scholarly journals An Exochitinase with N-Acetyl-β-Glucosaminidase-Like Activity from Shrimp Head Conversion by Streptomyces speibonae and Its Application in Hydrolyzing β-Chitin Powder to Produce N-Acetyl-d-Glucosamine

Polymers ◽  
2019 ◽  
Vol 11 (10) ◽  
pp. 1600 ◽  
Author(s):  
Thi Ngoc Tran ◽  
Chien Thang Doan ◽  
Minh Trung Nguyen ◽  
Van Bon Nguyen ◽  
Thi Phuong Khanh Vo ◽  
...  
Keyword(s):  
Monomer Unit ◽  
Polyacrylamide Gel Electrophoresis ◽  
Major Product ◽  
Molecular Weight Determination ◽  
Carbon And Nitrogen ◽  
Shrimp Shell ◽  
Shrimp Head ◽  
Higher Temperature ◽  
Shell Powder ◽  
Chitin Powder

Marine chitinous byproducts possess significant applications in many fields. In this research, different kinds of fishery chitin-containing byproducts from shrimp (shrimp head powder (SHP) and demineralized shrimp shell powder), crab (demineralized crab shell powder), as well as squid (squid pen powder) were used to provide both carbon and nitrogen (C/N) nutrients for the production of an exochitinase via Streptomyces speibonae TKU048, a chitinolytic bacterium isolated from Taiwanese soils. S. speibonae TKU048 expressed the highest exochitinase productivity (45.668 U/mL) on 1.5% SHP-containing medium at 37 °C for 2 days. Molecular weight determination analysis basing on polyacrylamide gel electrophoresis revealed the mass of TKU048 exochitinase was approximately 21 kDa. The characterized exochitinase expressed some interesting properties, for example acidic pH optima (pH 3 and pH 5–7) and a higher temperature optimum (60 °C). Furthermore, the main hydrolysis mechanism of TKU048 exochitinase was N-acetyl-β-glucosaminidase-like activity; its most suitable substrate was β-chitin powder. The hydrolysis experiment revealed that TKU048 exochitinase was efficient in the cleavage of β-chitin powder, thereby releasing N-acetyl-d-glucosamine (GlcNAc, monomer unit of chitin structure) as the major product with 0.335 mg/mL of GlcNAc concentration and a yield of 73.64% after 96 h of incubation time. Thus, TKU048 exochitinase may have potential in GlcNAc production due to its N-acetyl-β-glucosaminidase-like activity.

scholarly journals Conversion of Shrimp Head Waste for Production of a Thermotolerant, Detergent-Stable, Alkaline Protease by Paenibacillus sp.

Catalysts ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 798 ◽  
Author(s):  
Chien Thang Doan ◽  
Thi Ngoc Tran ◽  
I-Hong Wen ◽  
Van Bon Nguyen ◽  
Anh Dzung Nguyen ◽  
...  
Keyword(s):  
Alkaline Protease ◽  
Nitrogen Nutrition ◽  
Crab Shell ◽  
Carbon And Nitrogen ◽  
Optimal Activity ◽  
Shrimp Shell ◽  
Paenibacillus Sp ◽  
Shrimp Head ◽  
Ph Range ◽  
By Products

Fishery processing by-products have been of great interest to researchers due to their beneficial applications in many fields. In this study, five types of marine by-products, including demineralized crab shell, demineralized shrimp shell, shrimp head, shrimp shell, and squid pen, provided sources of carbon and nitrogen nutrition by producing a protease from Paenibacillus sp. TKU047. Strain TKU047 demonstrated the highest protease productivity (2.98 U/mL) when cultured for two days on a medium containing 0.5% of shrimp head powder (SHP). The mass of TKU047 protease was determined to be 32 kDa (approximately). TKU047 protease displayed optimal activity at 70–80 °C and pH 9, with a pH range of stability from 6 to 11. TKU047 protease also showed stability in solutions containing surfactants and detergents. Based on its excellent properties, Paenibacillus sp. TKU047 protease may be a feasible candidate for inclusion in laundry detergents.

The chitinolytic enzyme system of the compost-dwelling thermophilic fungus Thermomyces lanuginosus

2014 ◽  
Author(s):  
◽  
Meng Zhang
Keyword(s):  
Enzyme Characterization ◽  
Major Product ◽  
Thermomyces Lanuginosus ◽  
Chitinolytic Enzyme ◽  
Shrimp Shell ◽  
Gene Structures ◽  
Aspergillus Sp ◽  
Chitinase Genes ◽  
Shell Powder ◽  
Recent Sequencing

Chitin, a highly insoluble 1,4- -linked polymer of N-acetyl- -D-glucosamine, is the second-most abundant bio-polysaccharide in nature after cellulose. Most chitinolytic fungi are known to produce more than one kind of chitinase. The recent sequencing of the Thermomyces lanuginosus SSBP genome by our group has revealed four putative family 18 chitinases. In this study, three novel chitinase genes (chitl, chit2 and chit3) and the previously reported chit4 gene were cloned from Thermomyces lanuginosus SSBP and their gene structures were analysed. chit3, encoding a 36.6 kDa protein, and chit4, encoding a 44.1 kDa protein, were successfully expressed in Pichia pastoris. The recombinant Chit3 and Chit4 enzymes exhibited optimum activity at pH 4.0 and 5.0 and at 40oC and 50°C, respectively. Chit3 was stable at 40oC and retained 71% of its activity at 50°C after 60 min, while Chit4 was stable at 50°C and retained 56% of its activity at 60°C after 30 min. Both enzymes produced chitobiose as the major product using colloidal chitin, chitooligosaccharides and shrimp shell powder as substrates. Of the fungal strains tested, Chit3 displayed antifungal activity against Penicillium sp. and Aspergillus sp. This is the first report on the multi-chitinolytic system of T. lanuginosus and enzyme characterization has shown the potential of the enzymes to be used in degradation of the under-utilized bio-resource chitin.

