• 한국식품영양과학회지
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• 제25권2호
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• pp.255-260
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• 1996

증편반죽의 발효에 따른 해면상의 조직(망상구조)형성능의 mechanism을 조사하기 위하여 반죽의 구성성분의 경시적 물성 및 효소(diastase 및 protease) 활성의 변화, 구성 전분 분획의 glucose chain length 변화 및 1% SDS에 의해서 용출되는 단백질 분획의 변화에 대해서 검토하였다. 발효가 진행됨에 따라 증편반죽의 pH는 감소한 반면 점성 및 부피는 발효경과 10시간가지 증가하다가 그 이후로는 약간 감소하는 경향을 보였다. 발효의 진행과 더불어 diastase의 활성은 증가하였으며, 쌀전분 분획 중 amylose의 함량은 약간 감소하였다. 그리고 전분분자의 $\alpha-1,6-glucoside$ 결합을 isoamylase(debranching enzyme)로 가수분해시킨 후 Sephadex G-75를 이용한 chromatogram 분석에 의하면 쌀가루 전분 분획과 증편반죽 전분 분획의 glucose chain length 분포는 거의 유사하지만 발효가 진행됨에 따라 중합도가 낮은 부분이 우선적으로 diastase의 작용을 받은 것이라고 생각되어진다. 한편, 발효가 진행된에 따라 protease의 활성은 증가하고 있었음에도 불구하고 증편반죽의 당에 의한 단백질 분획의 고분자화가 Suprose CL-12 column chromatogram 상에서 관찰되었는데, 이것은 아마도 발효과정 중 증편반죽에 공존하는 미생물들의 발효산물인 당질(gum질)을 매개로 한 단백질 분자의 회합에 의한 결과라고 생각되어진다. 따라서 이러한 결과를 미루어 볼 때 증편반죽의 망상구조 형성능은 발효과정 중 일어나는 당과 단백질간의 상호작용에 의한 결과라 생각되어진다.

• Food Science and Biotechnology
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• 제18권2호
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• pp.402-406
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• 2009

The Japonica cultivar 'Janganbyeo' was cultivated and about half of paddy field was totally lodged at 30 days after heading. Both lodged paddy and unlodged paddy were harvested at intervals. The lodged paddy and brown rice did not show any signs of viviparity until the $4^{th}$ day of lodging. The activities of $\alpha$-amylase, diastase, and lipase of lodged paddy and brown rice began to increase on the $2^{nd}$ day of lodging and then increased slowly afterwards. The activities of protease and phytase of lodged paddy and brown rice reached the maximum values on the $2^{nd}$ day and then decreased until the final day of lodging. In contrast, unlodged paddy and brown rice showed relatively small increase in viviparity and in activities of $\alpha$-amylase, diastase, protease, lipase, and phytase. Especially, activities of diastase and lipase were observed even in unlodged paddy and brown rice.

• Journal of Microbiology and Biotechnology
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• 제19권11호
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• pp.1393-1400
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• 2009

A bacteriocin-producing strain PI80 was isolated from the gut of Penaeus indicus (Indian white shrimp) and identified as Streptococcus phocae PI80. The bacteriocin was purified from a culture supernatant to homogeneity as confirmed by Tricine SDS-PAGE. Reverse-phase HPLC analysis revealed a single active fraction eluted at 12.94 min, and MALDI-TOF mass spectrometry analysis showed the molecular mass to be 9.244 kDa. This molecular mass does not correspond to previously described streptococcal bacteriocins. The purified bacteriocin was named phocaecin PI80 from its producer strain, as this is the first report of bacteriocin production by Streptococcus phocae. The bacteriocin exhibited a broad spectrum of activity and inhibited important pathogens: Listeria monocytogenes, Vibrio parahaemolyticus, and V. fischeri. The antibacterial substance was also sensitive to proteolytic enzymes: trypsin, protease, pepsin, and chymotrypsin, yet insensitive to catalase, peroxidase, and diastase, confirming that the inhibition was due to a proteinaceous molecule (i.e., the bacteriocin), and not due to hydrogen peroxide or diacetyl. Phocaecin PI80 moderately tolerated heat treatment (up to $70^{\circ}C$ for 10 min) and resisted certain solvents (acetone, ethanol, and butanol). A massive leakage of $K^+$ ions from E. coli $DH5\alpha$, L. monocytogenes, and V. parahaemolyticus was induced by phocaecin PI80, as measured by Inductively Coupled Plasma Optical Emission Spectrometry (ICPOES). Therefore, the results of this study show that phocaecin PI80 may be a useful tool for inhibiting L. monocytogenes in seafood products that do not usually undergo adequate heat treatment, whereas the cells of Streptococcus phocae PI80 could be used to control vibriosis in shrimp farming.