Tasmia Saman

Bio: Tasmia Saman is an academic researcher from University of Sargodha. The author has contributed to research in topics: Pectinase & Schizophyllum commune. The author has an hindex of 3, co-authored 3 publications receiving 39 citations.

Pectinase Production from Schizophyllum commune Through Central Composite Design Using Citrus Waste and Its Immobilization for Industrial Exploitation

Abstract: Pectinase is an important group of industrial enzymes. Pectinase manufacturing occupies about 10% of the overall enzyme production world over. The aim of this study is to produce pectin lyase from Schizophyllum commune using the mosambi (sweet lime) fruit peels as substrate in solid state fermentation. The cultural parameters optimized through response surface methodology showed maximum pectin lyase production of 480.45 U/mL at initial medium pH of 6, incubation temperature of 35 °C, time period of 1 day, substrate concentration of 15 g and 3 mL of inoculum size. A purification fold of 3.08 with 355 U/mg specific activity and 4.16% yield was obtained after purification. Enzyme immobilization was done by entrapment with sodium alginate and adsorption with chitosan. Chitosan immobilized enzyme exhibited best thermal stability in the range of 45–55 °C and pH 8.0–9.0. Enzyme activity was stimulated in the presence of Ca2+ and Mg2+ while EDTA inhibited the enzyme activity. Chitosan immobilized pectin lyase was stable up to six cycles of reuse. The pH and thermal stability of S. commune pectin lyase makes it an important enzyme for industrial use. The results showed that pectin lyase produced from S. commune has significant potential for applications in the detergent and fruit juice industry. The enzyme produced from citrus agro waste via the proposed optimized biotechnological process can be explored for multiple industrial applications.

Protease Production from Cheotomium globusum Through Central Composite Design Using Agricultural Wastes and Its Immobilization for Industrial Exploitation

Abstract: Proteases are major group of industrial enzymes and account for approximately 60% of overall enzyme market and about 40% sale is reported total worldwide enzymes. In the present study, protease was isolated from Cheotomium globusum, then statistically optimized, characterized, purified and finally immobilized. Cheotomium globusum gave maximum yield (520.16 ± 1.6 U/mL) when grown on Vachellia nilotic (Kikar) while, the physical and nutritional parameters was optimized by Response Surface Methodology (RSM). The maximum protease activity (767.496 ± 3.5 U/mL) was achieved at pH 8, temperature 45 °C, time period 1 day, 5 mL of substrate and 5 mL inoculum size. A purification fold of 3.48 was achieved along with 321 U/mg specific activities while 4.5% yield was obtained after purification. The CHI-immobilized protease showed the stability in the alkaline pH range of 8–9 at 60 °C. Moreover, the CHI-immobilized protease showed significant stability up to 8 cycles of reuse. The pH and temperature stability of novel protease including its reusability makes it a very significant for commercial use. In conclusion, the protease produced from lignocellulosic substrates by Cheotomium globusum through SSF showed its potential in feathers degradation and Gelatin layer decomposition from X-ray film and detergent industry. The enzyme produced from lignocellulosic agro waste via the proposed optimized biotechnological process can be explored for multiple industrial applications.

Protease—A Versatile and Ecofriendly Biocatalyst with Multi-Industrial Applications: An Updated Review

Abstract: Proteases are important industrial biocatalysts that constitute the largest group of enzymes acting as proteinases, peptidases, and amidases with a broad range of industrial applications. In this review, particular attention has been given to comprehensively scrutinize the proteases. After the succinct introduction, classification of proteases as exopeptidases (amino and carboxy proteases) and endopeptidases (serine, aspartic, cysteine, and metalloproteases), sources of alkaline, acidic and neutral protease like animal, plant and microbial sources along with the multi-industrial applications have been dissertated. Now a day’s, mostly proteases, which are present in the market, are produced from microbial sources because of the fast production rate and the limited requirement of cultivation. In addition to this, a critique on the applications of proteases in food, detergent, leather, pharmaceutical, cosmetics, silk degumming, silver recovery, chemical industry, and wastewater treatment industries is also concisely addressed. Finally, protein engineering and immobilization strategies to improve the catalytic properties of protease are thoroughly vetted. The quest for novel sources of protease enzyme has been encouraged to fulfill their ever-increasing demands for industrial exploitation.

