The yield, nitrogen content, and dye’s binding capacity of chitin and chitosan of rotifer Brachionus rotundiformis

2013 ◽  
pp. 99
Author(s):  
Riny Modaso ◽  
Edi Suryanto ◽  
Trina Tallei ◽  
Inneke F.M Rumengan
Keyword(s):  
Nitrogen Content ◽  
Mass Culture ◽  
Binding Capacity ◽  
High Biomass ◽  
Brachionus Rotundiformis ◽  
Basic Properties ◽  
Dye Binding ◽  
Kjeldahl Method ◽  
Chitin And Chitosan

Chitin and chitosan from rotifer have not been previously explored due to the problem of high biomass required for extraction. This study aimed to obtain the chitin yield from rotifer biomass produced in mass culture, and to characterize the basic properties of chitin and chitosan, especially, nitrogen content and dye binding capacity. Methods of extraction and deacetylation of chitin were adopted from Chandumpai et al. (2004) with modification. The nitrogen content was analyzed using the semi-micro Kjeldahl method (AOAC, 1984), and dye binding capacity using the method developed by Cho et al. (1998). Results show that the yield of chitin obtained from the rotifer sample was relatively small (4.64%), and the yield of chitosan was even smaller, only 2,62%. The proportion of chitosan over chitin was 52,4%. The nitrogen content of chitin and chitosan of rotifer were 4.23 to 4.36% and 7.12-7.23%, respectively. The capacity of chitin to maintain the bonded dye was relatively stronger than that of chitosan, but the chitosan had higher capacity to absorb the dye. The characterization of other important properties of chitin and chitosan to be developed as biopolymer for industry is further aspects to be assessed© Eksplorasi kitin dan kitosan dari rotifer belum pernah dilakukan sebelumnya karena dihadapkan pada permasalahan kebutuhkan biomassa yang banyak. Penelitian ini bertujuan untuk memperoleh rendemen kitin dari biomassa rotifer hasil kultur massal, dan menjajaki karakterisasi awal sifat fisika kimia kitin yang mendasar yaitu daya ikat zat warna dan kadar nitrogen. Ekstraksi kitin dan kitosan dilakukan berdasarkan metode Chandupai et al. (2004), kadar nitrogen menggunakan metode semi-micro Kjeldahl (AOAC, 1984), dan daya ikat zar warna ditentukan menurut metode Cho et al. (1998). Dari penelitian ini, rendemen kitin yang diperoleh dari hasil ekstraksi relatif kecil berkisar 4,64 %, dan rendemen kitosan bahkan lebih kecil lagi hanya 2,62%. Proporsi kitosan dari kitin yaitu 52.4 %. Kadar nitrogen pada kitin rotifer berkisar 4,23-4,36 % dan kitosan berkisar dari 7,12-7,23%. Kitin memiliki sifat yang lebih baik dalam ketahanan untuk mengikat zat warna sebaliknya kitosan memperlihatkan sifatnya yang dapat mengikat zat warna dalam tingkat adsorpsi yang tinggi dibanding kitin. Karakterisasi  sifat fisika kimia kitin dan kitosan yang penting lainnya untuk pengembangannya sebagai biopolimer dalam skala industri, merupakan aspek-aspek yang perlu dikaji lebih lanjut©

scholarly journals Growth and characterization of BCN nanotubes with high boron and nitrogen content

2013 ◽  
Vol 125 (5) ◽  
pp. 1169-1176 ◽  
Author(s):  
GUO ZHANG ◽  
ZHIYE LIU ◽  
LIANPING ZHANG ◽  
LIQIANG JING ◽  
KEYING SHI
Keyword(s):  
Nitrogen Content ◽  
High Boron

scholarly journals A g-Type Lysozyme from Deep-Sea Hydrothermal Vent Shrimp Kills Selectively Gram-Negative Bacteria

Molecules ◽  
2021 ◽  
Vol 26 (24) ◽  
pp. 7624
Author(s):  
Jing-Chang Luo ◽  
Jian Zhang ◽  
Li Sun
Keyword(s):  
Deep Sea ◽  
Hydrothermal Vent ◽  
Binding Capacity ◽  
Cellular Membrane ◽  
Structural Features ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Bacterial Binding ◽  
Muramidase Activity

