Abstract Purpose The textile industry’s previous chemical use resulted in thousands of practical particulate emissions, such as machine component damage and drainage system blockage, both of which have practical implications. Enzyme-based textile processing is cost-effective, environmentally friendly, non-hazardous, and water-saving. The purpose of this review is to give evidence on the potential activity of microbial cellulase in the textile industry, which is mostly confined to the realm of research. Methods This review was progressive by considering peer-reviewed papers linked to microbial cellulase production, and its prospective application for textile industries was appraised and produced to develop this assessment. Articles were divided into two categories based on the results of trustworthy educational journals: methods used to produce the diversity of microorganisms through fermentation processes and such approaches used to produce the diversity of microbes through microbial fermentation. Submerged fermentation (SMF) and solid-state fermentation (SSF) techniques are currently being used to meet industrial demand for microbial cellulase production in the bio textile industry. Results Microbial cellulase is vital for increasing day to day due to its no side effect on the environment and human health becoming increasingly important. In conventional textile processing, the gray cloth was subjected to a series of chemical treatments that involved breaking the dye molecule’s amino group with Cl − , which started and accelerated dye(-resistant) bond cracking. A cellulase enzyme is primarily derived from a variety of microbial species found in various ecological settings as a biotextile/bio-based product technology for future needs in industrial applications. Conclusion Cellulase has been produced for its advantages in cellulose-based textiles, as well as for quality enhancement and fabric maintenance over traditional approaches. Cellulase’s role in the industry was microbial fermentation processes in textile processing which was chosen as an appropriate and environmentally sound solution for a long and healthy lifestyle. 

/pdf/microbial-cellulase-production-and-its-potential-application-36jtzo19.pdf

Microbial cellulase production and its potential application for textile industries

Bromelain is a unique enzyme-based bioactive complex containing a mixture of cysteine proteases specifically found in the stems and fruits of pineapple (Ananas comosus) with a wide range of applications. MD2 pineapple harbors a gene encoding a small bromelain cysteine protease with the size of about 19 kDa, which might possess unique properties compared to the other cysteine protease bromelain. This study aims to determine the expressibility and catalytic properties of small-sized (19 kDa) bromelain from MD2 pineapple (MD2-SBro). Accordingly, the gene encoding MD2-SBro was firstly optimized in its codon profile, synthesized, and inserted into the pGS-21a vector. The insolubly expressed MD2-SBro was then resolubilized and refolded using urea treatment, followed by purification by glutathione S-transferase (GST) affinity chromatography, yielding 14 mg of pure MD2-SBro from 1 L of culture. The specific activity and catalytic efficiency (kcat/Km) of MD2-SBro were 3.56 ± 0.08 U mg−1 and 4.75 ± 0.23 × 10−3 µM−1 s−1, respectively, where optimally active at 50 °C and pH 8.0, and modulated by divalent ions. The MD2-SBro also exhibited the ability to scavenge the 2,2-diphenyl-1-picryl-hydrazyl-hydrate (DPPH) with an IC50 of 0.022 mg mL−1. Altogether, this study provides the production feasibility of active and functional MD2-Bro as a bioactive compound.

/pdf/heterologous-expression-and-catalytic-properties-of-codon-3codhue5.pdf

Heterologous Expression and Catalytic Properties of Codon-Optimized Small-Sized Bromelain from MD2 Pineapple

