often leads to several diseases. Accordingly, the actions of these types of proteases are regulated by serine protease inhibitors (SPIs). Marine SPIs control complement activation and various other physiological functions, such as inflammation, immune function, fibrinolysis, blood clotting, and cancer metastasis. This review highlights the potential use of serine proteases and their inhibitors as the new wave of promising drugs.

Metabolites from Marine Microorganisms, Micro, and Macroalgae: Immense Scope for Pharmacology.

Marine organisms produce a large array of natural products with relevance in drug discovery. These compounds have biological activities such as antioxidant, antibacterial, antitumor, antivirus, anticoagulant, anti-inflammatory, antihypertensive, antidiabetic, and so forth. Consequently, several of the metabolites have made it to the advanced stages of clinical trials, and a few of them are commercially available. In this review, novel information on natural products isolated from marine microorganisms, microalgae, and macroalgae are presented. Given due research impetus, these marine metabolites might emerge as a new wave of promising drugs.

Morphometrics and Mitochondrial DNA Genes Analysis Suggest a New Species of Penaeus (Crustacea: Penaeidae) from the Persian Gulf.

There are two morphotypes of Penaeus semisulcatus described hitherto in the Persian Gulf, namely the banded and non-banded antennae morphotypes. In this study, we used morphometric measurements and two mitochondrial genes (16S rRNA and cytochrome oxidase subunit I-COI) to assess relationships between the two morphotypes of P. semisulcatus. Out of 25 morphological characters examined, 10 characters were found significantly different between the two morphotypes when tested against separate sexes or both sexes combined. Results from the 16S rRNA and COI sequence analysis of two morphotypes of P. semisulcatus morphotype showed up to 6% and 17% sequence divergence, respectively. The 16S rDNA and COI sequences of the non-banding morphotype were not only very different to those of the banding morphotype but was also very different to all other Penaeus species (i.e., P. monodon, P. merguiensis, and P. indicus) included in the study. Both parsimony and Neighbor-Joining trees based on 16S rDNA and COI sequences provide similar tree topology that clearly separated the two morphotypes into two distinct groups. Based on these findings, we propose the two morphotypes of P. semisulcatus to be relegated as two sympatric species.

Marine bacterial chitinase as sources of energy, eco-friendly agent, and industrial biocatalyst.

Chitin is the richest renewable polymer carbohydrate in the marine environment and is an energetic source of nitrogen and carbon for marine organisms. Marine chitinolytic bacteria play a basic role in the nutrient cycling in the oceans by biodegradation of chitinous waste to useful form. Chitinase-producing bacteria from marine wastes increasing attention has received, and it serves two purposes: (i) reduce environmental hazards by waste management and (ii) increases generation of industrially important value-added products. This review aims to present the environmental pitfalls caused by marine waste and successes of chitinase-producing bacteria in employ waste for the generation of functional and valuable products, as well as to present importance role of chitinase-producing bacteria in industry. The focus is on isolation, purification, biochemical and enzymatic characteristics of chitinolytic bacteria in the oceans.