A chitinase system from Carcinus maenas

Lunt, Mary R.; Kent, P. W.

doi:10.1016/0006-3002(60)91581-x

Cited by 31 publications

(6 citation statements)

References 5 publications

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“…It is hydrolyzed by two enzymes in sequence: chitinase, which converts the long chitin polymers into small oligosaccharides; and chitobiase (f-N-acetylglucosaminidase), which hydrolyzes these chito-oligomers into N-acetyl-D-glucosamine (Lunt and Kent, 1960;Jeuniaux, 1966;O'Brien et al, 1993). These enzymes might be degrading the coat wrapping the ovigerous hairs until it is able to slip off the hairs.…”

Section: Identity Of Ohssmentioning

confidence: 99%

Bioassay and Preliminary Characterization of Ovigerous-Hair Stripping Substance (OHSS) in Hatch Water of Crab Larvae

Saigusa¹

1995

The Biological Bulletin

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Hatch water (the filtrated medium into which zoea larvae have been released) of the estuarine terrestrial crab Sesarma haematocheir (akate-gani) contains a substance that causes premature detachment of embryos from ovigerous females. Detachment occurs when the ovigerous hairs along the female's ovigerous setae slip out of the investment coat that binds them to the embryos through stalks, or funiculi. The active factor, which I call ovigeroushair stripping substance (OHSS), is released outside of the egg capsule at the time of hatching, and is not secreted by the female. This study describes the results of a quantitative assay for measuring the activity of OHSS. Activity is measured as the percentage of hairs on a seta that can be induced to slip out of the coat without damage. Experiments with an extract of crushed embryos indicated that OHSS is present up to 2 days before hatching. Its activity was destroyed by heat and trypsin, suggesting that it is a protein. Its molecular size was estimated by gel filtration to be 15-20 kDa in S. haematocheir and 30 kDa in S. pictum. Reciprocal tests among different species indicated that OHSS occurs widely in intertidal and estuarine crabs.

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Section: Identity Of Ohssmentioning

confidence: 99%

Bioassay and Preliminary Characterization of Ovigerous-Hair Stripping Substance (OHSS) in Hatch Water of Crab Larvae

Saigusa¹

1995

The Biological Bulletin

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“…Chitinases (EC 3.2.1.14) hydrolyze the L-1,4-glucosidic bonds of chitin and are commonly found in a wide variety of organisms, including fungi [1,2], plants [3,4], insects [5], crustaceans [6], and bacteria [7^9]. The roles of these chitinases di¡er in the various hosts.…”

Section: Introductionmentioning

confidence: 99%

Cloning of the 52-kDa chitinase gene from Serratia marcescens KCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme

Gal¹

1998

FEMS Microbiology Letters

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A chitinase gene (pCHI52) encoding the 52-kDa chitinase was isolated from a Serratia marcescens KCTC2172 cosmid library. This chitinase gene consists of 2526 bp with an open reading frame that encodes 485 amino acids. Escherichia coli harboring the pCHI52 gene secreted not only a 52-kDa but also a 35-kDa chitinase into the culture supernatant. We purified both 52-kDa and 35-kDa chitinases using a chitin affinity column and Sephacryl-S-300 gel filtration chromatography. We determined that the 17 N-terminal amino acid sequences of the 52-kDa and the 35-kDa chitinase are identical. Furthermore, a protease obtained from S. marcescens KCTC2172 cleaved the 52-kDa chitinase into the 35-kDa protein with chitinase activity. These results suggest that the 35-kDa chitinase derives from the 52-kDa chitinase by post-translational proteolytic modification. The optimal reaction temperature of 45³C and the optimal pH of 5.5 were identical for both enzymes. The specific activities of the 52-kDa and 35-kDa chitinases on natural swollen chitin were 67 Wmol min 3I mg 3I and 60 Wmol min 3I mg 3I , respectively.

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“…ZoBell and Rittenberg (39) reported that chitinolytic bacteria, which are abundant and widely distributed in the sea, play an important role in converting insoluble chitin into a biologically usable form. Chitinases (EC 3.2.1.14) are enzymes which degrade chitin, and they have been detected in various microorganisms (3,25,28,30), plants (1,18), insects (5,13), and crustaceans (19). Alteromonas sp.…”

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confidence: 99%

Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Altermonas sp. strain O-7

et al. 1993

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The gene encoding an extracellular chitinase from marine Alteromonas sp. strain 0-7 was cloned in Escherichia coli JM109 by using pUC18. The chitinase produced was not secreted into the growth medium but accumulated in the periplasmic space. A chitinase-positive clone of E. coli produced two chitinases with different molecular weights from a single chitinase gene. These proteins showed almost the same enzymatic properties as the native chitinase ofAlteromonas sp. strain 0-7. The N-terminal sequences of the two enzymes were identical. The nucleotide sequence of the 3,394-bp SphI-HindIII fragment that included the chitinase gene was determined. A single open reading frame was found to encode a protein consisting of 820 amino acids with a molecular weight of 87,341. A putative ribosome-binding site, promoter, and signal sequence were identified. The deduced amino acid sequence of the cloned chitinase showed sequence homology with chitinases A (33.4%) and B (15.3%) from Serratia marcescens. Regardless of origin, the enzymes of the two bacteria isolated from marine and terrestrial environments had high homology, suggesting that these organisms evolved from a common ancestor.Chitin is a major component of the exoskeletons of insects and crustaceans, and it is abundantly distributed throughout nature. This polysaccharide is also an important nutrient source of both carbon and nitrogen in the marine environment. Yu et al. (38) pointed out that the oceans would be completely depleted of carbon and nitrogen in a relatively short time if chitin could not be returned to the ecosystem in a biologically usable form. However, marine sediment contains relatively little chitin, despite the production of huge amounts of this insoluble polysaccharide by crustaceans. ZoBell and Rittenberg (39) reported that chitinolytic bacteria, which are abundant and widely distributed in the sea, play an important role in converting insoluble chitin into a biologically usable form. Chitinases (EC 3.2.1.14) are enzymes which degrade chitin, and they have been detected in various microorganisms (3,25,28,30), plants (1, 18), insects (5, 13), and crustaceans (19). Alteromonas sp. strain 0-7 is a gram-negative, flagellated, motile, and aerobic rod-shaped bacterium of marine origin. This strain excretes chitinase into the growth medium in the presence of chitin (32). We have already reported the purification, properties, and partial amino acid sequence of the enzyme from this strain (33). Recently, bacterial chitinase genes from terrestrial and marine bacteria such as Serratia marcescens (6, 10), Bacillus circulans (35, 36), Vibrio harveyi (28), and Vibno vulnificus (37) have been cloned and sequenced. However, the mechanism of hydrolysis, the relationship between structure and function, and the regulatory system involved in enzyme induction are still unclear. In this report, we describe the cloning of a gene coding for chitinase and the purification of the gene products. The nucleotide sequence of the gene was determined, and the deduced amino acid s...

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A chitinase system from Carcinus maenas

Cited by 31 publications

References 5 publications

Bioassay and Preliminary Characterization of Ovigerous-Hair Stripping Substance (OHSS) in Hatch Water of Crab Larvae

Bioassay and Preliminary Characterization of Ovigerous-Hair Stripping Substance (OHSS) in Hatch Water of Crab Larvae

Cloning of the 52-kDa chitinase gene from Serratia marcescens KCTC2172 and its proteolytic cleavage into an active 35-kDa enzyme

Cloning, sequence, and expression of a chitinase gene from a marine bacterium, Altermonas sp. strain O-7

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