File Name: production of microbial enzymes and their applications .zip
Enzymes are very useful catalysts in many different industrial processes because they perform very specifically, at a particular processing step in the manufacture of a product. The enzymes used in industrial processes also originate from nature, and therefore can be used in the same way as nature does.
- Microbial lipases and their industrial applications: a comprehensive review
- Industrial enzymes
- Microbial Enzymes and Their Applications in Industries and Medicine 2014.
- Microbial Proteases Applications
Due to advancements in recent years, biocatalysis through isolated enzymes is considered more economical than use of whole cells. Enzymes may be used as a unit operation within a process to generate a desired product, or may be the product of interest. Industrial biological catalysis through enzymes has experienced rapid growth in recent years due to their ability to operate at mild conditions, and exceptional chiral and positional specificity, things that traditional chemical processes lack. Whole cells are typically used when a reaction requires a co-factor.
Microbial lipases and their industrial applications: a comprehensive review
The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others.
Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes. Among different producers of proteases, Bacillus sp. Proteases are successfully considered as an alternative to chemicals and an eco-friendly indicator for nature or the surroundings.
The evolutionary relationship among acidic, neutral, and alkaline proteases has been analyzed based on their protein sequences, but there remains a lack of information that regulates the diversity in their specificity. Researchers are looking for microbial proteases as they can tolerate harsh conditions, ways to prevent autoproteolytic activity, stability in optimum pH, and substrate specificity. The current review focuses on the comparison among different proteases and the current problems faced during production and application at the industrial level.
Deciphering these issues would enable us to promote microbial proteases economically and commercially around the world. Proteases are a universal entity that is found everywhere, namely, in plants, animals, and microbes. The peptide bond present in the polypeptide chain of amino acids is hydrolyzed by means of proteases Barrett and McDonald, Proteases are degradative enzymes and show specificity and selectivity in protein modification Rao et al.
In the industrial sector, Bacillus sp. Of the three largest groups of industrial enzymes, proteases are one of them, and their global market is drastically increasing annually. Proteases are an integral component of existing life on earth, such as animals, plants, and microbes. By a process of fermentation, proteases can be isolated and purified in a relatively shorter period of time, exhibiting high substrate specificity and catalytic activity Kumar and Takagi, ; Rifaat et al.
According to researchers, proteases control the activation, synthesis, and turnover of proteins to regulate physiological processes Rawlings et al. Different physiological processes, such as formation, birth, aging, and even death are regulated by proteases Chou et al.
Proteases are vital in the imitation and spread of infectious diseases, and because of their significant role in the life cycle, they are imperative for drug discovery. In more than 50 human proteases, a single amino acid mutation may lead to a hereditary disease Chou et al.
Proteases are involved in normal and pathophysiological processes or conditions. This involvement of proteases may lead them to produce a therapeutic agent against deadly diseases, such as cancer and AIDS Rawlings et al.
The proposed review highlights the proteolysis, function, and wide range of sources among different bacteria of microbial proteases.
It also discusses the broad range of applications and upcoming advancement for the discovery of new and fresh proteases, especially alkaline proteases from bacteria Reddy et al. Proteases have been successfully produced by researchers from different microbial sources. Microbes account a two-thirds share of commercial protease around the globe Beg and Gupta, Since the advent of enzymology, microbial proteolytic proteases have been the most widely studied enzyme.
These enzymes have gained interest not only due to their vital role in metabolic activities but also due to their immense utilization in industries Rao et al. The proteases available in the market are of microbial origin because of their high yield, less time consumption, less space requirement, lofty genetic manipulation, and cost-effectiveness, which have made them suitable for biotechnological application in the market Nisha and Divakaran, ; Ali et al. These microbial proteases are preferred to plant and animal proteases because of the presence of all desired characteristics for industrial applications Palsaniya et al.
Proteolytic enzymes found in microbes and mammalian systems are small in size, dense, and structurally spherical Oberoi et al. Among different producers of alkaline proteases, Bacillus sp. The proteases isolated from these microbial sources have a large number of dilutions in various industrial sectors Pastor et al.
