• Preventive Nutrition and Food Science
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• 제7권1호
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• pp.43-47
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• 2002

Crude caseinomacropeptide (CMP) was prepared from Na-caseinate using a commercial renneting enzyme. Most of the crude CMP was released from the Na-caseinate by hydrolyzing with the enzyme for 40 min. The hydrolysis of the k-casein with carbohydrate was slower than that of the k-casein without carbohydrate, as shown by the analyses of the sialic acid content and the tricine-SDS-polyacrylamide gel electrophoresis. The yield of crude CMP from Na-caseinate was 3.7%. Cation exchange chromatography showed that the crude CMP consisted of 40.5% CMP and 59.5% caseinogylcomacropetide (CGP). The effect of the TCA concentration on the solubility of CMP and CGP was determined by using crude CMP. The amounts of crude CMP and sialic acid decreased in the proportion to the increase of trichloroacetic acid (TCA) concentration from 2 to 12%, suggesting that the CGP containing carbohydrate, as well as the CMP having no carbohydrate, was precipitated in a range of 4 to 12%, depending on the TCA concentration. This result supports the hypothesis that the different non-glycosylated and glycosylated forms of CMP have different sensitivities to TCA precipitation.

• Biotechnology and Bioprocess Engineering:BBE
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• 제10권3호
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• pp.242-247
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• 2005

Caseinomacropeptide (CMP) is a glycopeptide of 64 amino acid residues derived from the C-terminal of mammalian milk K-casein. Recently, human CMP (hCMP) was produced from the recombinant yeast Saccharomyces cerevisiae. In this study, the antiobesity activity of the recombinant hCMP (rhCMP) was investigated in vivo using Sprague-Dawley rats. The rhCMP did not affect the rats fed with a normal fat diet (fat content, $5.0\%$), but decreased the body weight gain of the rats fed with a high fat diet (fat content, $20\%$) by up to $19\%$. Autopsies revealed that the weights of the liver, kidney and adipose tissues decreased when the rats were given the rhCMP, which also reduced the lipid concentrations in the plasma and liver, but enhanced the fecal excretion of lipids. These results suggest that rhCMP prevent the accumulation of lipid by stimulating its fecal excretion, so could be used as a food supplement to alleviate the obesity problem caused by a high fat diet.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2003년도 생물공학의 동향(XII)
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• pp.522-523
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• 2003

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2001년도 추계학술발표대회
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• pp.441-443
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• 2001

CMP(caseinomacropeptide) is known to be a peptide which controls the gain of body weight and eventually will be used as a new candidate to control obesity problem. In this study, CMP gene was obtained using RT-PCR and ligated to secretion vectors having different kinds of promoters and P.pastoris and S.cerevisiae were transformed with these vectors. Colonies showing high titre of CMP cxpressecl were chosen and fed-batch fermentation is being carried out with these transformant to test economic feasibility

• 한국식품과학회지
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• 제28권1호
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• pp.99-104
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• 1996

탄수화물을 갖고 있지 않은 caseinomacropeptide (CMP)를 감성유청분말로부터 12% TCA법에 의해 분리한 결과 100 g의 감성유청분말로 부터 2.7 g을 얻을 수 있었다. 분리된 CMP는 전기영동과 아미노산 조성을 분석한 결과 매우 순도가 높은 CMP로 나타나 12% TCA침전법은 감성유청분말로 부터 CMP를 분리하는 효과적인 방법임을 알 수 있었다. 트립신을 pore glass beads에 carbodiimide (EDC) 방법으로 amide결합에 의해 고정화시켰으며 고정화된 트립신의 양은 1 g glass beads당 20 mg이었다. 수용성 트립신에 의한 CMP 가수분해는 24시간이 지나면 거의 완료되었으며 고정화 트립신은 24시간이 지난 후에도 가수분해가 진행되고 있었다. 가수분해물을 Bio-Gel P4 column에 의해 분획한 후 혈소판 응집 저해작용을 측정한 결과 고정화 트립신에 의해 24시간 가수분해시킨 CMP 분해물이 가장 높은 혈소판 응집 억제능을 보였다.

• 한국식품영양과학회지
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• 제27권6호
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• pp.1117-1124
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• 1998

Chymosin was purified from commercial rennet with DEAE Sepharose CL 6B and immobilized on CeliteTM using glutaraldehyde. Whole casein from fresh raw milk was hydrolyzed by immobilized chymosin and total CMP was isolated by trichloroacetic acid(TCA) and ultrafiltration, and characterized. The amount of chymosin purified from 15g commercial rennet by DEAE Sepharose CL 6B was 0.16g and 18mg of chymosin was immobilized on 1g of CeliteTM by 5% glutaraldehyde. Immobilized chy mosin hydrolyzed most of casein on whole casein within 2 hours to leave para casein and casei nomacropeptide(CMP). The total CMP isolated from 10g of whole casein hydrolyzate by TCA and ultrafiltration was 0.4g and 0.1g, respectively. Results of electrophoresis, amount of sialic acid, com position of amino acid and ratio of A280 to A214 showed that total CMP by TCA was purer and had more CMP without carbohydrate than one by ultrafiltration. CMP isolated from total CMP by 12% TCA precipitation was 50% of total CMP and most of caseinoglycopeptide(CGP) was removed from total CMP, indicating less amount of sialic acid in CMP than in total CMP.