editorial microbial enzymes and their applications in...

Hindawi Publishing CorporationBioMed Research InternationalVolume 2013, Article ID 204014, 2 pageshttp://dx.doi.org/10.1155/2013/204014

EditorialMicrobial Enzymes and Their Applications inIndustries and Medicine

Periasamy Anbu,1 Subash C. B. Gopinath,2

Arzu Coleri Cihan,3 and Bidur Prasad Chaulagain4

1 Department of Biological Engineering, Inha University, Incheon 402-751, Republic of Korea2Nanoelectronics Research Institute, National Institute of Advanced Industrial Science and Technology,1-1 Higashi, Tsukuba, Ibaraki 305-8562, Japan

3Department of Biology, Faculty of Science, Ankara University, Tandogan, Ankara 06100, Turkey4Department of Plant Biology and Biotechnology, University of Copenhagen, Copenhagen, Denmark

Correspondence should be addressed to Periasamy Anbu; [email protected]

Received 23 October 2013; Accepted 23 October 2013

Copyright © 2013 Periasamy Anbu et al.This is an open access article distributed under theCreativeCommonsAttribution License,which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Enzymes are considered as a potential biocatalyst for a largenumber of reactions. Particularly, the microbial enzymeshave widespread uses in industries and medicine. Themicrobial enzymes are also more active and stable thanplant and animal enzymes. In addition, the microorganismsrepresent an alternative source of enzymes because they canbe cultured in large quantities in a short time by fermentationand owing to their biochemical diversity and susceptibility togene manipulation. Industries are looking for new microbialstrains in order to produce different enzymes to fulfil thecurrent enzyme requirements. This special issue covers tenarticles including three review articles, mainly highlightingthe importance and applications of biotechnologically andindustrially valuable microbial enzymes.

M. Dinarvand et al. in their paper optimized the condi-tions for overproduction of intraextracellular inulinase andinvertase from the fungus Aspergillus niger ATCC 20611.Optimization is one of the most important criteria in devel-oping any new microbial process. Response surface analysisis one of the vital tools to determine the optimal processconditions. This kind of design of a limited set of variablesis advantageous compared to the conventional method. Theresponse surfacemethodology was used for this optimizationand achieved the increment until 16 times. This study wouldbe highly useful for the potential application in fermentationindustries.

In this review, N. Gurung et al. have made an attempt tohighlight the importance of different enzymes with a special

focus on amylase and lipase. Enzymes generally increasethe reaction rates by several million times than normalchemical reactions. Lipases play an important role in thefood, detergent, chemical, and pharmaceutical industries. Inthe past, microbial lipases gained significant attention in theindustries due to their substrate specificity and stability undervaried conditions. Amylase is an enzyme that catalyses thebreakdown of starch into sugars, abundant in the processof animal and human digestion. The major advantage ofmicrobial amylases is being economical and easy to manip-ulate. Currently, much attention is paid to rapid developmentof microbial enzyme technology, and these enzymes arerelatively more stable than the enzymes derived from plantsand animals.

P. Mukherjee and P. Roy in their paper have purified andcharacterized the enzyme hydrocarbon dioxygenase fromStenotrophomonas maltophilia PM102, which has a broadsubstrate specificity. They found that the presence of copperinduces the enzyme activity to be 10.3-fold higher, andNADHinduces the increment to be 14.96-fold. Proposed copperenhanced monooxygenase activity and Fourier transform-infrared (FT-IR) characterization of biotransformation prod-ucts from trichloroethylene satisfy the production of indus-trially and medically important chemicals and make biore-mediation more attractive by improving the development ofthis technology.

C. Huynen et al. in their review paper discuss theimportance of protein scaffold to develop hybrid enzymes.

2 BioMed Research International

The paper discusses the use of class A betalactamase asversatile scaffolds to design hybrid enzymes mentioned asbetalactamase hybrid proteins (BHPs), in which an externalpolypeptide, peptide, protein, or their fragment is inserted atvarious suitable positions. The paper highlights further howBHPs can be specifically designed to develop as bifunctionalproteins to produce and characterize the proteins otherwisedifficult to express, to determine the epitope of specific anti-bodies, to generate antibodies against nonimmunogenic epi-topes, and to understand the structure/function relationshipof proteins. The hybrid proteins can be applied to producedifficult-to-express peptides/proteins/protein fragments, tomap epitopes, to display antigens, and to study proteinstructure/function relationships. Among other applications,BHPs could be an important player in biosensors and inaffinity chromatography, drug screening, and drug targeting.

