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

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.

Author(s):  
Douglas R. Keene ◽  
Gregory P. Lunstrum ◽  
Patricia Rousselle ◽  
Robert E. Burgeson

A mouse monoclonal antibody produced from collagenase digests of human amnion was used by LM and TEM to study the distribution and ultrastructural features of an antigen present in epithelial tissues and in cultured human keratinocytes, and by immunoaffinity chromatography to partially purify the antigen from keratinocyte cell culture media.By immunofluorescence microscopy, the antigen displays a tissue distribution similar to type VII collagen; positive staining of the epithelial basement membrane is seen in skin, oral mucosa, trachea, esophagus, cornea, amnion and lung. Images from rotary shadowed preparations isolated by affinity chromatography demonstrate a population of rod-like molecules 107 nm in length, having pronounced globular domains at each end. Polyacrylamide gel electrophoresis suggests that the size of this molecule is approximately 440kDa, and that it is composed of three nonidentical chains disulfide bonded together.


1981 ◽  
Vol 197 (1) ◽  
pp. 105-109 ◽  
Author(s):  
D R Thatcher ◽  
B Hodson

A polyacrylamide-gel-electrophoresis method has been developed that permits the analysis of conformational changes that occur during the thermal denaturation of macromolecules. A stable transverse temperature gradient was produced in an aluminium heating jacket clamped around a vertical polyacrylamide slab gel. After temperature equilibration, gels were loaded with either a layer of protein solution (20-200 micrograms/gel) or a solution of double-stranded DNA (20 micrograms/gel) and electrophoresis begun. At the end of the run the gels were stained and the effect of temperature on mobility observed. The technique proved informative both for the irreversible unfolding of proteins (Drosophila alcohol dehydrogenase and lactic acid dehydrogenase) and for a protein that was reversibly denatured by heat (beta-lactamase). In the latter case a clear transition between the native enzyme and a slower-migrating denatured state was observed. The patterns obtained were analogous to the type produced by the transverse-urea-gradient-electrophoretic method of Creighton [(1979) J. Mol. Biol. 129, 253-264]. The method also resolved a complex mixture of double-stranded-DNA restriction-digest fragments.


2014 ◽  
Vol 989-994 ◽  
pp. 1020-1024
Author(s):  
Nan Nan ◽  
Xi Jing Liu

Radix Isatidis is a traditional Chinese medicine for treatment of influenza and inflammation in China. In this paper, in order to study the degradation situation of Radix Isatidis polypeptide in artificial gastrointestinal environment, the SDS-PAGE (Sodium dodecyl sulfate-polyacrylamide gel electrophoresis) method was used to detect the degradation of Radix Isatidis polypeptide in artificial intestinal juice and gastric juice, and it showed that Radix Isatidis peptides could be degradated to different degrees. HPLC (High Performance Liquid Chromatography) was used to determine the change of peptides degradation, and it indicated that free amino acid levels did not change significantly. The result after degradation was also detected by BCA method, and it showed that there were still a large number of polypeptides in the liquid. From this experiment we can come to this conclusion that Radix Isatidis polypeptides in artificial gastrointestinal juice mostly degraded into a series of different molecular weight peptides.


Author(s):  
Hazriani Ra ◽  
Lisa Amir ◽  
Ratna Farida

Objectives: The objective of this study is to evaluate the effect of HPLs with no additional GFs on the HUVEC protein profile. Methods: HUVEC cultures were examined in groups as follows: Fetal bovine serum (FBS), 2%-HPL with a GF, and 2%- and 5%-HPL without a GF which were analyzed with a sodium dodecyl sulfate-polyacrylamide gel electrophoresis test. Results: The intensity, thickness, and molecular weight of HUVEC band proteins cultured without a GF were not significantly different compared to the control groups (FBS or HPL with a GF). Conclusions: No difference was found in the HUVEC protein profile after they were cultured with FBS and HPLs, with or without GFs.


2014 ◽  
Vol 1073-1076 ◽  
pp. 314-318
Author(s):  
Xiao Jing Li ◽  
Yun Zhe Ji ◽  
Xiao Jie Wang

Steroid microbial conversion system is a complex but controllable system with multiple factors involved. In the process of steroid microbial conversion, strain screening and selection is essential to improving productivity and reducing costs. However, good-quality strains need optimal environmental conditions to best play their roles. Therefore, environmental conditions can significantly affect the conversion rate in addition to the quality of the strains utilized. Microbial environment includes physiological and biochemical environment, physical and materialized environment and hydro-mechanical environment. For example, the composition, pH value and dissolved oxygen of culture medium affect the physiological and biochemical environment; gas-liquid interface and liquid-solid interface of culture media affect the physical and materialized environment; scattered and mixed conditions of culture system affect the hydro-mechanical environment. Representative physical factors and their applications in steroid microbial conversion system are briefly reviewed herein.


