282727-46-2Relevant articles and documents
Simplified determination of the content and average degree of acetylation of chitin in crude black soldier fly larvae samples
D'Hondt, Els,Soetemans, Lise,Bastiaens, Leen,Maesen, Miranda,Jespers, Vincent,Van den Bosch, Bert,Voorspoels, Stefan,Elst, Kathy
supporting information, (2020/01/25)
Insects are considered a promising alternative protein source for food and feed, but contain significant amounts of chitin, often undesirable due to indigestibility, disagreeable texture and negative effect on nutrients intake. Fractionation strategies are thus increasingly being applied to isolate and valorize chitin separately. The analysis of chitin generally requires an intensive pretreatment to remove impurities, and derivatization to generate sufficient detector response. In this work, a liquid chromatography method, without pretreatment nor derivatization, was developed for the simultaneous determination of chitin content and degree of acetylation in non-purified samples of black soldier fly (BSF) larvae. The method is found to be more suitable, compared to traditional methods, for assessing high degrees of acetylation. For the first time, the degree of acetylation of BSF chitin (81 ± 2%) is reported. Additionally, the chitin content of BSF soft tissues is estimated at approximately 20% of the total chitin content (8.5 ± 0.1%).
Process optimization, purification and characterization of a novel acidic, thermostable chitinase from Humicola grisea
Kumar, Manish,Brar, Amandeep,Vivekanand,Pareek, Nidhi
, p. 931 - 938 (2018/05/29)
An extracellular acidic and thermostable chitinase (HgChi) from thermophilic Humicola grisea was purified and characterized. Enhancement in chitinase production (Qp = 2.9662 Ul?1 h?1) was achieved through derivation of optimum fermentation conditions via central composite design. H. grisea observed to produce various isoforms of chitinase, among which the major expressed form has molecular mass of about 50 kDa. Purified chitinases exhibited optimal activity at pH 3.0 and 70 °C. Chitinase showed notable stability at increasing temperatures. Half-life of chitinase is 169.06 min at optimum temperature. Chitinase has effectively catalyzed N-acetyl chitobiose (GlcNAc)2, and N-acetyl chitotriose (GlcNAc)3 and colloidal chitin. Purified chitinase from H. grisea showed high affinity towards colloidal chitin as evident by its comparatively lower Km value. Presence of metal ions viz. Mn2+, Co2+, NH4 + and Mg2+ significantly increased the chitinase activity. Thin layer chromatography (TLC) analysis revealed the significant hydrolyzing competence of HgChi for colloidal chitin, (GlcNAc)3 and (GlcNAc)2 into oligomers and N-acetyl–D-glucosamine (GlcNAc). Thermostable chitinase appeared as potential candidate for efficient conversion of chitin to bioactive oligosaccharides at industrial scale.
Pro-apoptotic activity of acylated triterpenoid saponins from the stem bark of Albizia chevalieri harms
Noté, Olivier Placide,Messi, Lin Marcellin,Mbing, Joséphine Ngo,Azouaou, Sarah Ali,Sarr, Mamadou,Guillaume, Dominique,Muller, Christian Dominique,Pegnyemb, Dieudonné Emmanuel,Lobstein, Annelise
, p. 95 - 101 (2017/10/05)
As a continuation of our interest in apoptosis-inducing triterpenoid saponins from Albizia genus, phytochemical investigation of the stem bark of Albizia chevalieri led to the isolation of three new oleanane-type saponins, named chevalierosides A–C (1–3). Their structures were established on the basis of extensive analysis of 1D and 2D NMR (1H-, 13C NMR, DEPT, COSY, TOCSY, ROESY, HSQC and HMBC) experiments, HRESIMS studies, and by chemical evidence. The pro-apoptotic effect of the three saponins was evaluated on two human cell lines (pancreatic carcinoma AsPC-1 and hematopoietic monocytic THP-1). Cytometric analyses showed that saponins 1–3 induced apoptosis of both human cell lines (AsPC-1 and THP-1) in a dose-dependent manner.