Next generation applications of lignin derived commodity products, their life cycle, techno-economics and societal analysis.

The pulp and biorefining industries produce their waste as lignin, which is one of the most abundant renewable resources. So far, lignin has been remained severely underutilized and generally burnt in a boiler as a low-value fuel. To demonstrate lignin's potential as a value-added product, we will review market opportunities for lignin related applications by utilizing the thermo-chemical/biological depolymerization strategies (with or without catalysts) and their comparative evaluation.

Multifunctional silica-coated mixed polymeric micelles for integrin-targeted therapy of pediatric patient-derived glioblastoma.

Glioblastoma multiforme (GBM) remains a major cause of mortality because treatments are precluded by to the limited transport and penetration of chemotherapeutics across the blood-brain barrier. Pitavastatin (PTV) is a hydrophobic Food and Drug Administration (FDA)-approved anticholesterolemic agent with reported anti-GBM activity. In the present study, we encapsulate PTV in silica-coated polymeric micelles (SiO PMs) surface-modified with the cyclic peptide Arg-Gly-Asp-Phe-Val (cRGDfV) that actively targets the αβ integrin overexpressed in the BBB endothelium and GBM.

Multidomain drug delivery systems of β-casein micelles for the local oral co-administration of antiretroviral combinations.

The antiretroviral (ARV) cocktailrevolved the treatment of the human immunodeficiency virus (HIV) infection. Drug combinations have been also tested to treat other infectious diseases, including the recentcoronavirus disease 2019 (COVID-19) outbreak. To simplify administration fixed-dose combinationshave been introduced, however, oral anti-HIV therapy still struggles with low oral bioavailability of many ARVs.

Enhanced Thermostability and Anticancer Activity in Breast Cancer Cells of Laccase Immobilized on Pluronic-Stabilized Nanoparticles.

Laccases are multi-copper oxidase enzymes having widespread applications in various biotechnological fields. However, low stability of free enzymes restricts their industrial use. Development of effective methods to preserve and even increase the enzymatic activity is critical to maximize their use, though this remains a challenge.

Draft genome analysis of lignocellulolytic enzymes producing Aspergillus terreus with structural insight of β-glucosidases through molecular docking approach.

Members of the genus Aspergillus are extensively studied ascomycetes because of their ability to synthesize high value-added compounds and enzymes of industrial interest. Precise whole genome assembly and gene annotation are significant for gene functional analyses. Here, we report the draft genome sequencing, assembly and whole genome analysis of Aspergillus terreus P14_T3, isolated from rumen sample of cattle fed with coconut-coir.

Development of eco-friendly process for the production of bioethanol from banana peel using inhouse developed cocktail of thermo-alkali-stable depolymerizing enzymes.

Conversion of agro-industrial wastes to energy is an innovative approach for waste valorization and management which also mitigates environmental pollution. In this view, present study investigated the feasibility of producing bioethanol from banana peels using cocktail of depolymerizing enzyme/s. We isolated Geobacillus stearothermophilus HPA19 from natural resource which produces cocktail of thermo-alkali-stable xylano-pectino-cellulolytic enzyme/s using wheat bran within 24 h.

Cloning, molecular modeling and characterization of acidic cellulase from buffalo rumen and its applicability in saccharification of lignocellulosic biomass.

Cellulase hydrolyses the cellulose by cleaving the β-1,4-linkages to produce mono-, oligo- and shorter polysaccharide units. These enzymes have applications in various industries such as pulp and paper, laundry, food and feed, textile, brewing industry and in biofuel production. In the present study we have cloned acid-cellulase gene (Cel-1) from the fosmid library of buffalo rumen metagenomic DNA and functionally expressed it in Escherichia coli.

Bacterial laccase: recent update on production, properties and industrial applications.

Laccases (benzenediol: oxygen oxidoreductase, EC 1.10.3.

Coproduction of protease and mannanase from Bacillus nealsonii PN-11 in solid state fermentation and their combined application as detergent additives.

Bacillus nealsonii PN-11 produces thermo-alkalistable mannanase and protease active in wide temperature and pH range. Optimization of coproduction of protease and mannanase from this strain and application of cocktail of these enzymes as detergent additives were studied. On optimization mannanase yield of 834Ug (11.

Role of various enzymes for deinking paper: a review.

Paper manufacturing industries depend mainly on forests for wood, which is the basic raw material. Forest plays an important role in balancing the ecosystem to protect forest deinking and bleaching (recycling) of waste paper had gained a lot of importance. Conventional chemical deinking processes require large amount of chemicals which are toxic and hazardous to the environment, hence other effective deinking methods are needed.

Insight into microbial mannosidases: a review.

Mannan is the major constituent of hemicelluloses in softwoods. Mannan hydrolyzing enzymes cleave the 1,4-β-mannopyranosyl linkages of the hetero-1,4-β-d-mannans to yield mannose. β-Mannosidases are mandatory for the complete depolymerization of mannan, these are exo-acting enzymes, which acts on non-reducing end of mannooligomers and on mannobiose removing mannose residues.

Bacterial carrageenases: an overview of production and biotechnological applications.

Carrageenan, one of the phycocolloids is a sulfated galactan made up of linear chains of galactose and 3,6-anhydrogalactose with alternating α-(1 → 3) and β-(1 → 4) linkages and further classified based on the number and the position of sulfated ester(s); κ-, ι- and λ-carrageenan. Enzymes which degrade carrageenans are called k-, ι-, and λ-carrageenases. They all are endohydrolases that cleave the internal β-(1-4) linkages of carrageenans yielding products of the oligo-carrageenans.

Cloning, molecular modeling, and docking analysis of alkali-thermostable β-mannanase from Bacillus nealsonii PN-11.

An alkali-thermostable β-mannanase gene from Bacillus nealsonii PN-11 was cloned by functional screening of E. coli cells transformed with pSMART/HaeIII genomic library. The ORF encoding mannanase consisted of 1100 bp, corresponding to protein of 369 amino acids and has a catalytic domain belonging to glycoside hydrolase family 5.

An extracellular thermo-alkali-stable laccase from Bacillus tequilensis SN4, with a potential to biobleach softwood pulp.

Degradation of residual lignin in kraft pulp by chemical bleaching is implicated in causing environmental pollution. The use of thermo- and alkali-tolerant bacterial laccases is considered to be important biological alternative to chemical processing. Laccases from Bacillus species have shown promise in this respect but their intracellular/spore bound presence make their industrial application economically unfeasible.

A process for reduction in viscosity of coffee extract by enzymatic hydrolysis of mannan.

Mannan is the main polysaccharide component of coffee extract and is responsible for its high viscosity, which in turn negatively affects the technological processing involved in making instant coffee. In our study, we isolated mannan from coffee beans and extract of commercial coffee and it was enzymatically hydrolyzed using alkali-thermostable mannanase obtained from Bacillus nealsonii PN-11. As mannan is found to be more soluble under alkaline conditions, an alkali-thermostable mannanase is well suited for its hydrolysis.

Mannanases: microbial sources, production, properties and potential biotechnological applications.

Mannans are the major constituents of the hemicellulose fraction in softwoods and show widespread distribution in plant tissues. The major mannan-degrading enzymes are β-mannanases, β-mannosidases and β-glucosidases. In addition to these, other enzymes such as α-galactosidases and acetyl mannan esterases, are required to remove the side chain substituents.