Kinetic Analysis of Crude Enzyme Extract Produced Via Solid State Fermentation of Banana Pseudo Stem Waste

Mapping Intimacies ◽

10.21203/rs.3.rs-773292/v1 ◽

2021 ◽

Author(s):

Mira Chares Subash ◽

Muthiah Perumalsamy

Keyword(s):

Solid State ◽

Solid State Fermentation ◽

Crude Enzyme ◽

Enzyme Extract ◽

Waste Biomass ◽

Textile Processing ◽

Banana Fiber ◽

Crude Enzyme Extract ◽

Banana Fibers ◽

Pectinase Enzyme

Abstract Banana Pseudo stem waste after each harvest contributes about 70–80 Milli Tons Per hector. The banana pseudo stem will be thrown as waste biomass after each harvest as it is unstable for the upcoming harvest. The biggest challenge in banana cultivation is the utilization of biomass of banana pseusostem waste into valuable products. In this study, Xylano-pectinase enzyme extract was produced from banana pseudo stem waste under solid-state fermentation by Enterobacter cloacae PMC04. The highest pectinase and xylanase activities obtained using banana pseudo stem as carbon source were 124.62 U/ml and 173.81 U/ml respectively. Thermodynamics stated that range 40-50oC were considered to be the optimal temperature for xylano-pectinase enzyme production and subsequent degumming of banana fibers. The crude enzyme extract were then used in the degumming of banana fibers for textile application. Textile processing of banana fiber necessitates the removal of hemicellulose substance which can be achieved by crude xylano-pectinase enzyme. It was found that crude xylano-pectinase was efficient in the removal of hemicellulose substance from the fibers. Results obtained from this study demonstrate that the proposed bioprocess could be successfully applied for the degumming of banana fibers sustainably.

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Kinetic Analysis of a Crude Enzyme Extract Produced via Solid State Fermentation of Bakery Waste

ACS Sustainable Chemistry & Engineering ◽

10.1021/acssuschemeng.5b00323 ◽

2015 ◽

Vol 3 (9) ◽

pp. 2043-2048 ◽

Cited By ~ 32

Author(s):

Wei Han ◽

Wan Chi Lam ◽

Mehmet Melikoglu ◽

Man Tung Wong ◽

Hoi Ting Leung ◽

...

Keyword(s):

Solid State ◽

Kinetic Analysis ◽

Solid State Fermentation ◽

Crude Enzyme ◽

Enzyme Extract ◽

Crude Enzyme Extract

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Valorization of Lignocellulosic Wastes to Produce Phytase and Cellulolytic Enzymes from a -Thermophilic Fungus, Thermoascus aurantiacus SL16W, under Semi-Solid State Fermentation

Journal of Fungi ◽

10.3390/jof7040286 ◽

2021 ◽

Vol 7 (4) ◽

pp. 286

Author(s):

Keerati Tanruean ◽

Watsana Penkhrue ◽

Jaturong Kumla ◽

Nakarin Suwannarach ◽

Saisamorn Lumyong

Keyword(s):

