70 research outputs found
Novel combination of feed enzymes to improve the degradation of Chlorella vulgaris recalcitrant cell wall
Research Areas: Science & TechnologyABSTRACT - In this study, a rational combination of 200 pre-selected Carbohydrate-Active enzymes (CAZymes) and
sulfatases were tested, individually or combined, according to their ability to degrade Chlorella vulgaris
cell wall to access its valuable nutritional compounds. The disruption of microalgae cell walls by a four enzyme mixture (Mix) in comparison with the control, enabled to release up to 1.21g/L of reducing
sugars (p<0.001), led to an eight-fold increase in oligosaccharides release (p<0.001), and reduced
the fuorescence intensity by 47% after staining with Calcofuor White (p<0.001). The Mix treatment
was successful in releasing proteins (p<0.001), some MUFA (p<0.05), and the benefcial 18:3n-3 fatty
acid (p0.05), total carotenoids were
increased in the supernatant (p<0.05) from the Mix treatment, relative to the control. Taken together,
these results indicate that this four-enzyme Mix displays an efective capacity to degrade C. vulgaris cell
wall. Thus, these enzymes may constitute a good approach to improve the bioavailability of C. vulgaris
nutrients for monogastric diets, in particular, and to facilitate the cost-efective use of microalgae by
the feed industry, in general.info:eu-repo/semantics/publishedVersio
Evidence for temporal regulation of the two Pseudomonas cellulosa xylanases belonging to glycoside hydrolase family 11
The membrane-bound α-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan
The N-terminal family 22 carbohydrate-binding module of xylanase 10B of Clostridium themocellum is not a thermostabilizing domain
Homologous xylanases from Clostridium thermocellum: evidence for bi-functional activity, synergism between xylanase catalytic modules and the presence of xylan-binding domains in enzyme complexes
Crystal Structure of a Cellulosomal Family 3 Carbohydrate Esterase from Clostridium thermocellum Provides Insights into the Mechanism of Substrate Recognition.
Probing the β-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants
Family 46 Carbohydrate-binding Modules Contribute to the Enzymatic Hydrolysis of Xyloglucan and β-1,3–1,4-Glucans through Distinct Mechanisms
Overproduction, purification, crystallization and preliminary X-ray characterization of the C-terminal family 65 carbohydrate-binding module (CBM65B) of endoglucanase Cel5A from Eubacterium cellulosolvens
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