Lysozyme is a key effector molecule of the innate immune system in both vertebrate and invertebrate. It is classified into six types, one of which is the goose-type (g-type). To date, no study on g-type lysozyme in crustacean has been documented. Here, we report the identification and characterization of a g-type lysozyme (named LysG1) from the shrimp inhabiting a deep-sea hydrothermal vent in Manus Basin. LysG1 possesses conserved structural features of g-type lysozymes. The recombinant LysG1 (rLysG1) exhibited no muramidase activity and killed selectively Gram-negative bacteria in a manner that depended on temperature, pH, and metal ions. rLysG1 bound target bacteria via interaction with bacterial cell wall components, notably lipopolysaccharide (LPS), and induced cellular membrane permeabilization, which eventually caused cell lysis. The endotoxin-binding capacity enabled rLysG1 to alleviate the inflammatory response induced by LPS. Mutation analysis showed that the bacterial binding and killing activities of rLysG1 required the integrity of the conserved α3 and 4 helixes of the protein. Together, these results provide the first insight into the activity and working mechanism of g-type lysozyme in crustacean and deep-sea organisms.

scholarly journals Human xylosyltransferase I and N-terminal truncated forms: functional characterization of the core enzyme

2006 ◽  
Vol 394 (1) ◽  
pp. 163-171 ◽  
Author(s):  
Sandra Müller ◽  
Jennifer Disse ◽  
Manuela Schöttler ◽  
Sylvia Schön ◽  
Christian Prante ◽  
...  
Keyword(s):  
Amino Acids ◽  
Catalytic Activity ◽  
Binding Capacity ◽  
Functional Characterization ◽  
Terminal Region ◽  
Binding Motif ◽  
Heparin Binding ◽  
Loss Of Function ◽  
The Impact

Human XT-I (xylosyltransferase I; EC 2.4.2.26) initiates the biosynthesis of the glycosaminoglycan linkage region and is a diagnostic marker of an enhanced proteoglycan biosynthesis. In the present study, we have investigated mutant enzymes of human XT-I and assessed the impact of the N-terminal region on the enzymatic activity. Soluble mutant enzymes of human XT-I with deletions at the N-terminal domain were expressed in insect cells and analysed for catalytic activity. As many as 260 amino acids could be truncated at the N-terminal region of the enzyme without affecting its catalytic activity. However, truncation of 266, 272 and 273 amino acids resulted in a 70, 90 and >98% loss in catalytic activity. Interestingly, deletion of the single 12 amino acid motif G261KEAISALSRAK272 leads to a loss-of-function XT-I mutant. This is in agreement with our findings analysing the importance of the Cys residues where we have shown that C276A mutation resulted in a nearly inactive XT-I enzyme. Moreover, we investigated the location of the heparin-binding site of human XT-I using the truncated mutants. Heparin binding was observed to be slightly altered in mutants lacking 289 or 568 amino acids, but deletion of the potential heparin-binding motif P721KKVFKI727 did not lead to a loss of heparin binding capacity. The effect of heparin or UDP on the XT-I activity of all mutants was not significantly different from that of the wild-type. Our study demonstrates that over 80% of the nucleotide sequence of the XT-I-cDNA is necessary for expressing a recombinant enzyme with full catalytic activity.

Extraction, chemical modification and characterization of chitin and chitosan

2018 ◽  
Vol 120 ◽  
pp. 1181-1189 ◽  
Author(s):  
Hakima El Knidri ◽  
Raja Belaabed ◽  
Abdellah Addaou ◽  
Ali Laajeb ◽  
Ahmed Lahsini
Keyword(s):  
Chemical Modification ◽  
Chitin And Chitosan

scholarly journals CHARACTERIZATION OFWASTE BIOMASS FROM GREENHOUSE ROSE CULTIVATION AND PACKAGING

2010 ◽  
Vol 41 (2) ◽  
pp. 29
Author(s):  
Giovanni Cascone ◽  
Alessandro D'Emilio ◽  
Erika Buccellato
Keyword(s):  
Nitrogen Content ◽  
Calorific Value ◽  
Volatile Matter ◽  
Chemical Processes ◽  
The Other ◽  
Waste Biomass

In this work a characterization of the waste biomass originating from a rose cultivation under greenhouse was carried out. Two types of biomass were examined: one made of both branches and leaves, and the other made up only of branches. For each type of biomass the following properties were determined: percentage of carbon, hydrogen and nitrogen, content of moisture, volatile matter and ashes, gross and net calorific value. The results show that the biomass made of only branches has a better quality than the biomass with leaves for use in thermo-chemical processes.

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