Usually, extracellular alkaline proteases are secreted out from the producer into the liquid broth from where these proteases are simplified and purified through down streaming to produce an end product. Comparatively, proteases produced by plants and animals are more labor-intensive than microbially produced proteases Gupta et al. Proteases produced by microbial sources are classified into groups based on their acidic or basic properties.
They are also classified based on the presence of functional groups and the position of peptide bond Gessesse, ; Panda et al. Microbial proteases are the most commercially exploited enzyme worldwide.
A large number of intracellular proteases are produced by microbes playing a vital role in differentiation, protein turnover, hormone regulation, and cellular protein pool, whereas extracellular proteases are significant in protein hydrolysis Rao et al. Keratins are proteins that are usually present in two forms, namely, hard keratins and soft keratins. Hard keratins mainly include the structural proteins that are prevalently present in fingernails, horns, beaks, upper layer of skin, and mainly hair.
Fibers of the keratin proteins are self-assembled into compact follicles that make up the structure of hair. The process of assembling keratin proteins into a complex hair is under the control of multiple genes, cytokines, and growth factors Charles et al.
In contrast to hard keratins, soft keratins are those that are abundantly present in tissues, such as epithelial tissues. The structure of wool keratin shows great similarity to hair keratin. Three types of hair keratin have been known Cheng et al. The first one is the alpha keratins; these range in size from 60 to 80 kDa. Having low sulfur content, these comprise mainly of alpha-helical domains. Overall, alpha keratins make up the structural class of proteins, as they reside in the fiber cortex of hair.
The second type is the beta keratins, which are a non-extractable, less-studied class of keratins. These are usually present in the hair cuticle and perform protective functions. Their size is comparatively smaller than the other classes of keratin. These keratins help to maintain the cortical superstructure by cross-linking the disulfide bonds in the hair Cheng et al.
All these types of keratins can be degraded by the enzyme keratinase, which belongs to a class of protease enzymes. The enzyme keratinase E. According to UniProt results, one of the protein keratinases produced by Bacillus subtilis contains two domains. The first one is 59 amino acids long and encodes for inhibitor I9; the other one is amino acids long and encodes for peptidase S8.
The first domain occurs from 19 to 77 amino acid sequences and the second domain occurs from to amino acid sequences.
The enzyme also has a metal ion binding site for calcium ion. This means that calcium ions act as cofactors for keratinases; the presence of calcium ions in the media can enhance the activity of keratinases. The structure of keratinase makes it very efficient in its function of degrading keratin proteins Arora and Mishra, ; Moraga et al.
Our daily green waste and animal waste includes plenty of keratins, which remain undegraded due to their complexity. Such insoluble keratins may lead to environmental pollution if left untreated. Thus, as a solution, such wastes are treated by keratinase enzymes, which convert the waste into simpler as well as biodegradable substances Cavello et al. The extracellular keratinases have been successfully isolated from several microbes by using several fermentation techniques and by optimizing conditions, such as pH, temperature, and type of nitrogen and carbon source and the choice of microbe Govinden and Puchooa, ; Lateef et al.
The keratinases from microbes are effective, biodegradable, and economic and provide much better results as compared to chemical treatments Manirujjaman et al. The genus Bacillus is vital for commercially important alkaline protease EC.
These alkaline protease producers are distributed in water, soil, and highly alkaline conditions. From a variety of sources, such as detergent contamination Hsiao et al. The detergent industry consumes alkaline proteases most abundantly, which are serine proteases with an alkaline pH range Gupta et al. These alkaline serine proteases, which are easily inactivated by phenyl methane sulfonyl fluoride PMSF , account for one-third of the share of the enzyme market Page and Di Cera, Alkaline proteases are unique in their activity and maintain a constant alkaline pH while being exploited for different formulations in pharmaceutical, food, and other related industries Banerjee et al.
A broad range of applications of these alkaline proteases are getting more attention from researchers with the hope of discovering new strains with unique properties and substantial activity Najafi et al. It is reported that for dehairing of animal skin and hides, Bacillus sp. These Bacillus strains have been commercially exploited around the globe due to the huge amounts of enzyme secreted with high enzymatic activity Jacobs, ; Ito et al.
