Journal of Amino Acids最新文献

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Dicer functions in aquatic species. Dicer在水生物种中起作用。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-06-09 DOI: 10.4061/2011/782187
Yasuko Kitagishi, Naoko Okumura, Hitomi Yoshida, Chika Tateishi, Yuri Nishimura, Satoru Matsuda
{"title":"Dicer functions in aquatic species.","authors":"Yasuko Kitagishi,&nbsp;Naoko Okumura,&nbsp;Hitomi Yoshida,&nbsp;Chika Tateishi,&nbsp;Yuri Nishimura,&nbsp;Satoru Matsuda","doi":"10.4061/2011/782187","DOIUrl":"https://doi.org/10.4061/2011/782187","url":null,"abstract":"<p><p>Dicer is an RNase III enzyme with two catalytic subunits, which catalyzes the cleavage of double-stranded RNA to small interfering RNAs and micro-RNAs, which are mainly involved in invasive nucleic acid defense and endogenous genes regulation. Dicer is abundantly expressed in embryos, indicating the importance of the protein in early embryonic development. In addition, Dicer is thought to be involved in defense mechanism against foreign nucleic acids such as viruses. This paper will mainly focus on the recent progress of Dicer-related research and discuss potential RNA interference pathways in aquatic species.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"782187"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/782187","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968226","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 7
The dynamic structure of the estrogen receptor. 雌激素受体的动态结构。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-07-26 DOI: 10.4061/2011/812540
Raj Kumar, Mikhail N Zakharov, Shagufta H Khan, Rika Miki, Hyeran Jang, Gianluca Toraldo, Rajan Singh, Shalender Bhasin, Ravi Jasuja
{"title":"The dynamic structure of the estrogen receptor.","authors":"Raj Kumar,&nbsp;Mikhail N Zakharov,&nbsp;Shagufta H Khan,&nbsp;Rika Miki,&nbsp;Hyeran Jang,&nbsp;Gianluca Toraldo,&nbsp;Rajan Singh,&nbsp;Shalender Bhasin,&nbsp;Ravi Jasuja","doi":"10.4061/2011/812540","DOIUrl":"https://doi.org/10.4061/2011/812540","url":null,"abstract":"<p><p>The estrogen receptor (ER) mediates most of the biological effects of estrogens at the level of gene regulation by interacting through its site-specific DNA and with other coregulatory proteins. In recent years, new information regarding the dynamic structural nature of ER has emerged. The physiological effects of estrogen are manifested through ER's two isoforms, ER(α) and ER(β). These two isoforms (ER(α) and ER(β)) display distinct regions of sequence homology. The three-dimensional structures of the DNA-binding domain (DBD) and ligand-binding domain (LBD) have been solved, whereas no three-dimensional natively folded structure for the ER N-terminal domain (NTD) is available to date. However, insights about the structural and functional correlations regarding the ER NTD have recently emerged. In this paper, we discuss the knowledge about the structural characteristics of the ER in general and how the structural features of the two isoforms differ, and its subsequent role in gene regulation.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"812540"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/812540","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968304","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 217
Comparative Study on Biochemical Properties and Antioxidative Activity of Cuttlefish (Sepia officinalis) Protein Hydrolysates Produced by Alcalase and Bacillus licheniformis NH1 Proteases. 阿尔卡拉酶和地衣芽孢杆菌 NH1 蛋白酶产生的墨鱼(Sepia officinalis)蛋白水解物的生化特性和抗氧化活性比较研究
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-10-03 DOI: 10.4061/2011/107179
Rafik Balti, Ali Bougatef, Nedra El Hadj Ali, Naourez Ktari, Kemel Jellouli, Naima Nedjar-Arroume, Pascal Dhulster, Moncef Nasri
{"title":"Comparative Study on Biochemical Properties and Antioxidative Activity of Cuttlefish (Sepia officinalis) Protein Hydrolysates Produced by Alcalase and Bacillus licheniformis NH1 Proteases.","authors":"Rafik Balti, Ali Bougatef, Nedra El Hadj Ali, Naourez Ktari, Kemel Jellouli, Naima Nedjar-Arroume, Pascal Dhulster, Moncef Nasri","doi":"10.4061/2011/107179","DOIUrl":"10.4061/2011/107179","url":null,"abstract":"<p><p>Antioxidative activities and biochemical properties of protein hydrolysates prepared from cuttlefish (Sepia officinalis) using Alcalase 2.4 L and Bacillus licheniformis NH1 proteases with different degrees of hydrolysis (DH) were determined. For the biochemical properties, hydrolysis by both enzymes increased protein solubility to above 75% over a wide pH range. The antioxidant activities of cuttlefish protein hydrolysates (CPHs) increase with increasing DH. In addition, all CPHs exhibited antioxidative activity in a concentration-dependent manner. NH1-CPHs generally showed greater antioxidative activity than Alcalase protein hydrolysates (P < 0.05) as indicated by the higher 1,1-diphenyl-1-picryhydrazyl (DPPH) radical scavenging activity and ferrous chelating activity. Both Alcalase and NH1 protein hydrolysates were able to retard lipid peroxidation and β-carotene-linoleic acid oxidation. Alcalase-CPH (DH = 12.5%) and NH1-CPH (DH = 15%) contained 75.36% and 80.11% protein, respectively, with histidine and arginine as the major amino acids, followed by glutamic acid/glutamine, serine, lysine, and leucine. In addition, CPHs have a high percentage of essential amino acids made up 48.85% and 50.04%. Cuttlefish muscle protein hydrolysates had a high nutritional value and could be used as supplement to poorly balanced dietary proteins.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"107179"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3268033/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39967714","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
