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Saccharification of macroalgal polysaccharides through prioritized cellulase producing bacteria.

ABSTRACT: Marine macroalgal cell wall is predominantly comprised of cellulose (polysaccharide) with the complex chain of glycosidic linkages. Bioethanol production from macroalgae entails breaking this complex chain into simple glucose molecule, which has been the major challenge faced by the industries. Cellulases have been preferred for hydrolysis of cellulose due to the absence of inhibitors affecting the subsequent fermentation process. Cellulose degrading bacteria were isolated from wide-ranging sources from marine habitats to herbivore residues and gastrointestinal region. The investigation reveals that Vibrio parahaemolyticus bacteria has higher hydrolytic capacity with salt tolerance up to 14% and 3.5% salinity is optimum for growth. Higher hydrolytic activity of 2.45 was recorded on carboxymethyl cellulose medium at 48 h and hydrolytic activity of 2.46 on Ulva intestinalis hydrolysate, 3.06 on Ulva lactuca hydrolysate at 72 h of incubation. Total activity of enzyme of 2.11 U/ml and specific activity of 6.05 U/mg were recorded at 24 h. Enzyme hydrolysis of macroalgal biomass; U. intestinalis and U. lactuca produced 135.9 mg/g and 107.6 mg/g of reducing sugar respectively. The study reveals that the enzyme extracted from salt tolerant Vibrio parahaemolyticus bacteria is suitable for optimal saccharification of seaweed polysaccharides towards biofuel production.

SUBMITTER: Hebbale D

PROVIDER: S-EPMC6431756 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:BackgroundNon-productive binding of enzymes to lignin is thought to impede the saccharification efficiency of pretreated lignocellulosic biomass to fermentable sugars. Due to a lack of suitable analytical techniques that track binding of individual enzymes within complex protein mixtures and the difficulty in distinguishing the contribution of productive (binding to specific glycans) versus non-productive (binding to lignin) binding of cellulases to lignocellulose, there is currently a poor understanding of individual enzyme adsorption to lignin during the time course of pretreated biomass saccharification.ResultsIn this study, we have utilized an FPLC (fast protein liquid chromatography)-based methodology to quantify free Trichoderma reesei cellulases (namely CBH I, CBH II, and EG I) concentration within a complex hydrolyzate mixture during the varying time course of biomass saccharification. Three pretreated corn stover (CS) samples were included in this study: Ammonia Fiber Expansion(a) (AFEX™-CS), dilute acid (DA-CS), and ionic liquid (IL-CS) pretreatments. The relative fraction of bound individual cellulases varied depending not only on the pretreated biomass type (and lignin abundance) but also on the type of cellulase. Acid pretreated biomass had the highest levels of non-recoverable cellulases, while ionic liquid pretreated biomass had the highest overall cellulase recovery. CBH II has the lowest thermal stability among the three T. reesei cellulases tested. By preparing recombinant family 1 carbohydrate binding module (CBM) fusion proteins, we have shown that family 1 CBMs are highly implicated in the non-productive binding of full-length T. reesei cellulases to lignin.ConclusionsOur findings aid in further understanding the complex mechanisms of non-productive binding of cellulases to pretreated lignocellulosic biomass. Developing optimized pretreatment processes with reduced or modified lignin content to minimize non-productive enzyme binding or engineering pretreatment-specific, low-lignin binding cellulases will improve enzyme specific activity, facilitate enzyme recycling, and thereby permit production of cheaper biofuels.

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Saccharification of macroalgal polysaccharides through prioritized cellulase producing bacteria.

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