Optimization for Extraction of Astaxanthin from Shrimp Shell Using Response Surface Method

2011 ◽  
Vol 396-398 ◽  
pp. 609-613
Author(s):  
Hong Chao Liu ◽  
Peng Li ◽  
Guang Wang ◽  
He Ping Yu ◽  
Zong Qiang Zeng ◽  
...  
Keyword(s):  
Sodium Hydroxide ◽  
Response Surface ◽  
Organic Solvents ◽  
Response Surface Method ◽  
Extraction Method ◽  
Alkali Solution ◽  
Surface Method ◽  
Shrimp Shell ◽  
Shrimp Head ◽  
Bioactive Substance

In this work, the extraction of astaxanthin i.e. bioactive substance in the shrimp head and shell was studied. The extraction method of astaxanthin was established: the alkali method and organic solvents method were combined to extract astaxanthin, the solvent of the alkali solution was ethanol:water =4:1, dichloromethane was selected as the extractant. The best extraction conditions for astaxanthin were optimized: the concentration of sodium hydroxide was 1.4mol / L, the optimum extaction process was at 54°C for 24 h, and the ration of solid to liquid was 8:1. In this condition, the absorption value of astaxanthin was 1.2048, the concentration of astaxanthin was 3.26μg/mL, which was equivalent to 32.6 μg/g dry shrimp shell.

scholarly journals Pig liver pyruvate carboxylase. Purification, properties and cation specificity

1974 ◽  
Vol 139 (2) ◽  
pp. 297-310 ◽  
Author(s):  
Graham B. Warren ◽  
Keith F. Tipton
Keyword(s):  
Pyruvate Carboxylase ◽  
Monomer Unit ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Liver Mitochondria ◽  
Univalent Cations ◽  
Acetyl Coa ◽  
Pig Liver ◽  
Apparent Homogeneity ◽  
Polypeptide Chains

1. Pyruvate carboxylase was purified to apparent homogeneity from pig liver mitochondria and shown to be free of all kinetically contaminating enzymes. 2. The enzyme has a mol. wt. of 520000 and is composed of four subunits, each with a mol. wt. of 130000. 3. The enzyme can exist as the active tetramer, dimer and monomer, although the tetramer appears to be the form in which the enzyme is normally assayed. 4. For every 520000g of the enzyme there are 4mol of biotin, 3mol of zinc and 1mol of magnesium. No significant concentrations of manganese were detected. 5. Analysis by sodium dodecyl sulphate–polyacrylamide gel electrophoresis indicates three polypeptide chains per monomer unit, each with a mol. wt. of 47000. 6. The amino acid analysis, stoicheiometry of the reaction and the activity of the enzyme as a function of pH are also presented. 7. The enzyme is activated by a variety of univalent cations but not by Tris+ or triethanolamine+. 8. The activity of the enzyme is dependent on the presence of acetyl-CoA; the low rate in the absence of added acetyl-CoA is not due to an enzyme-bound acyl-CoA. The dissociation constant for enzyme-bound acetyl-CoA is a marked function of pH.

scholarly journals Microbial Conversion of Shrimp Heads to Proteases and Chitin as an Effective Dye Adsorbent

Polymers ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 2228 ◽  
Author(s):  
Chien Thang Doan ◽  
Thi Ngoc Tran ◽  
Chuan-Lu Wang ◽  
San-Lang Wang
Keyword(s):  
Culture Media ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protease Production ◽  
Adsorptive Capacity ◽  
Microbial Conversion ◽  
N Nutrition ◽  
Chitin Extraction ◽  
Electrophoresis Method ◽  
Shrimp Head ◽  
Shrimp Heads

As a green and effective technique in the production of a large number of valuable products, the microbial conversion of chitinous fishery wastes is receiving much attention. In this study, protease production using the Paenibacillus mucilaginosus TKU032 strain was conducted on culture media containing several common types of chitinous fishery by-products serving as the carbon and nitrogen (C/N) nutrition source. Among the chitinous wastes, 1.5% (w/v) shrimp head powder (SHP) was found to be the most appropriate nutritional source for protease production when a maximal enzyme activity of 3.14 ± 0.1 U/mL was observed on the 3rd day of the culture period. The molecular mass of P. mucilaginosus TKU032 protease was estimated to be nearly 32 kDa by the polyacrylamide gel electrophoresis method. The residual SHP obtained from the culture medium was also considered to be utilized for chitin extraction. The deproteinization rate of the fermentation was estimated to be 45%, and the chitin obtained from fermented SHP (fSHP) displayed a similar characteristic Fourier-transform infrared spectroscopy (FTIR) profile as that from SHP. In addition, SHP, fSHP, and chitins obtained from SHP and fSHP were investigated for their adsorptive capacity of nine types of dyes, and chitin obtained from fSHP displayed a good adsorption rate on Congo Red and Red No. 7, at 99% and 97%, respectively. In short, the results provide potential support for the utilization of SHP in the production of P. mucilaginosus TKU032 protease via the fermentation as well as the preparation of chitin from fSHP as an effective dye adsorbent.

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