Xylanases are hydrolytic enzymes which cleave the β-1, 4 backbone of the complex plant cell wall polysaccharide xylan. Xylan is the major hemicellulosic constituent found in soft and hard food. It is the next most abundant renewable polysaccharide after cellulose. Xylanases and associated debranching enzymes produced by a variety of microorganisms including bacteria, actinomycetes, yeast and fungi bring hydrolysis of hemicelluloses. Despite thorough knowledge of microbial xylanolytic systems, further studies are required to achieve a complete understanding of the mechanism of xylan degradation by xylanases produced by microorganisms and their promising use in pulp biobleaching. Cellulase-free xylanases are important in pulp biobleaching as alternatives to the use of toxic chlorinated compounds because of the environmental hazards and diseases caused by the release of the adsorbable organic halogens. In this review, we have focused on the studies of structural composition of xylan in plants, their classification, sources of xylanases, extremophilic xylanases, modes of fermentation for the production of xylanases, factors affecting xylanase production, statistical approaches such as Plackett Burman, Response Surface Methodology to enhance xylanase production, purification, characterization, molecular cloning and expression. Besides this, review has focused on the microbial enzyme complex involved in the complete breakdown of xylan and the studies on xylanase regulation and their potential industrial applications with special reference to pulp biobleaching, which is directly related to increasing pulp brightness and reduction in environmental pollution.

P-solubilizing bacterial isolate CB7 isolated from apple rhizosphere soil of Himachal Pradesh, India was identified as Bacillus circulans on the basis of phenotypic characteristics, biochemical tests, fatty acid methyl esters analysis, and 16S rRNA gene sequence. The isolate exhibited plant growth-promoting traits of P-solubilization, auxin, 1-aminocyclopropane-1-carboxylate deaminase activity, siderophore, nitrogenase activity, and antagonistic activity against Dematophora necatrix. In vitro studies revealed that P-solubilization and other plant growth-promoting traits were dependent on the presence of glucose in PVK medium and removal of yeast extract had no significant effect on plant growth-promoting traits. Plant growth-promoting traits of isolate CB7 were repressed in the presence of KH2 PO4 . P-solubilization activity was associated with the release of organic acids and a drop in the pH of the Pikovskaya's medium. HPLC analysis detected gluconic and citric acid as major organic acids in the course of P-solubilization. Remarkable increase was observed in seed germination (22.32%), shoot length (15.91%), root length (25.10%), shoot dry weight (52.92%) and root dry weight (31.4%), nitrogen (18.75%), potassium (57.69%), and phosphorus (22.22%) content of shoot biomass over control. These results demonstrate that isolate CB7 has the promising PGPR attributes to be developed as a biofertilizer to enhance soil fertility and promote plant growth.

Alkalophilic Cellulosimicrobium cellulans CKMX1 isolated from mushroom compost is first report on actinomycetes that has the ability to produce thermostable cellulase-free xylanase, which is an important industrial enzyme used in the pulp and paper industry. Strain CKMX1 was characterized by metabolic fingerprinting, whole-cell fatty acids methyl ester analysis and 16Sr DNA and found to be C. cellulans CKMX1.The enzyme was purified by gel permeation and anion exchange chromatography and had a molecular mass of 29 kDa. Xylanase activity was optimum at pH 8.0 and 55 °C. The enzyme was somewhat thermostable, retaining 50 % of the original activity after incubation at 50 °C for 30 min. The xylanase had K m and V max values of 2.64 mg/ml and 2,000 µmol/min/mg protein in oat spelt xylan, respectively. All metal ions except HgCl2, CoCl2 as well as CdCl2 were well tolerated and did not adversely affect xylanase activity. The deduced internal amino acid sequence of C. cellulans CKMX1 xylanase by matrix assisted laser desorption ionization-time of flight mass spectrometry resembled the sequence of β-1,4-endoxylanase, which is a member of glycoside hydrolase family 11. Some of the novel characteristics that make this enzyme potentially effective in xylan biodegradation could be useful for pulp and paper biobleaching are discussed in this manuscript.

Proteases are ubiquitous enzymes, having significant physiological roles in both synthesis and degradation. The use of microbial proteases in food fermentation is an age-old process, which is today being successfully employed in other industries with the advent of ‘omics’ era and innovations in genetic and protein engineering approaches. Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics. With the rising demands and applications, researchers are exploring various approaches to discover, redesign, or artificially synthesize enzymes with better applicability in the industrial processes. These enzymes offer a sustainable and environmentally safer option, besides possessing economic and commercial value. Various bacterial and fungal proteases are already holding a commercially pivotal role in the industry. The current review summarizes the characteristics and types of proteases, microbial source, their current and prospective applications in various industries, and future challenges. Promoting these biocatalysts will prove significant in betterment of the modern world.

A thermostable extracellular alkaline protease producing Bacillus amyloliquefaciens SP1 was isolated from apple rhizosphere having multifarious plant growth promoting activities. Strain SP1 was purified to 6.48-fold using four-step purification protocol and characterized in detail for its robustness and ecofriendly application in leather and detergent industries. Structural analysis revealed that the protease was monomeric and had a molecular weight of 43 kDa. It exhibited optimum activity at 60°C in alkaline environment (pH 8.0) and stable in the presence of surfactants and oxidizing agents. Enzyme was thermostable at 50°C and retained more than 70% activity after 30 min incubation. It has shown stain removal property and dehairing of goat skin without chemical assistance and hydrolyzing fibrous proteins. This protease showed Km of 0.125 mg ml(-1) and V(max) of 12820 μg ml(-1) indicating its excellent affinity and catalytic role. Thermal inactivation of the pure enzyme followed first-order kinetics. The half life of the pure enzyme at 50, 60, and 65°C was 77, 19.80, and 13.33 min, respectively. The activation energy was 37.19 KJ mol(-1). The results suggest that the B. amyloliquefaciens SP1 has a potential application in different industries.