Hak Jun Kim

Prof. Hak Jun Kim

Department of Chemistry, Pukyong National University, Busan, Republic of Korea
orcid

Research Focus & Metrics

Academic Career Length

13Years (2014-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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27 January 2017 in Marine Drugs
Verified
Journal Article
Open access
PDF file
Hak Jun KimHak Jun Kim
Hak Jun Kim
JLJun Hyuck Lee
Jun Hyuck Lee
YHYoung Baek Hur
Young Baek Hur
CLChangwoo Lee
Changwoo Lee
SPSun-Ha Park
Sun-Ha Park
BKBon-Won Koo
Bon-Won Koo
Antifreeze proteins (AFPs) are biological antifreezes with unique properties, including thermal hysteresis(TH),ice recrystallization inhibition(IRI),and interaction with membranes and/or membrane proteins. These properties have been utilized in the preservation of biological samples at low temperatures. Here, we review the structure and function of marine-derived AFPs, including moderately active fish AFPs and hyperactive polar AFPs. We also survey previous and current reports of cryopreservation using AFPs. Cryopreserved biological samples are relatively diverse ranging from diatoms and reproductive cells to embryos and organs. Cryopreserved biological samples mainly originate from mammals. Most cryopreservation trials using marine-derived AFPs have demonstrated that addition of AFPs can improve post-thaw viability regardless of freezing method (slow-freezing or vitrification), storage temperature, and types of biological sample type.

4 February 2019 in ChemistrySelect
Verified
Journal Article
Closed access
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SNSondavid K. Nandanwar
Sondavid K. Nandanwar
Hak Jun KimHak Jun Kim
Hak Jun Kim

13 August 2018 in Applied Sciences
Verified
Journal Article
Open access
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SUSelvakumari Ulagesan
Selvakumari Ulagesan
Hak Jun KimHak Jun Kim
Hak Jun Kim
Snails have been used both as a food and as a treatment for a variety of medicinal conditions. In this study, seven different snail proteins were evaluated for their antimicrobial activity. Fresh water and land snails of seven different live species were collected and identified. Crude proteins were extracted from seven different snails. The extracted proteins were estimated using Bradford’s method and snail proteins were displayed using a sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The seven different snail proteins were evaluated for their antimicrobial activity against various pathogenic bacterial and fungal cultures by agar well diffusion method and MIC (Minimum Inhibitory Concentration). One of the most active, crude proteins was from land snail Cryptozona bistrialis and its protein was capable of completely inhibiting the development of pathogenic bacterial and fungal cultures. This study shows that the land snail C. bistrialis proteins could be used as an antibiotic in biomedical research.

8 March 2014 in Marine Biotechnology
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Journal Article
Closed access
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WJWoongsic Jung
Woongsic Jung
YGYunho Gwak
Yunho Gwak
PDPeter L. Davies
Peter L. Davies
Hak Jun KimHak Jun Kim
Hak Jun Kim
EJEonSeon Jin
EonSeon Jin

1 December 2014 in Process Biochemistry
Verified
Journal Article
Closed access
YLYong-Xin Li
Yong-Xin Li
SHS.W.A. Himaya
S.W.A. Himaya
PDPradeep Dewapriya
Pradeep Dewapriya
Hak Jun KimHak Jun Kim
Hak Jun Kim
Se-Kwon KimSe-Kwon Kim
Se-Kwon Kim

17 November 2020 in Applied Sciences
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Journal Article
Open access
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SNSondavid Nandanwar
Sondavid Nandanwar
SBShweta Borkar
Shweta Borkar
JLJun Hyuck Lee
Jun Hyuck Lee
Hak Jun KimHak Jun Kim
Hak Jun Kim
Cold-active enzymes increase their catalytic efficiency at low-temperature, introducing structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied by lower thermal stability. These characteristics have made cold-active enzymes into attractive targets for the industrial applications, since they could reduce the energy cost in the reaction, attenuate side-reactions, and simply be inactivated. In addition, the increased structural flexibility could result in broad substrate specificity for various non-native substrates, which is called substrate promiscuity. In this perspective, we deal with a less addressed aspect of cold-active enzymes, substrate promiscuity, which has enormous potential for semi-synthesis or enzymatic modification of fine chemicals and drugs. Further structural and directed-evolutional studies on substrate promiscuity of cold-active enzymes will provide a new workhorse in white biotechnology.