NOP Receptor Ligands as Potential Agents for Inflammatory and Autoimmune Diseases. NOP受体配体作为炎症和自身免疫性疾病的潜在药物。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-11-17 DOI: 10.4061/2011/836569
Elaine C Gavioli, Pedro R T Romão
{"title":"NOP Receptor Ligands as Potential Agents for Inflammatory and Autoimmune Diseases.","authors":"Elaine C Gavioli,&nbsp;Pedro R T Romão","doi":"10.4061/2011/836569","DOIUrl":"https://doi.org/10.4061/2011/836569","url":null,"abstract":"<p><p>Nociceptin/orphanin FQ (N/OFQ) is a seventeen-amino acid peptide that is the endogenous ligand of a G-protein-coupled receptor (NOP). Various immune cells express the precursor protein and secrete N/OFQ as well as display binding sites for this peptide. The functional capacity of NOP receptor was demonstrated in vitro and in vivo studies by the ability of N/OFQ to induce chemotaxis of immune cells, to regulate the expression of cytokines and other inflammatory mediators, and to control cellular and humoral immunity. In this context, N/OFQ could modulate the outcome of some inflammatory diseases, such as sepsis and autoimmune pathologies by mechanisms not clearly elucidated yet. In fact, human body fluid revealed increased levels of N/OFQ under sepsis, arthritis, and Parkinson's diagnose. Preclinical studies pointed to the blockade of NOP receptor signaling as successful in treating these experimental conditions. Further preclinical and clinical studies are required to investigate the potential of NOP ligands in treating inflammatory diseases.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"836569"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/836569","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968002","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 23
The Importance of GLWamide Neuropeptides in Cnidarian Development and Physiology. 谷氨酰胺神经肽在刺胞细胞发育和生理中的重要性。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-10-20 DOI: 10.4061/2011/424501
Toshio Takahashi, Masayuki Hatta
{"title":"The Importance of GLWamide Neuropeptides in Cnidarian Development and Physiology.","authors":"Toshio Takahashi,&nbsp;Masayuki Hatta","doi":"10.4061/2011/424501","DOIUrl":"https://doi.org/10.4061/2011/424501","url":null,"abstract":"<p><p>The peptide-signaling molecules (<50 amino acid residues) occur in a wide variety of invertebrate and vertebrate organisms, playing pivotal roles in physiological, endocrine, and developmental processes. While some of these peptides display similar structures in mammals and invertebrates, others differ with respect to their structure and function in a species-specific manner. Such a conservation of basic structure and function implies that many peptide-signaling molecules arose very early in the evolutionary history of some taxa, while species-specific characteristics led us to suggest that they also acquire the ability to evolve in response to specific environmental conditions. In this paper, we describe GLWamide-family peptides that function as signaling molecules in the process of muscle contraction, metamorphosis, and settlement in cnidarians. The peptides are produced by neurons and are therefore referred to as neuropeptides. We discuss the importance of the neuropeptides in both developmental and physiological processes in a subset of hydrozoans, as well as the potential use as a seed compound in drug development and aspects related to the protection of corals.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"424501"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/424501","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 19
Methionine-35 of aβ(1-42): importance for oxidative stress in Alzheimer disease. aβ(1-42)的蛋氨酸-35:对阿尔茨海默病氧化应激的重要性。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-06-04 DOI: 10.4061/2011/198430
D Allan Butterfield, Rukhsana Sultana
