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Biodiscovery of Marine Microbial Enzymes in Indonesia
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Ekowati Chasanah, Pujo Yuwono, Dewi Seswita Zilda, Siswa Setyahadi
From what we delivered, Indonesia is also rich in unique biocatalysts that can potentially be used as bioconversion agent-producing ingredients and processing aids. Until now, Indonesia is importing microbial biocatalysts and ingredients to support their industries. Microbial enzymes, especially from marine life, offer a uniqueness that industries need most due to their safety, specificity and environmentally friendly processes. It is estimated that the growth of the enzyme industry is increasing both local and globally, so it is possible to develop domestic enzyme industries in Indonesia. But the challenge is to create a strategy that strongly supports national industries by utilizing the genetic resources originating in Indonesia.
Biotransformation of Monoterpenoids by Microorganisms, Insects, and Mammals
Published in K. Hüsnü Can Başer, Gerhard Buchbauer, Handbook of Essential Oils, 2020
Yoshiaki Noma, Yoshinori Asakawa
One of the first reports in this area dealt with the biotransformation of citronellol (258) by B. cinerea (Brunerie et al., 1987a, 1988). The substrate was mainly metabolized by ω-hydroxylation. The same group also investigated the bioconversion of citral (275 and 276) (Brunerie et al., 1987b). A comparison was made between grape must and a synthetic medium. When using grape must, no volatile bioconversion products were found. With a synthetic medium, biotransformation of citral (275 and 276) was observed yielding predominantly nerol (272) and geraniol (271) as reduction products and some ω-hydroxylation products as minor compounds. Finally, the bioconversion of geraniol (271) and nerol (272) was described by the same group (Bock et al., 1988). When using grape must, a complete bioconversion of geraniol (271) was observed mainly yielding ω-hydroxylation products.
B-Group Vitamin-Producing Lactic Acid Bacteria
Published in Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani, Lactic Acid Bacteria, 2020
Marcela Albuquerque Cavalcanti de Albuquerque, María del Milagro Teran, Luiz Henrique Groto Garutti, Ana Clara Candelaria Cucik, Susana Marta Isay Saad, Bernadette Dora Gombossy de Melo Franco, Jean Guy LeBlanc
The concept of bioavailability is defined as the proportion of a food compound that is absorbed by the organism and achieves the systemic circulation. It depends on two mainly factors: (1) bioaccessibility, that refers to the proportion of a food compound released from the food matrix in a absorbable form in the gastrointestinal tract; (2) bioconversion, that is the fraction of the component converted to the active form. The bioefficacy is the sum of bioavailability and bioconversion (Marze et al. 2017).
Enzyme-assisted modification of flavonoids from Matricaria chamomilla: antioxidant activity and inhibitory effect on digestive enzymes
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Elida Paula Dini de Franco, Fabiano Jares Contesini, Bianca Lima da Silva, Anna Maria Alves de Piloto Fernandes, Camila Wielewski Leme, João Pedro Gonçalves Cirino, Paula Renata Bueno Campos, Patrícia de Oliveira Carvalho
The bioconversion reaction was carried out in screw-capped glass tubes with shaking (130 rpm) at controlled temperature (40 °C) for 8 h using 10 ml of aqueous infusion of Matricaria chamomilla. To initiate the hydrolysis of the flavonoid glycosides, 1 ml of enzyme mixture solution prepared in 0.1 M acetate buffer pH 4.0 was added to the reaction mixture. The enzyme mixture used had equal parts of each up (hesperidinase and β-galactosidase) to a final concentration of 0.02 mg/mL. Optimisation of hydrolysis conditions and incubation time using the enzyme combination was previously performed21. The reactions were stopped by boiling for 20 min and the samples were stored in a refrigerator to await analysis. The assays were performed in triplicate. According to the manufacturer’s information, hesperidinase expresses both α-l-rhamnosidase (EC 3.2.1.40) and β-d-glucosidase (3.2.1.21) activities. One unit will liberate 1.0 µmole of reducing sugar (as glucose) from hesperidin per min at pH 3.8, at 40 °C. For β-galactosidase activity, one unit will hydrolyse 1.0 µmole of lactose per minute at pH 4.5, at 30 °C.
Biological activity of terpene compounds produced by biotechnological methods
Published in Pharmaceutical Biology, 2016
Roman Paduch, Mariusz Trytek, Sylwia K. Król, Joanna Kud, Maciej Frant, Martyna Kandefer-Szerszeń, Jan Fiedurek
Erlenmeyer flasks containing 50 mL of sterile BM media were inoculated uniformly with 2 mL of fungal spore suspensions (about 4 × 105 spores) and cultivated at 20 °C on a rotary shaker (150 rpm). For biotransformation of (−)-α-pinene with C. pannorum, the substrate was added to the medium sequentially (at a total of 1.5% v/v). Bioconversions were started by adding 0.2% of (−)-α-pinene to a 1-d-old fungal culture and then in doses of 0.3, 0.5, and 0.5% every 12 h, after which bioconversion was continued for 36 h at 20 °C. Total bioconversion time was 72 h. In the case of M. minutissima-based biotransformation, after 72 h of fungal growth, 500 μL of 50% (R)-(+)-limonene solution in methanol was added to the medium and converted for further 48 h at 15 °C.
Preclinical developments of enzyme-loaded red blood cells
Published in Expert Opinion on Drug Delivery, 2021
Luigia Rossi, Francesca Pierigè, Alessandro Bregalda, Mauro Magnani
Enzyme delivery is a medical need for several conditions, including the treatment of metabolic diseases, the treatment of acute or chronic assumption of alcohol and the treatment of certain forms of cancer. The key requirements for an effective benefit in the usage of therapeutic enzymes are listed below and, among the other, we find that the drug must be specific for the bioconversion of the target substrate, must be stable, must be retained in circulation, and has no or limited immunogenicity. These conditions are not easily obtainable and frequently one achievement is obtained at the expense of another relevant property. The selection of the therapeutic enzyme usually benefits from the genetic variability found in a number of living organisms and the selected enzyme may be advantageously optimized by protein engineering. This approach was successful in several cases. We currently have therapeutic enzymes that derive from genes present in algae, bacteria and in other living organisms but not in the human genome. A far more complex issue is the handling of immunogenicity. In fact, many therapeutic enzymes have been approved by the FDA and other regulatory agencies by the inclusion of a black box highlighting the risk of anaphylaxis and guidelines that have to be strictly followed through drug titration, administration in the presence of an expert clinician and other mandatory procedures. To overcome this critical issue experienced by several therapeutic enzymes, the protein is commonly PEGylated. PEGylation apparently reduce immunogenicity and protect the therapeutic protein from the inactivation by anti-drug antibodies but, in some cases, patients have also developed anti-PEG antibodies.