Author(s):  
Won-Ki Min ◽  
Jae Ok Lee ◽  
Chun Hee Kim ◽  
Junghan Song ◽  
Jin Q Kim

We determined serum lipoprotein(a) [Lp(a)] concentrations and apolipoprotein(a) [apo(a)] phenotypes in 193 healthy Koreans. We analysed the apo(a) phenotypes by a simplified sodium dodecyl sulphate-polyacrylamide gel electrophoresis method and classified apo(a) isoforms objectively using an apo(a) phenotype standard with a known number of kringle IV repeats. The frequency distribution of Lp(a) levels showed marked positive skew with a mean of 0·143 g/L and a median of 0·052 g/L. Of the 193 subjects tested, no bands were detected in three, and single- and double-band phenotypes were observed in 103 and 87, respectively. Among the Koreans, the most frequent phenotype was S5(39·4%), followed by S4S5(17·1%), S5S5(14·0%), S4(11·4%), S3S5(5·2%), and the remaining phenotypes (13·0%). The calculated apo(a) allele frequencies were LpF, 0·003; LpS1, 0·013; LpS2, 0·010; LpS3 0·048; LpS4 0·198; LpS5, 0·563 and Lp0, 0·165. We found that the serum Lp(a) concentration in Koreans was similar to that of Caucasians, but the apo(a) allele size distribution was shifted toward higher molecular weights.


1988 ◽  
Vol 256 (1) ◽  
pp. 35-40 ◽  
Author(s):  
H Larjava ◽  
J Heino ◽  
T Krusius ◽  
E Vuorio ◽  
M Tammi

Dermatan sulphate proteoglycans (DSPGs) synthesized in the presence of 35SO4 were characterized in culture media of fibroblast lines obtained from skin, synovium, and gingiva. The molecular mass of DSPG varied from 95-130 kDa as estimated by SDS/polyacrylamide-gel electrophoresis. Gingival fibroblasts constantly produced larger DSPGs than skin fibroblasts. This was due to the larger dermatan sulphate (DS) chains, which also showed tissue-related heterogeneity in the distribution of 4- and 6-sulphated disaccharide units. The N-glycosylated cores (44 and 47 kDa) obtained following chondroitinase ABC treatment were of identical size in all tissues. The cores from the different tissues were also of the same size (38 kDa) when addition of the N-linked oligosaccharides was inhibited by tunicamycin or when they were removed by N-glycanase treatment. No evidence for low-molecular-mass sulphated oligosaccharides was found. All tissues contained two mRNA species (1.6 and 1.9 kb) for the DSPG core protein. These data suggest that the pattern of transferase activities involved in the construction of DS chains differs from one tissue to another. This variation may modulate the functions of DSPG in the extracellular matrix.


Fishes ◽  
2021 ◽  
Vol 6 (3) ◽  
pp. 30
Author(s):  
Van Bon Nguyen ◽  
San-Lang Wang ◽  
Anh Dzung Nguyen ◽  
Tu Quy Phan ◽  
Kuaanan Techato ◽  
...  

The aim of this work was to reuse a fish processing waste, shrimp head powder (SHP), for the production of prodigiosin (PG) via microbial technology and to assess its potential bioactivities. PG was produced in a 12 L-bioreactor system, and the highest PG productivity of 6310 mg L−1 was achieved when Serratia marcescens CC17 was used for fermentation in a novel designed medium (6.75 L) containing 1.5% C/N source (SHP/casein = 9/1), 0.02% K2SO4, ans 0.025% Ca3(PO4)2, with initial pH 7.0, and fermentation was performed at 28 °C for 8 h. The purified PG showed moderate antioxidants, efficient anti-NO (anti-nitric oxide), and acetylcholinesterase (AChE) inhibitory activities. In a docking study, PG showed better binding energy scores (−12.3 kcal/mol) and more interactions (6 linkages) with several prominent amino acids in the biding sites on AChE that were superior to those of Berberine chloride (−10.8 kcal/mol and one linkage). Notably, this is the first investigation using shrimp heads for the mass bioproduction of PG with high productivity, and Ca3(PO4)2 salt was also newly found to significantly enhance PG production by S. marcescens. This study also provided available data on the anti-NO and anti-AChE effects of PG, especially from the docking simulation PG towards AChE that was described for the first time in this study. The above results suggest that SHP is a good material for the cost-effective bioproduction of PG, which is a potential candidate for anti-NO and anti-Alzheimer drugs.


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