Abstract The structure of Thermotoga maritima MSB8 pullulanase (PulA) was modified for checking the relationship of domain and site-directed mutagenesis with enzymatic properties. PulA was roughly linked by five domains as CBM41-X-CBM48-catalytic domain-C domain from N-terminal to C-terminal. The deleted certain domains mutants as PulA1 (deleted CBM41) and PulA2 (deleted CBM41-X) were survived with different properties, whereas the PulA3 (deleted CBM41-X-CBM48) and PulA4 (deleted C domain) lose their enzyme activities. The apparent melting temperatures (T m app ) measured by differential scanning fluorimetry of PulA, PulA1 and PulA2 were 76.5 o C, 78.8 o C and 66.6 o C, respectively. The thermal stability of PulA1 was increased slightly but PulA2 was reduced significantly, which shows that the existence of X domain may play a positive role for stability of PulA. To investigate the interaction of CBM48 with X domain, a few site-directed mutants as M1 (E172G), M2 (E172G/R190G), M3 (E172G/D198G), M4 (E172G/R190G/D198G) on the surface of X domain were constructed to reduce the hydrogen bond between X domain with CBM48. The optimum temperature of those four mutants and PulA were 90 o C. The T m app values of M1, M2, M3, and M4 were 77.4 o C, 71.7 o C, 73.2 o C and 71.9 o C, respectively. The specific activity of M1 and M2 were increased slightly, while the pH stability of M3 and M4 were significantly improved at low pH. This study provides the information of the structure-function relationship of pullulanase. 

/pdf/domain-analysis-and-site-directed-mutagenesis-of-a-20ygp7lr.pdf

Domain analysis and site-directed mutagenesis of a thermophilic pullulanase from Thermotoga maritima MSB8

This study is aimed at isolating and identifying a thermophilic cellulolytic bacterium from hot spring water and characterizing thermostable cellulase produced by the isolate. Enrichment and culture of water sample was used for isolation of bacterial strains and an isolate with highest cellulase activity was chosen for the production, partial purification, and biochemical characterization of the enzyme. Different staining techniques, enzymatic tests, and 16s ribosomal DNA (16s rDNA) gene sequencing were used for the identification of the isolate. The cellulase producing isolate was Gram positive, motile, and sporulated rod-shaped bacterium growing optimally between 55°C and 65°C. Based on partial 16s rDNA sequence analysis, the isolate was identified as Geobacillus sp. and was designated as Geobacillus sp. KP43. The cellulase enzyme production condition was optimized, and the product was partially purified and biochemically characterized. Optimum cellulase production was observed in 1% carboxymethyl cellulose (CMC) at 55°C. The molecular weight of the enzyme was found to be approximately 66 kDa on 12% SDS-PAGE analysis. Biochemical characterization of partially purified enzyme revealed the temperature optimum of 70°C and activity over a wide pH range. Further, cellulase activity was markedly stimulated by metal ion Fe2+. Apart from cellulases, the isolate also depicted good xylanase, cellobiase, and amylase activities. Thermophilic growth with a variety of extracellular enzyme activities at elevated temperature as well as in a wide pH range showed that the isolated bacteria, Geobacillus sp. KP43, can withstand the harsh environmental condition, which makes this organism suitable for enzyme production for various biotechnological and industrial applications.

/pdf/production-optimization-and-biochemical-characterization-of-1pui20ru.pdf

Production Optimization and Biochemical Characterization of Cellulase from Geobacillus sp. KP43 Isolated from Hot Spring Water of Nepal

Being the largest and most diverse class of enzymes, hydrolases offer an opportunity to explore the conformational diversity which forms the basis of their differential biological functions. In recent times, there is an urge to re-evaluate and update our existing knowledge on functional and conformational transitions of these enzymes, in the context of emerging scientific trends. In this chapter, we discuss hydrolases in terms of their diversity, classification, and different nomenclature styles that exist. Further, the concepts of protein stability and significance of studying the structure–function relationship of hydrolases are mentioned in detail taking serine protease as an example. The chapter talks about multiple ways by which an enzyme’s structure and function can be explored. The available information and literature survey on hydrolases have been systematically summarized for an easy understanding. Various experimental methods and techniques involving artificial intelligence are introduced in the later sections. The knowledge obtained by these strategies contributes to our current knowledge of the interplay between the stability, structure, and function of these enzymes. This, in turn, can help in designing and engineering these proteins with improved functional and structural features toward the goal of increasing their applicability in biotechnology.

Hydrolases: The most Diverse Class of Enzymes

Heterologous expression and characterization of glycoside hydrolase with its potential applications in hyperthermic environment

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Heterologous expression and characterization of glycoside hydrolase with its potential applications in hyperthermic environment