Although alkaline proteases are produced by multiple sources Ellaiah et al. Two essential types of alkaline proteases, such as subtilisin Carlsberg and subtilisin novo are obtained from Bacillus sp. In halophilic sources, different microbial sp. The entomopathogenic bacterium Photorhabdus sp. Owing to its broad-spectrum specificity with different proteins and peptides, it is suggested that PhPrtPI provides nutrients to the nematodes by degradation of insect tissues Soroor et al.
A Salinivibrio sp. It is a highly recommended strain due to its thermal and halophilic properties Amoozegar et al. Another strain, Bacillus clausii , is also recommended for use at a commercial scale for the production of alkaline protease with the use of peptone, Cu, and fructose as the sole source of energy. A strain of Bacillus sp. Very rare microbes, such as Kurthia spiroforme are also capable of producing alkaline protease Amoozegar et al.
Different mushrooms producing alkaline protease are also reported Steele et al. Acid proteases are stable and active between pH 3. The optimum pH of acidic proteases is 3—4 and the isoelectric point range is between 3 and 4. Furthermore, acid proteases are also exploited for use in clearing beer and fruit juice, improving texture of flour paste, and tenderizing the fibril muscle Zhang et al. In comparison with alkaline proteases, these extracellular acid proteases are mostly produced by fungal species, such as Aspergillus niger Sielecki et al.
Most of the fungal extracellular acid proteases are known as aspergilla opepsins. Aspartic proteases are acid proteases consisting of — long chains of amino acid residues constituting the active site for catalytic activity.
These acidic proteases are endopeptidases and grouped into three families: pepsin A1 , retropepsin A2 , and enzymes from Para retroviruses A3 Somkuti and Babel, These three families are placed in clan AA. It is found that A1 and A2 are closely related to each other while members of the A3 family show some relatedness to families A1 and A2. An active site cleft of the members of the pepsin family is located between lobes of a bilobal structure Pushpam et al.
The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others. Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes.
Microbial Enzymes and Their Applications in Industries and Medicine 2014.
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Periasamy Anbu, Subash C. Box , Kalanki, Kathmandu, Nepal. Enzymes are biocatalysts that play an important role in metabolic and biochemical reactions [ 1 ]. Microorganisms are the primary source of enzymes, because they are cultured in large quantities in short span of time and genetic manipulations can be done on bacterial cells to enhance the enzyme production [ 2 — 4 ]. In addition, the microbial enzymes have been paid more attention due to their active and stable nature than enzymes from plant and animal [ 2 — 4 ].
В обязанности Мидж как эксперта по обеспечению внутренней безопасности входило наблюдение за всем, что творилось в стенах АНБ… в том числе и в кладовке столовой агентства. Бринкерхофф поднялся со своего места, словно стоя ему было легче защищаться, но Мидж уже выходила из его кабинета. - Руки на стол, - бросила она через плечо.
Microbial Proteases Applications
Ничего не читайте. - Энсей Танкадо… родился в январе… - Пожалуйста, - вежливо сказал Беккер. - Положите на место. Офицер еще какое-то время разглядывал паспорт, потом положил его поверх вороха одежды. - У этого парня была виза третьего класса. По ней он мог жить здесь многие годы. Беккер дотронулся до руки погибшего авторучкой.
Когда я летел домой, - сказал он, желая переменить тему, - я позвонил президенту университета. Сьюзан радостно встрепенулась. - Скажи, что ты ушел с поста декана. Дэвид кивнул. - В следующем семестре я возвращаюсь в аудиторию.
Начинаем отключение резервного питания. Приготовиться. Приступайте. - Мы не успеем! - крикнула Соши.
Только туда ей и оставалось идти в наглухо запертом помещении. Поднявшись по ступенькам, она обнаружила, что дверь в кабинет шефа открыта, поскольку электронный замок без электропитания бесполезен. Она вошла. - Коммандер? - позвала Сьюзан.
- Если не скажешь, тебе меня больше не видать. - Врешь. Она ударила его подушкой. - Рассказывай.
Человек ничего не сказал, задумался на мгновение, а потом обратился к Сьюзан. - Лиланд Фонтейн, - представился он, протягивая руку. - Я рад, что вы живы-здоровы. Сьюзан не отрывала глаз от директора.
Стратмор также понимал, что первым делом нужно разрядить ситуацию. Выдержав паузу, он как бы нехотя вздохнул: - Хорошо, Грег.