Solid State ◽

Rice Bran ◽

Solid State Fermentation ◽

Reducing Sugar ◽

Crude Enzyme ◽

Enzyme Extract ◽

Thermoascus Aurantiacus ◽

Tea Leaves ◽

Crude Enzyme Extract ◽

Semi Solid

Agricultural wastes are lignocellulosic biomasses that contain high mineral and nutrient contents. This waste can be used as a raw material in industrial enzyme production by microbial fermentation. Phytase is an important enzyme used in animal feed to enhance the amount of phosphorus available for the growth and overall health improvement of monogastric animals. Fungi offer high potential as an effective source in the production of various extracellular enzymes. In this study, the production of lignocellulolytic enzymes (endoglucanase and xylanase) and phytase by a thermophilic fungus, namely Thermoascus aurantiacus strain SL16W, was evaluated using sixteen different Thai agricultural forms of waste under conditions of high temperature (45 °C). Semi-solid state fermentation was used in the production experiments. The results of this study reveal that the highest phytase activity (58.6 U/g substrate) was found in rice bran, whereas the highest degrees of activity of endoglucanase and xylanase were observed in wheat bran and red tea leaves at 19 and 162 U/g substrate, respectively. Consequently, the optimal conditions for phytase production of this fungus using rice bran were investigated. The results indicate that the highest phytase yield (58.6 to 84.1 U/g substrate) was observed in rice bran containing 0.5% ammonium sulfate as a nitrogen source with 10 discs of inoculum size at a cultivation period of 9 days at 45 °C and moisture content of 95%. Notably, the phytase yield increased by 1.71-fold, while endoglucanase and xylanase were also increased by 1.69- and 1.12-fold, respectively. Furthermore, the crude enzyme obtained from the optimal condition was extracted. The crude enzyme extract was then separately added to red tea leaves, rice straw, corncobs, palm residue, and peanut husks. Subsequently, total reducing sugar and phosphorus contents were determined. The results indicate that the highest level of reducing sugar (122.6 mg/L) and phosphorus content (452.6 mg/L) (p < 0.05) were obtained in palm residue at 36 and 48 h, respectively, after the addition of the crude enzyme extract. This study has provided valuable information on a potentially eco-friendly way to valorize agricultural waste into value-added products as industrial enzymes.

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Purification and Characterization of Aspartic Protease Produced from Aspergillus oryzae DRDFS13 under Solid-State Fermentation

10.1101/2020.10.19.346486 ◽

2020 ◽

Author(s):

Jermen Mamo ◽

Jorge Fernando Suarez Orellana ◽

Vikas Yelemane ◽

Martin Kangwa ◽

Hector Marcelo Fernandez-Lahore ◽

...

Keyword(s):

Molecular Weight ◽

Solid State ◽

Ion Exchange ◽

Solid State Fermentation ◽

Aspartic Protease ◽

Crude Enzyme ◽

Crude Enzyme Extract ◽

Standard Methods ◽

Protease Enzyme ◽

Cheese Production

AbstractAspartic proteases (E.C.3.4.23.) are endopeptidases with molecular masses ranging between 30–45 kDa. They depend on aspartic acid residues for their catalytic activity and show maximal activity at low pH. Thus the main objective of the present study was to purify and characterize aspartic protease from locally identified fungi by solid-state fermentation. The aspartic protease in the current study was obtained from A. oryzae DRDFS13 under SSF. The crude enzyme extract was purified by size-exclusion (SEC) and ion-exchange (IEC) chromatography. The protein contents of crude enzyme and IEC fractions were determined by BCA methods while the presence of N-glycosylation was checked using Endo-H. Inhibition studies were conducted using protease inhibitors. The milk-clotting activity (MCA), protease activity (PA); molecular weight and enzyme kinetics were determined using standard methods. Optimum temperature and stability, optimum pH and stability, and the effect of cations on MCA were assessed using standard methods. The maximum MCA (477.11 U/mL) was recorded from IEC fraction A8. The highest specific activity (183.50 U/mg), purification fold (6.20) and yield (9.2%) were also obtained from the same fraction (IEC A8). The molecular weight of 40 kDa was assigned for the purified enzyme (IEC A8). However, its molecular weight was decreased to 30 KDa upon deglycosylation assay which infers that the protein is glycosylated. Incubation of the pure enzyme (IEC A8) with pepstatin A caused a 94 % inhibition on MCA. The dialyzed enzyme showed a Km and Vmax values of 17.50 mM and 1369 U, respectively. The enzyme showed maximum MCA at 60 °C and pH 5.0 with stability at pH 4.5-6.5 and temperature 35-45 °C. Most cat-ions stimulate the activity of the enzyme; moreover, the highest MCA was detected at 50 mM of MnSO4. Furthermore, the results obtained in the present study confirmed that the aspartic protease enzyme produced from A. oryzae DRDFS13 and purified in ion-exchange chromatography could be used as a substitute source of rennet enzyme for cheese production.ImportanceThe production of pure aspartic protease enzyme from local microbes which is useful to substitute shortage of calf rennet enzyme and valuable to diversify cheese production throughout the world.

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