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Platform Molecules from Algae by Using Supercritical CO2 and Subcritical Water Extraction
Published in Gokare A. Ravishankar, Ranga Rao Ambati, Handbook of Algal Technologies and Phytochemicals, 2019
Nidhi Hans, Satya Narayan Naik, Anushree Malik
Enzymes are the biological catalyst that enhances the rate of conversion of substrate to product under mild conditions. Mixtures of enzymes are used to enhance the extraction of targeted bioactive compounds from algae, like proteins, phenols, carotenoids and lipids, by degrading its cell wall, which is chemically and structurally heterogeneous. Enzymes used in this method are nontoxic, ecofriendly and of food grade (Michalak and Chojnacka, 2014). Enzymes used frequently are amyloglucosidase, agarase, alcalase (for hydrolysis of proteins), carragenanase, celluclast (to break cellulosic material), kojizyme (protease), neutrase (metallo-proteinase), termamyl (amylase), ultraflo (hydrolyze 1,3- or 1,4- linkages in β-D-glucans xylanase), umamizyme (proteolytic enzyme), xylanase and viscozyme (break cell wall) (Kadam et al., 2013). This technology is highly specific and is executed under mild conditions to protect bioactive compounds from degradation. This technique is difficult to scale up to industrial scale as enzyme activities vary with different environmental conditions.
Biodiscovery of Marine Microbial Enzymes in Indonesia
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Ekowati Chasanah, Pujo Yuwono, Dewi Seswita Zilda, Siswa Setyahadi
Agarase is a hydrolytic enzyme that is capable of hydrolyzing agar into agar-oligosaccharides. There are grouped as α-agarases and β-agarases according to the sites of hydrolysis. The α-agarases cleave the α-L-(1,3) linkages of agarose to produce oligosaccharides, namely, agarobiose, whereas the β-agarases cleave the β-D-(1,4) linkages of agarose to produce neoagarooligosaccharides. Oligosaccharide products with 3,6-anhydro-L-galactopyranose at the reducing end are produced by α-agarases while products with D-galactopyranoside residues at the reducing end are produced by β-agarases (Li, Sha, Zilda, Hu, & He, 2014) (Anggraeni & Ansorge-Schumacher, 2021). Biodiscovery research on agarase from Indonesia reported that Bacillus sp. BI-3 produce thermostable agarase when cultured in a medium composed of 0.3% (w/v) peptone, 0.3% (w/v) yeast extract, 0.3% (w/v) NaCl, and 2.0% (w/v) agar incubated at 55°C. The bacteria were isolated from a hot spring in Kalianda, Lampung. The pure enzyme, with a size of 58 kDa, was obtained by running the cell-free crude enzyme onto a Q-Sepharose column (2.6 × 40 cm), followed by a Sephacryl S-200 column. The agarase enzyme works best at a pH of 6.4 and a temperature of 70°C, but it is stable and active in a pH range of 5.8–8.0 at 80°C for 15 min. This enzyme is interesting because it produced neoagarobiose as the final product, which has great potential in the cosmetics industry since the reported product can perform both moisturizing and whitening effects on skin (Kobayashi, Takisada, Suzuki, Kirimura, & Usami, 1997). Another interesting agarase from Indonesia has been reported from Microbulbifer elongatus PORT2 that have been isolated from seawater in Batu Karas, Pangandaran, West Java, Indonesia. PORT2 recombinant agarases (which were expressed in E. coli) worked best at 50°C as thermostable agarases even though the bacteria Microbulbifer elongatus were from a mesophilic environment. The agarases’ activity produced not only the saccharides neagarohexaose (NA6), neoagarotetraose (NA4) and neoagraobiose (NA2), which are typical agar-derived products, but also the modified ones from Indonesian natural agar, which is promising potential novel bioactivity (Anggraeni & Ansorge-Schumacher, 2021). Agarase has also been detected in Vibrio alteromonas, Salinivibrio and Marinobacter that were isolated from marine sediment of Bara Caddi, South Sulawesi, Indonesia (Zilda, Patantis, Prawira, Sibero, & Fawzya, 2021).
Linear and branched β-Glucans degrading enzymes from versatile Bacteroides uniformis JCM 13288T and their roles in cooperation with gut bacteria
Published in Gut Microbes, 2020
Ravindra Pal Singh, Sivasubramanian Rajarammohan, Raksha Thakur, Mohsin Hassan
Macroalgae is commonly used as dietary fibers in Japanese population every day with an estimate of 14.2 g per person per day – mainly in the form of nori and wasabi.54 These dietary fibers are mainly utilized by the human gut bacteria, in which Bacteroides is predominantly present1 and renders unprecedented benefits for gut health.2,7 The array of CAZymes present in Bacteroides is highly diverse7 and there is a growing understanding that dietary fibers act as a selective pressure to acquire unique genes or gene clusters from other environments. In order to further reinforce this concept, we sequenced a genome of the Japanese gut bacterium, B. uniformis JCM 13288 T, which is shown to be unique in a sense that it can robustly grow on macroalgal glycans such as laminarin, agarose, porphyran (Figure 2(e)), and fungal derived glucan (Supplementary Fig. S11). Its genome sequence was compared with B. uniformis JCM 5828, wherein AP-PUL was found to be uniquely present only in the JCM 13288 T strain that enabled it to grow on porphyran and agarose. Astonishingly, AP-PUL of the B. uniformis JCM 13288 T showed 100% synteny to the P- PUL present in B. plebeius. We looked for homology of some of the genes of AP-PUL in public domain (NCBI-BlastP), which matched mostly with marine bacteria with varied degree of identities, 24 to 60% (Supplementary excel sheet 1). This observation was congruent with previous findings, which suggest that enrichment of CAZymes for utilization of macroalgae in Bacteroides most likely happened through HGT-ICE events from marine bacteria that are commonly consumed along with food/dietary fibers.55,56 PULs for agarose/porphyran digestion are highly abundant in the metagenomes of Japanese populations;55 however, the ICE containing the AP-PUL identified in our study is unique and contains an additional PUL (PUL45) (Figure 2(c) and supplementary excel sheet 1). We hypothesize that the common regions contained within the ICEs may be the ancestral architecture of the ICE and the B. uniformis JCM13288T strain contains a second ICE (containing PUL45) that integrated within the ancestral ICE without disrupting the functionality of PUL46 that allowed the strain to grow on porphyran. The PUL45, based on genomic analysis, is predicted to be involved in utilization of chondritic sulfate/heparin sulfate and a gene (BUNIF_04562) near to the 3ʹ end of tRNA-lys, which showed 40% homology to β- agarase (PDB-5T3B) of the B. plebeius, present in another location of the genome. Further studies may be required to check the activity of this identified β- agarase gene. Therefore, the genomic architecture of this ICE is unique and to the best of our knowledge has not been reported from any other Bacteroides species. Further functional genomics investigations may throw light on the additional role(s) of this ICE region apart from agarose/porphyran utilization.