P. Manivasagan et al. in their paper focus on purificationand characterization of the protease from Streptomyces sp.MAB18. The authors have optimized the conditions for over-production of protease using response surface methodology.They have also determined the molecular mass of purifiedenzyme and great activity and stability of enzyme in differentpH and temperatures. Furthermore, the authors confirmedthat the protease has an antioxidant ability. In industries, thepoultry waste derived protease will be useful as a protein oras an antioxidant.

The paper titled “𝛽-Glucosidases from the fungus Tricho-derma: an effeicient cellulose machinery in biotechnologicalapplications” is a detailed review on 𝛽-glucosidases whichare members of the cellulose enzyme complex describedby P. Tiwari et al. The authors especially focus on 𝛽-glucosidases from the fungus Trichoderma, mostly used forthe saccharification of cellulosic biomass for biofuel produc-tion. They describe the enzyme family, their classification,structural parameters, properties, and studies at the genomicsand proteomics levels. In addition, by bypassing the lowenzyme production with hypersecretory strains, they give aninsight on using these strains for renewable energy sourceslike bioethanol production. They imply the importance offungal 𝛽-glucosidases which might be successful for biofuelproduction in order to meet the need in energy crisis.

A. Khoramnia et al. in their paper discuss yeast enzymeapplication for medium chain fatty acids (MCFAs) modifi-cation for industrial purpose and antibacterial applications.The paper focuses on the conceptualization, design, andassay of the enzyme produced from a Malaysian strain ofGeotrichum candidum. With the modification on fatty acidprocessing using a naturally derived enzyme, a free lauricacid richMCFAs can be obtained which can become a sourceof antibacterial use for both Gram-positive (Staphylococcusaureus) and Gram-negative (E. coli) bacteria which aredifficult microbes due to some of their strains becomingdrug resistant. They also describe that the higher lipolysis bythe strain specific enzyme is associated with the increasedmoisture content in the reaction environment on coconut oilhydrolysis.

M. A. Hassan et al. in their paper discuss isolationof Bacillus amyloliquefaciencs and B. subtilis from soil andproduction and characterization of keratinolytic protease.

These bacteria were able to degrade the wool completelywithin 5 days and also produced the highest enzyme activity.The characterization studies confirmed that the enzyme isstable in a broad range of pH and temperatures. Furthermore,they confirmed that the keratinolytic proteases from isolatedbacteria are stable in various organic solvents.

In this review article, S. C. B. Gopinath et al. put differentstrategies to characterize fungal lipases for their role inindustry and medicine. The advantage of fungal lipases isbestowed with their extracellular nature of production thusreducing the complexities and high operation cost comparingto other bacterial enzymes. The authors provide severalillustrations to show how lipolysis can be utilized and putstrategies for the characterization of fungal lipases that arecapable of degrading fatty substances from different sources,with an effort to highlight further applications. This reviewwould contribute to the isolation and characterization oflipase from various fungal sources and application of lipasefor medical and dairy industry and degradation of fattysubstance from oil spillages.

A. Knob et al. in their paper focus on xylanses anddiscuss the purification and characterization of a xylanaseproduced by Penicillium glabrum using brewer’s spent grainas a substrate in their paper. This study is the first report asthe characterization of xylanase was carried out by using suchan agroindustrial waste. Furthermore, the researchers alsodetermined the molecular mass of the purified xylanase, theenzyme activity and stability on various pH and temperatureranges, the optimal enzyme production conditions, and theeffect of some metal ions and inhibitors on xylanase activity.The authors concluded that the use of substrate brewer’s spentgrain for xylanase production not only decreased the amountof this waste but also reduced the xylanase production cost asdesired in biotechnological processes.

Periasamy AnbuSubash C. B. Gopinath

Arzu Coleri CihanBidur Prasad Chaulagain

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