{"title":"Methionine-35 of aβ(1-42): importance for oxidative stress in Alzheimer disease.","authors":"D Allan Butterfield, Rukhsana Sultana","doi":"10.4061/2011/198430","DOIUrl":"10.4061/2011/198430","url":null,"abstract":"<p><p>Alzheimer disease (AD) is an age-related progressive neurodegenerative disorder. This devastating disease is characterized by the presence of senile plaques (SP), neurofibrillary tangles (NFTs), and loss of synapses. Amyloid beta-peptide 1-42 (Aβ(1-42)) is the main component of SP and is pivotal to AD pathogenesis. Brain of subjects with AD and arguably its earliest manifestation, mild cognitive impairment (MCI), demonstrate increased levels of oxidative stress markers. Our laboratory combined these two aspects of AD and MCI and proposed the Aβ(1-42)-associated free radical oxidative stress hypothesis to explain oxidative stress under which the MCI and AD brain exist and the loss of synapses in both disorders. A large number of in vitro and in vivo studies showed that Aβ causes protein oxidation, lipid peroxidation, reactive oxygen species formation, and cell death in neuronal and synaptosomal systems. Methionine located at residue 35 of Aβ(1-42) is an important contributor to the oxidative stress associated with this neurotoxic peptide. In this paper, we summarize studies involving Met-35 of Aβ(1-42). Understanding the role of the single methionine residue of Aβ(1-42) may help in understanding underlying disease mechanisms in AD and MCI.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"198430"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3268025/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968207","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase. 带电残基在大肠杆菌ATP合酶催化位点的作用。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-07-13 DOI: 10.4061/2011/785741
Zulfiqar Ahmad, Florence Okafor, Thomas F Laughlin
{"title":"Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.","authors":"Zulfiqar Ahmad,&nbsp;Florence Okafor,&nbsp;Thomas F Laughlin","doi":"10.4061/2011/785741","DOIUrl":"https://doi.org/10.4061/2011/785741","url":null,"abstract":"<p><p>Here we describe the role of charged amino acids at the catalytic sites of Escherichia coli ATP synthase. There are four positively charged and four negatively charged residues in the vicinity of of E. coli ATP synthase catalytic sites. Positive charges are contributed by three arginine and one lysine, while negative charges are contributed by two aspartic acid and two glutamic acid residues. Replacement of arginine with a neutral amino acid has been shown to abrogate phosphate binding, while restoration of phosphate binding has been accomplished by insertion of arginine at the same or a nearby location. The number and position of positive charges plays a critical role in the proper and efficient binding of phosphate. However, a cluster of many positive charges inhibits phosphate binding. Moreover, the presence of negatively charged residues seems a requisite for the proper orientation and functioning of positively charged residues in the catalytic sites. This implies that electrostatic interactions between amino acids are an important constituent of initial phosphate binding in the catalytic sites. Significant loss of function in growth and ATPase activity assays in mutants generated through charge modulations has demonstrated that precise location and stereochemical interactions are of paramount importance.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"785741"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/785741","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968257","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 19
Proteins and enzymes from marine resources. 来自海洋资源的蛋白质和酶。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-11-20 DOI: 10.4061/2011/594646
Nabil Miled, Moncef Nasri, Hideki Kishimura, Faouzi Ben Rebah
{"title":"Proteins and enzymes from marine resources.","authors":"Nabil Miled,&nbsp;Moncef Nasri,&nbsp;Hideki Kishimura,&nbsp;Faouzi Ben Rebah","doi":"10.4061/2011/594646","DOIUrl":"https://doi.org/10.4061/2011/594646","url":null,"abstract":"Sea products are valuable resources of natural substances such as lipids, polysaccharides, enzymes, vitamins, and proteins. In this issue, a variety of fish proteases (trypsin, alcalase, etc.) have been characterized and sometimes purified. Many of these enzymes display potentially interesting new biochemical properties for industrial applications. Their potential adequacy for biotechnological applications such as chitin extraction was demonstrated. Biochemical characteristics of crude alkaline protease extracts from the viscera of goby (Zosterisessor ophiocephalus), thornback ray (Raja clavata), and scorpionfish (Scorpaena scrofa) were studied. At least four caseinolytic proteases bands were observed in zymogram of each enzyme preparation. These proteolytic preparations were successfully used in the deproteinization of shrimp wastes for chitin extraction. Furthermore, a trypsin was purified from the pyloric ceca of Pacific cod (Gadus macrocephalus) using chromatographic methods. The cod trypsin was successfully applied to catalyze dipeptide synthesis using series of “inverse substrates.” A Mackerel trypsin was also purified from defatted viscera by supercritical carbon dioxide, and its biochemical properties were studied.","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"594646"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/594646","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968314","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 1
Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease. 微小的变化巨大的影响:蛋白质翻译后修饰在细胞稳态和疾病中的作用。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-07-21 DOI: 10.4061/2011/207691
Tejaswita M Karve, Amrita K Cheema
{"title":"Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease.","authors":"Tejaswita M Karve,&nbsp;Amrita K Cheema","doi":"10.4061/2011/207691","DOIUrl":"https://doi.org/10.4061/2011/207691","url":null,"abstract":"<p><p>Posttranslational modifications (PTMs) modulate protein function in most eukaryotes and have a ubiquitous role in diverse range of cellular functions. Identification, characterization, and mapping of these modifications to specific amino acid residues on proteins are critical towards understanding their functional significance in a biological context. The interpretation of proteome data obtained from the high-throughput methods cannot be deciphered unambiguously without a priori knowledge of protein modifications. An in-depth understanding of protein PTMs is important not only for gaining a perception of a wide array of cellular functions but also towards developing drug therapies for many life-threatening diseases like cancer and neurodegenerative disorders. Many of the protein modifications like ubiquitination play a decisive role in various drug response(s) and eventually in disease prognosis. Thus, many commonly observed PTMs are routinely tracked as disease markers while many others are used as molecular targets for developing target-specific therapies. In this paper, we summarize some of the major, well-studied protein alterations and highlight their importance in various chronic diseases and normal development. In addition, other promising minor modifications such as SUMOylation, observed to impact cellular dynamics as well as disease pathology, are mentioned briefly.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"207691"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/207691","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968554","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 304
Digestive Alkaline Proteases from Zosterisessor ophiocephalus, Raja clavata, and Scorpaena scrofa: Characteristics and Application in Chitin Extraction. 蛇头带绦虫、克拉瓦塔鱼和天蝎消化性碱性蛋白酶的特性及其在甲壳素提取中的应用。
Journal of Amino Acids Pub Date : 2011-01-01 Epub Date: 2011-07-18 DOI: 10.4061/2011/913616
Rim Nasri, Islem Younes, Imen Lassoued, Sofiane Ghorbel, Olfa Ghorbel-Bellaaj, Moncef Nasri
{"title":"Digestive Alkaline Proteases from Zosterisessor ophiocephalus, Raja clavata, and Scorpaena scrofa: Characteristics and Application in Chitin Extraction.","authors":"Rim Nasri,&nbsp;Islem Younes,&nbsp;Imen Lassoued,&nbsp;Sofiane Ghorbel,&nbsp;Olfa Ghorbel-Bellaaj,&nbsp;Moncef Nasri","doi":"10.4061/2011/913616","DOIUrl":"https://doi.org/10.4061/2011/913616","url":null,"abstract":"<p><p>The aim of this work was to study some biochemical characteristics of crude alkaline protease extracts from the viscera of goby (Zosterisessor ophiocephalus), thornback ray (Raja clavata), and scorpionfish (Scorpaena scrofa), and to investigate their applications in the deproteinization of shrimp wastes. At least four caseinolytic proteases bands were observed in zymogram of each enzyme preparation. The optimum pH for enzymatic extracts activities of Z. ophiocephalus, R. clavata, and S. scrofa were 8.0-9.0, 8.0, and 10.0, respectively. Interestingly, all the enzyme preparations were highly stable over a wide range of pH from 6.0 to 11.0. The optimum temperatures for enzyme activity were 50°C for Z. ophiocephalus and R. clavata and 55°C for S. scrofa crude alkaline proteases. Proteolytic enzymes showed high stability towards non-ionic surfactants (5% Tween 20, Tween 80, and Triton X-100). In addition, crude proteases of S. scrofa, R. clavata, and Z. ophiocephalus were found to be highly stable towards oxidizing agents, retaining 100%, 70%, and 66%, respectively, of their initial activity after incubation for 1 h in the presence of 1% sodium perborate. They were, however, highly affected by the anionic surfactant SDS. The crude alkaline proteases were tested for the deproteinization of shrimp waste in the preparation of chitin. All proteases were found to be effective in the deproteinization of shrimp waste. The protein removals after 3 h of hydrolysis at 45°C with an enzyme/substrate ratio (E/S) of 10 were about 76%, 76%, and 80%, for Z. ophiocephalus, R. clavata, and S. scrofa crude proteases, respectively. These results suggest that enzymatic deproteinization of shrimp wastes by fish endogenous alkaline proteases could be applicable to the chitin production process.</p>","PeriodicalId":14901,"journal":{"name":"Journal of Amino Acids","volume":" ","pages":"913616"},"PeriodicalIF":0.0,"publicationDate":"2011-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4061/2011/913616","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39968879","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 34
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