Biochemical Prospects of Various Microbial Pectinase and Pectin: An Approachable Concept in Pharmaceutical Bioprocessing.

Abstract: Both pectin and pectinase are vitally imperative biomolecules in the biotechnological sector. These molecules are a feasible non-toxic contrivance of nature with extensive applicative perception. Understanding pectic substances and their structure, unique depolymerization, and biochemical properties such as a catalytic mechanism and the strong interrelationship among these molecules could immensely enhance their applicability in industries. For instance, gaining knowledge with respect to the versatile molecular heterogeneity of the compounds could be considered as the center of concern to resolve the industrial issues from multiple aspects. In the present review, an effort has been made to orchestrate the fundamental information related to structure, depolymerization characteristics, and classification of pectin as well as the types and biochemical properties of pectinase. Furthermore, various production methods related to the optimization of the product and its significant contribution to the pharmaceutical industry (either pectinase or derived pectic substances) are described in this article.

Advances in upstream and downstream strategies of pectinase bioprocessing: A review.

Abstract: This review aims to highlight the bioprocessing strategies behind one of the most commercially produced enzymes in the biotechnological market, pectinase Significant steps in the upstream processing of this enzyme include its source, the selection of the substrate, the reaction conditions and the overall reactor design, all of which will be discussed in great detail Past literature which has contributed to the viability of this design will be highlighted with the intention of generating a comparative review that accounts not only for the contributions of previous research but also for what needs to be done in the future to further increase the productivity of this vital industrial process There is an incredibly wide net of application based research and industry which currently depends on the bioprocessing of pectinase, these will thereby benefit greatly from the concepts of process intensification and optimisation which are at the forefront of this review and will likely be inspired by the outlined steps that need to be taken to further improve this process

Biopolymers and nanostructured materials to develop pectinases-based immobilized nano-biocatalytic systems for biotechnological applications.

Abstract: Pectinases are the emerging enzymes of the biotechnology industry with a 25% share in the worldwide food and beverage enzyme market. These are green and eco-friendly tools of nature and hold a prominent place among the commercially produced enzymes. Pectinases exhibit applications in various industrial bioprocesses, such as clarification of fruit juices and wine, degumming, and retting of plant fibers, extraction of antioxidants and oil, fermentation of tea/coffee, wastewater remediation, modification of pectin-laden agro-industrial waste materials for high-value products biosynthesis, manufacture of cellulose fibres, scouring, bleaching, and size reduction of fabric, cellulosic biomass pretreatment for bioethanol production, etc. Nevertheless, like other enzymes, pectinases also face the challenges of low operational stability, recoverability, and recyclability. To address the above-mentioned problems, enzyme immobilization has become an eminently promising approach to improve their thermal stability and catalytic characteristics. Immobilization facilitates easy recovery and recycling of the biocatalysts multiple times, leading to enhanced performance and commercial feasibility.In this review, we illustrate recent developments on the immobilization of pectinolytic enzymes using polymers and nanostructured materials-based carrier supports to constitute novel biocatalytic systems for industrial exploitability. The first section reviewed the immobilization of pectinases on polymers-based supports (ca-alginate, chitosan, agar-agar, hybrid polymers) as a host matrix to construct robust pectinases-based biocatalytic systems. The second half covers nanostructured supports (nano-silica, magnetic nanostructures, hybrid nanoflowers, dual-responsive polymeric nanocarriers, montmorillonite clay), and cross-linked enzyme aggregates for enzyme immobilization. The biotechnological applications of the resulted immobilized robust pectinases-based biocatalytic systems are also meticulously vetted. Finally, the concluding remarks and future recommendations are also given.

Recent Trends on the Valorization Strategies for the Management of Citrus By-products

Abstract: Citrus is one of the most widely cultivated, processed and consumed fruits throughout the world. A large amount of by-products is generated from citrus processing industries, which causes severe en...